WO2019238761A1 - Water soluble multilayer films containing wash active chemicals and enzymes - Google Patents
Water soluble multilayer films containing wash active chemicals and enzymes Download PDFInfo
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- WO2019238761A1 WO2019238761A1 PCT/EP2019/065359 EP2019065359W WO2019238761A1 WO 2019238761 A1 WO2019238761 A1 WO 2019238761A1 EP 2019065359 W EP2019065359 W EP 2019065359W WO 2019238761 A1 WO2019238761 A1 WO 2019238761A1
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- 150000002576 ketones Chemical class 0.000 description 1
- 238000007759 kiss coating Methods 0.000 description 1
- 150000003951 lactams Chemical class 0.000 description 1
- 229940116108 lactase Drugs 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 238000007644 letterpress printing Methods 0.000 description 1
- 235000018977 lysine Nutrition 0.000 description 1
- VTHJTEIRLNZDEV-UHFFFAOYSA-L magnesium dihydroxide Chemical compound [OH-].[OH-].[Mg+2] VTHJTEIRLNZDEV-UHFFFAOYSA-L 0.000 description 1
- 239000000347 magnesium hydroxide Substances 0.000 description 1
- 235000012254 magnesium hydroxide Nutrition 0.000 description 1
- 229910001862 magnesium hydroxide Inorganic materials 0.000 description 1
- 229940035034 maltodextrin Drugs 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 230000007246 mechanism Effects 0.000 description 1
- 239000000155 melt Substances 0.000 description 1
- 239000002207 metabolite Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 108010009355 microbial metalloproteinases Proteins 0.000 description 1
- 235000011929 mousse Nutrition 0.000 description 1
- 231100000350 mutagenesis Toxicity 0.000 description 1
- QYZFTMMPKCOTAN-UHFFFAOYSA-N n-[2-(2-hydroxyethylamino)ethyl]-2-[[1-[2-(2-hydroxyethylamino)ethylamino]-2-methyl-1-oxopropan-2-yl]diazenyl]-2-methylpropanamide Chemical compound OCCNCCNC(=O)C(C)(C)N=NC(C)(C)C(=O)NCCNCCO QYZFTMMPKCOTAN-UHFFFAOYSA-N 0.000 description 1
- GORGQKRVQGXVEB-UHFFFAOYSA-N n-ethenyl-n-ethylacetamide Chemical compound CCN(C=C)C(C)=O GORGQKRVQGXVEB-UHFFFAOYSA-N 0.000 description 1
- PNLUGRYDUHRLOF-UHFFFAOYSA-N n-ethenyl-n-methylacetamide Chemical compound C=CN(C)C(C)=O PNLUGRYDUHRLOF-UHFFFAOYSA-N 0.000 description 1
- OFESGEKAXKKFQT-UHFFFAOYSA-N n-ethenyl-n-methylformamide Chemical compound C=CN(C)C=O OFESGEKAXKKFQT-UHFFFAOYSA-N 0.000 description 1
- DSENQNLOVPYEKP-UHFFFAOYSA-N n-ethenyl-n-methylpropanamide Chemical compound CCC(=O)N(C)C=C DSENQNLOVPYEKP-UHFFFAOYSA-N 0.000 description 1
- HAZULKRCTMKQAS-UHFFFAOYSA-N n-ethenylbutanamide Chemical compound CCCC(=O)NC=C HAZULKRCTMKQAS-UHFFFAOYSA-N 0.000 description 1
- IUWVWLRMZQHYHL-UHFFFAOYSA-N n-ethenylpropanamide Chemical compound CCC(=O)NC=C IUWVWLRMZQHYHL-UHFFFAOYSA-N 0.000 description 1
- SLCVBVWXLSEKPL-UHFFFAOYSA-N neopentyl glycol Chemical compound OCC(C)(C)CO SLCVBVWXLSEKPL-UHFFFAOYSA-N 0.000 description 1
- 150000002826 nitrites Chemical class 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- SNQQPOLDUKLAAF-UHFFFAOYSA-N nonylphenol Chemical compound CCCCCCCCCC1=CC=CC=C1O SNQQPOLDUKLAAF-UHFFFAOYSA-N 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 238000007645 offset printing Methods 0.000 description 1
- 229940055577 oleyl alcohol Drugs 0.000 description 1
- XMLQWXUVTXCDDL-UHFFFAOYSA-N oleyl alcohol Natural products CCCCCCC=CCCCCCCCCCCO XMLQWXUVTXCDDL-UHFFFAOYSA-N 0.000 description 1
- 229920001542 oligosaccharide Polymers 0.000 description 1
- 150000002482 oligosaccharides Chemical class 0.000 description 1
- LVZSQWIWCANHPF-UHFFFAOYSA-N p-nitrophenyl palmitate Chemical compound CCCCCCCCCCCCCCCC(=O)OC1=CC=C([N+]([O-])=O)C=C1 LVZSQWIWCANHPF-UHFFFAOYSA-N 0.000 description 1
- 238000007649 pad printing Methods 0.000 description 1
- 238000002888 pairwise sequence alignment Methods 0.000 description 1
- 108090000155 pancreatic elastase II Proteins 0.000 description 1
- 239000001814 pectin Substances 0.000 description 1
- 229920001277 pectin Polymers 0.000 description 1
- 235000010987 pectin Nutrition 0.000 description 1
- 150000004965 peroxy acids Chemical class 0.000 description 1
- ACVYVLVWPXVTIT-UHFFFAOYSA-N phosphinic acid Chemical class O[PH2]=O ACVYVLVWPXVTIT-UHFFFAOYSA-N 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 150000003018 phosphorus compounds Chemical class 0.000 description 1
- 238000005375 photometry Methods 0.000 description 1
- 230000000704 physical effect Effects 0.000 description 1
- 229940085127 phytase Drugs 0.000 description 1
- 229940012957 plasmin Drugs 0.000 description 1
- 229920002006 poly(N-vinylimidazole) polymer Polymers 0.000 description 1
- 229920000233 poly(alkylene oxides) Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920005906 polyester polyol Polymers 0.000 description 1
- 229920000151 polyglycol Polymers 0.000 description 1
- 239000010695 polyglycol Substances 0.000 description 1
- 229940051841 polyoxyethylene ether Drugs 0.000 description 1
- XAEFZNCEHLXOMS-UHFFFAOYSA-M potassium benzoate Chemical compound [K+].[O-]C(=O)C1=CC=CC=C1 XAEFZNCEHLXOMS-UHFFFAOYSA-M 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000003825 pressing Methods 0.000 description 1
- 150000003140 primary amides Chemical class 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 125000001500 prolyl group Chemical group [H]N1C([H])(C(=O)[*])C([H])([H])C([H])([H])C1([H])[H] 0.000 description 1
- 230000002633 protecting effect Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000017854 proteolysis Effects 0.000 description 1
- 230000006337 proteolytic cleavage Effects 0.000 description 1
- 238000004080 punching Methods 0.000 description 1
- JUJWROOIHBZHMG-UHFFFAOYSA-N pyridine Substances C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 1
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 1
- 229920005604 random copolymer Polymers 0.000 description 1
- 230000035484 reaction time Effects 0.000 description 1
- 230000001105 regulatory effect Effects 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 238000007763 reverse roll coating Methods 0.000 description 1
- 238000012552 review Methods 0.000 description 1
- 238000007142 ring opening reaction Methods 0.000 description 1
- 125000006413 ring segment Chemical group 0.000 description 1
- 102220224495 rs1060503668 Human genes 0.000 description 1
- 238000007650 screen-printing Methods 0.000 description 1
- 210000002374 sebum Anatomy 0.000 description 1
- 150000003335 secondary amines Chemical class 0.000 description 1
- 238000007767 slide coating Methods 0.000 description 1
- 238000007764 slot die coating Methods 0.000 description 1
- 229910001379 sodium hypophosphite Inorganic materials 0.000 description 1
- 239000000600 sorbitol Substances 0.000 description 1
- 235000012424 soybean oil Nutrition 0.000 description 1
- 239000003549 soybean oil Substances 0.000 description 1
- 238000004528 spin coating Methods 0.000 description 1
- 238000001694 spray drying Methods 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 239000010935 stainless steel Substances 0.000 description 1
- 229910001220 stainless steel Inorganic materials 0.000 description 1
- 238000004659 sterilization and disinfection Methods 0.000 description 1
- 235000000346 sugar Nutrition 0.000 description 1
- 150000008163 sugars Chemical class 0.000 description 1
- LSNNMFCWUKXFEE-UHFFFAOYSA-L sulfite Chemical class [O-]S([O-])=O LSNNMFCWUKXFEE-UHFFFAOYSA-L 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-M sulfonate Chemical compound [O-]S(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-M 0.000 description 1
- 229910052717 sulfur Inorganic materials 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- RVUXIPACAZKWHU-UHFFFAOYSA-N sulfuric acid;heptahydrate Chemical compound O.O.O.O.O.O.O.OS(O)(=O)=O RVUXIPACAZKWHU-UHFFFAOYSA-N 0.000 description 1
- 239000000454 talc Substances 0.000 description 1
- 229910052623 talc Inorganic materials 0.000 description 1
- 239000003760 tallow Substances 0.000 description 1
- 238000010345 tape casting Methods 0.000 description 1
- 229920001897 terpolymer Polymers 0.000 description 1
- KQYLUTYUZIVHND-UHFFFAOYSA-N tert-butyl 2,2-dimethyloctaneperoxoate Chemical compound CCCCCCC(C)(C)C(=O)OOC(C)(C)C KQYLUTYUZIVHND-UHFFFAOYSA-N 0.000 description 1
- OPQYOFWUFGEMRZ-UHFFFAOYSA-N tert-butyl 2,2-dimethylpropaneperoxoate Chemical compound CC(C)(C)OOC(=O)C(C)(C)C OPQYOFWUFGEMRZ-UHFFFAOYSA-N 0.000 description 1
- ISIJQEHRDSCQIU-UHFFFAOYSA-N tert-butyl 2,7-diazaspiro[4.5]decane-7-carboxylate Chemical compound C1N(C(=O)OC(C)(C)C)CCCC11CNCC1 ISIJQEHRDSCQIU-UHFFFAOYSA-N 0.000 description 1
- WYKYCHHWIJXDAO-UHFFFAOYSA-N tert-butyl 2-ethylhexaneperoxoate Chemical compound CCCCC(CC)C(=O)OOC(C)(C)C WYKYCHHWIJXDAO-UHFFFAOYSA-N 0.000 description 1
- GJBRNHKUVLOCEB-UHFFFAOYSA-N tert-butyl benzenecarboperoxoate Chemical compound CC(C)(C)OOC(=O)C1=CC=CC=C1 GJBRNHKUVLOCEB-UHFFFAOYSA-N 0.000 description 1
- BWSZXUOMATYHHI-UHFFFAOYSA-N tert-butyl octaneperoxoate Chemical compound CCCCCCCC(=O)OOC(C)(C)C BWSZXUOMATYHHI-UHFFFAOYSA-N 0.000 description 1
- 108010031354 thermitase Proteins 0.000 description 1
- 239000010409 thin film Substances 0.000 description 1
- 150000004764 thiosulfuric acid derivatives Chemical class 0.000 description 1
- 125000000341 threoninyl group Chemical group [H]OC([H])(C([H])([H])[H])C([H])(N([H])[H])C(*)=O 0.000 description 1
- 229960004072 thrombin Drugs 0.000 description 1
- 230000007704 transition Effects 0.000 description 1
- ZIBGPFATKBEMQZ-UHFFFAOYSA-N triethylene glycol Chemical compound OCCOCCOCCO ZIBGPFATKBEMQZ-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
- 230000001810 trypsinlike Effects 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 239000007762 w/o emulsion Substances 0.000 description 1
- 239000001993 wax Substances 0.000 description 1
- 108010062040 wax-ester hydrolase Proteins 0.000 description 1
- 238000004804 winding Methods 0.000 description 1
- 229920001285 xanthan gum Polymers 0.000 description 1
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
- C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
- C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
- C11D17/042—Water soluble or water disintegrable containers or substrates containing cleaning compositions or additives for cleaning compositions
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B32—LAYERED PRODUCTS
- B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
- B32B27/00—Layered products comprising a layer of synthetic resin
- B32B27/18—Layered products comprising a layer of synthetic resin characterised by the use of special additives
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B32—LAYERED PRODUCTS
- B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
- B32B27/00—Layered products comprising a layer of synthetic resin
- B32B27/30—Layered products comprising a layer of synthetic resin comprising vinyl (co)polymers; comprising acrylic (co)polymers
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38681—Chemically modified or immobilised enzymes
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B32—LAYERED PRODUCTS
- B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
- B32B2250/00—Layers arrangement
- B32B2250/24—All layers being polymeric
- B32B2250/246—All polymers belonging to those covered by groups B32B27/32 and B32B27/30
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B32—LAYERED PRODUCTS
- B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
- B32B2307/00—Properties of the layers or laminate
- B32B2307/70—Other properties
- B32B2307/716—Degradable
- B32B2307/7166—Water-soluble, water-dispersible
-
- B—PERFORMING OPERATIONS; TRANSPORTING
- B32—LAYERED PRODUCTS
- B32B—LAYERED PRODUCTS, i.e. PRODUCTS BUILT-UP OF STRATA OF FLAT OR NON-FLAT, e.g. CELLULAR OR HONEYCOMB, FORM
- B32B2432/00—Cleaning articles, e.g. mops or wipes
Definitions
- the present invention relates to water soluble multilayer films containing wash active chemicals and enzymes, their production and use.
- Multilayer films for example wash active films, as described for example in unpublished patent applications PCT/EP2017/083133 and PCT/EP2017/083127, usually comprise acidic compo- nents (as mentioned in US 20160369210 A1 ).
- wash active films described in the above publications due to their acidic nature, offer an environment which is not suitable for enzyme integration into such films.
- laundry products usually comprise enzymes, in order to enhance washing perfor- mance.
- laundry products have to withstand considerable storage periods (for example when a laundry product is stored in a supermarket, and subsequently in the home of a consumer), under variable storage conditions, for example varying temperatures and humidities.
- WO2013/148492 Use of enzymes for preparing water-soluble films, enzymes+polyol for preparation of water soluble film containing PVA, PEO, glycerol, MPG, CaCh, protease; film used for unit dose products
- W014152547 Detergent pouch with enzymatic water-soluble film, enzyme in the film is different from enzyme in the detergent (protease or lipase in film); architecture of pouch film, compartments and ingredients; several layers are described having or not having enzyme for pro tecting enzyme from detergent
- W014186464 Stabilized Lipase in water soluble aims, water-soluble film containing lipase (sequence claimed); lipase in in solid, particulate form; film comprises 35-90% PVA with 75-99% degree of hydrolysis and 10-50% polyols; use of film for preparing a detergent unit dose product
- a multilayer film for example a wash active multilayer film
- incorporation of two or more enzymes into a multilayer film may present additional challenges, since some enzymes are incompatible with each other.
- protease in case of using protease and at least one different enzyme, such as amylase, it becomes necessary to include a protease inhibitor in order to prevent rapid decomposition of the different enzyme, (see EP2799533, W014152674) This may hold true also in case of protease alone, which also decomposes itself, in the presence of water, in particular at relatively high mass fractions of protease.
- protease inhibitors inhibit protease’s proteolytic activity, such that protease is prevented from decomposing proteins, like for example other enzymes (and itself).
- Common protease inhibitors include boron-containing compounds. Suitable boron-containing compounds are selected from boric acid or its derivatives and from boronic acid or its derivatives such as aryl boronic acids or its derivatives, from salts thereof, and from mixtures thereof. Furthermore, peptide aldehydes like di-, tri- or tetrapeptide aldehydes or aldehyde analogues may also be used to inhibit protease.
- protease inhibitors for example boron-containing compounds as mentioned above, lead to environmental stress and are costly.
- an object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage.
- Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least two enzymes, preferably two en zymes incompatible with each other, wherein the enzymes should be stable on storage.
- Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing protease and at least one further enzyme, wherein the enzymes should be stable on storage.
- Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing protease and at least one further enzyme, wherein the enzymes should be stable on storage, and wherein it is possible to refrain from using a protease inhibitor.
- an object of the present invention was to provide a water- soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage, and wherein at least one of the films would be wash active in itself (so that additional cost and environmental stress by adding another wash-active layer can be avoided).
- Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage and wherein the washing and/or cleaning performance should be at least stable compared to a comparable wash and cleaning active multilayer film without any enzyme, preferably improved compared to a comparable wash and cleaning active multilayer film without any enzyme.
- Another object of the present invention was to provide a process for manufacturing a water- soluble multilayer film, preferably a wash and cleaning active multilayer film, as described above and below.
- the newly found multilayer concept allows for the separation of incompatible en zymes from each other, for example separation of protease and enzymes that suffer under the presence of protease, such as lipase, into at least two discrete layers, making protease inhibi tors unnecessary.
- At least two enzymes incompatible with each other are incorporated into two discrete layers, and in addition, the two discrete layers are spatially separated by a fur ther layer devoid of any enzyme.
- the term“polymer film” refers to a flat structure which has an essentially two-dimensional extension.
- the thickness of the films according to the inven tion is preferably 0.5 pm to 20 mm, particularly preferably 1 pm to 10 mm.
- the thickness of the polymer films of the invention is small in relation to the length and width.
- the thick ness of the polymer films is smaller by a factor of at least 2, more preferably of at least 5 and especially of at least 10 than the length of the greatest longitudinal axis.
- the thickness of the polymer films is smaller by a factor of at least 20, more specifically at least 50, even more specifically at least 100 and very specifically at least 500 than the length of the greatest longitudinal axis.
- the upper value for the greatest longitudinal extent of the polymer films of the invention is uncritical.
- the polymer films of the invention can be pro-losed, for example, in the form of film rolls, where the greatest length may even be in the region of 100 m or higher.
- the polymer films of the invention can be in form of single layer films or multilayer films.
- multi-layered film in connection with the present invention defines a self-supporting planar construction which comprises at least two film layers.
- a multi-layered film according to the present invention is a film composite which comprises at least two films which are perma- nently connected with a substantial part of their surface over its entire surface. Thereby, it is understood that at least two films are permanently connected with at least 50% of their surface over its entire surface. If two films of different sizes are connected to each other, at least the film with the smaller surface is permanently connected over its entire surface to at least 50% of its surface.
- the multi-layered films used in the process of the present invention differ from films used for the production of water-soluble container known in the art in which a single film or two or more films are connected by means of a seal seam. Those films known in the art are only connected over their entire surfaces to not more than 50% of their surfaces.
- the thickness of enzyme containing layers is usually below that of today’s single layer PVA films. Due to this reduced enzyme formulation space, the enzyme concentration in the film needs to be higher compared to state of the art. Approaches as described by Monosol/Novozymes, e. g. in W013/148492 or W014/186464, cause additional challenges to enzyme stability.
- the resulting enzyme containing wash active multilayer films shows better wash performance than enzyme containing PVOH films according to the state of the art, due to the additional wash active polymers which could not be formulated into the liquid detergent up to now (e.g. poly acrylic acid).
- the present invention is directed at a water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1) obtainable by physical blending of at least one polymer P1 ') obtainable by by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A‘) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, and at least one polyether component PE), or by free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically unsaturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic acids and mixtures
- homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
- homo- and copolymers comprising at least one copolymerized monomer selected from N- vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, salts of the three latter monomers, vinylpyridine N-oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof, homo- and copolymers of acrylic acid and/or methacrylic acid, especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
- copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least one copoly- merized hydrophobic monomer selected from C-i-Cs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
- copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C2-C8 olefin,
- polyalkylene glycols mono- or diethers of polyalkylene glycols
- multifunctional alkoxylated diamines preferably alkoxylated diamines with 2 to 10 methylene groups
- cellulose derivatives preferably cellulose ethers, cellulose esters, carboxyalkyl celluloses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
- amphoteric modified starch and mixtures thereof,
- At least two of the layers preferably two of the layers, comprise at least one type of enzyme EN) each.
- the film comprises at least one layer comprising or consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
- the polymer P1’) can be prepared by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A‘) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, optionally at least one monomer B’) which is selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, unsaturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures thereof, and
- Monomer composition M’ Monomer A’):
- the monomer composition M’) used for producing the polymer P1’) comprises at least one monomer A’) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
- the monomer composition M’) consists only of a,b-ethylenically un- saturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
- the a,b-ethylenically unsaturated carboxylic acid is preferably selected from acrylic acid, meth- acrylic acid, ethacrylic acid, maleic acid, fumaric acid, itaconic acid, a-chloroacrylic acid, croton- ic acid, citraconic acid, mesaconic acid, glutaconic acid and aconitic acid.
- Suitable salts of the aforementioned acids are, in particular, the sodium, potassium and ammonium salts, and the salts with amines.
- the monomers A’) can be used as such or as mixtures with one another. The stated weight fractions all refer to the acid form.
- the at least one a,b-ethylenically unsaturated carboxylic acid is used for the polymerization in non-neutralized form. If the a,b-ethylenically unsaturated carboxylic acids are used for the polymerization in partially neutralized form, then the acid groups are neutralized preferably to at most 50 mol%, particularly preferably to at most 30 mol%.
- the monomer A’ is selected from acrylic acid, methacrylic acid, maleic acid, fumaric acid, itaconic acid, salts of the aforementioned carboxylic acids and mixtures thereof.
- the monomer A’ is selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid and mixtures thereof.
- the monomer A’ is used preferably in an amount of from 50 to 100% by weight, particularly preferably 60 to 100% by weight, based on the total weight of the monomer composition M’).
- the monomer composition M’ consists to at least 50% by weight, preferably to at least 80% by weight, in particular to at least 90% by weight, based on the total weight of the monomer composition M’), of acrylic acid and/or acrylic acid salts.
- the monomer composition M’) can comprise, in addition to the monomers A’), at least one monomer B’) which is selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, unsaturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures there of.
- the monomer B’) is preferably selected from 2-acrylamido-2-methylpropanesulfonic acid, vinyl- sulfonic acid, allylsulfonic acid, sulfoethyl acrylate, sulfoethyl methacrylate, sulfopropyl acrylate, sulfopropyl methacrylate, 2-hydroxy-3-acryloxypropylsulfonic acid, 2-hydroxy-3- methacryloxypropylsulfonic acid, styrenesulfonic acid, vinylphosphonic acid, allylphosphonic acid, salts of the aforementioned acids, and mixtures thereof.
- Suitable salts of the aforementioned acids are in particular the sodium, potassium and ammoni um salts, and the salts with amines.
- the monomers B’) can be used as such or as mixtures with one another.
- the stated weight fractions all refer to the acid form.
- the monomer composition M’) then consists to at least 50% by weight, particularly preferably to at least 80% by weight, in particular to at least 90% by weight, based on the total weight of the monomer composition M’), of monomers A’) and B’). If the monomer composition M’) comprises at least one monomer B’), then this is used preferably in an amount of from 0.1 to 50% by weight, particularly preferably 1 to 25% by weight, based on the total weight of the monomer composition M’).
- the monomer composition M’) can additionally comprise at least one further monomer different from the monomers containing acid groups and salts thereof.
- the monomer composition M’) additionally comprises at least one comonomer C’) selected from
- x is 0, 1 or 2
- k and I independently of one another, are an integer from 0 to 100, where the sum of k and I is at least 2, preferably at least 5,
- R 1 is hydrogen or methyl
- R 2 is hydrogen, C1-C4-alkyl
- the monomer composition M’) can comprise the further monomers C1’) to C3’) in each case preferably in an amount of from 0 to 30% by weight, particularly preferably 0 to 20% by weight, in particular 0 to 10% by weight, based on the total weight of the monomer composition M’). If the monomer composition M’) comprises at least one monomer selected from C1’) to C3’), then in each case preferably in an amount of from 0.1 to 30% by weight, particularly preferably 1 to 20% by weight, in particular 1.5 to 10% by weight, based on the total weight of the monomer composition M’). In a specific embodiment, the monomer composition M’) comprises no further comonomers apart from the monomers A’).
- Preferred nitrogen heterocycles with a free-radically polymerizable a,b-ethylenically unsaturated double bond C1’) are selected from 1-vinylimidazole (N-vinylimidazole), vinyl- and allyl-substitu- ted nitrogen heterocycles different from 1 -vinylimidazole, and mixtures thereof.
- Suitable monomers C1’) are also the compounds obtained by protonation or quaternization of 1 - vinylimidazole and vinyl- and allyl-substituted nitrogen heterocycles different therefrom.
- Acids suitable for the protonation are e.g. carboxylic acids, such as lactic acid, or mineral acids, such as phosphoric acid, sulfuric acid and hydrochloric acid.
- Alkylating agents suitable for the quaternization are Ci-C4-alkyl halides or di(Ci-C4-alkyl) sulfates, such as ethyl chloride, ethyl bromide, methyl chloride, methyl bromide, dimethyl sulfate and diethyl sulfate.
- a protonation or quaternization can generally take place either before or after the polymerization.
- a protonation or quaternization takes place after the polymerization.
- Examples of such charged monomers C1’) are quaternized vinylimidazoles, in particular 3-methyl-1 -vinylimidazolium chloride, methosulfate and ethosulfate.
- Preferred monomers C1’) are furthermore vinyl- and allyl-substituted nitrogen heterocycles different from vinylimidazoles selected from 2-vinylpyridine, 4-vinylpyridine, 2-allylpyridine, 4-allyl- pyridine and the salts thereof obtained by protonation or by quaternization.
- the monomer composition M’) comprises at least one comonomer C1’) selected from 1-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, 2-allylpyridine, 4-allylpyridine and the salts thereof obtained by protonation or by quaternization.
- the monomer composition M’) comprises 1 -vinylimidazole as comonomer C1’).
- Suitable amide-group-containing monomers C2’ are compounds of the general formula (II)
- R 3 and R 4 together with the amide group to which they are bonded, can also be a lactam having 5 to 8 ring atoms,
- R 4 and R 5 together with the nitrogen atom to which they are bonded, can also be a five- to seven-membered heterocycle.
- the monomers C2’) are selected from primary amides of a,b-ethylenically unsaturat ed monocarboxylic acids, N-vinylamides of saturated monocarboxylic acids, N-vinyllactams, N-alkyl- and N,N-dialkylamides, a,b-ethylenically unsaturated monocarboxylic acids and mixtures thereof.
- Preferred monomers C2’ are N-vinyllactams and derivatives thereof, which can have, e.g., one or more C1-C6-alkyl substituents, such as methyl, ethyl, n-propyl, isopropyl, n-butyl, sec-butyl, tert-butyl, etc.
- N-vinylpyrrolidone N-vinylpiperidone, N-vinylcaprolactam
- N-vinyl-5-methyl-2-pyrrolidone N-vinyl-5-ethyl-2-pyrrolidone
- N-vinyl-6-methyl-2-piperidone N-vinyl-6-ethyl-2-piperidone
- N-vinyl-7-methyl-2 -caprolactam N-vinyl-7-ethyl-2-caprolactam.
- N-vinylpyrrolidone and/or N-vinylcaprolactam are particularly preferred.
- Suitable monomers C2’) are furthermore acrylamide and methacrylamide.
- N-Alkyl- and N,N-dialkylamides of a,b-ethylenically unsaturated monocarboxylic acids suitable as monomers C2’) are, for example, methyl(meth)acrylamide, methylethacrylamide, ethyl(meth)acrylamide, ethylethacrylamide, n-propyl(meth)acrylamide, isopropyl(meth)acryl- amide, n-butyl(meth)acrylamide, tert-butyl(meth)acrylamide, tert-butylethacrylamide, and mixtures thereof.
- Open-chain N-vinylamide compounds suitable as monomers C2’ are, for example, N-vinylfor- mamide, N-vinyl-N-methylformamide, N-vinylacetamide, N-vinyl-N-methylacetamide, N-vinyl-N- ethylacetamide, N-vinylpropionamide, N-vinyl-N-methylpropionamide, N-vinylbutyramide and mixtures thereof. Preference is given to using N-vinylformamide.
- the monomer composition M’) can additionally comprise at least one monomer C3’) selected from compounds of the general formulae (I. a) and (l.b), as defined above.
- k is preferably an integer from 1 to 100, particularly preferably 2 to 50, in particular 3 to 30.
- I is an integer from 0 to 50.
- R 2 in the formulae I. a) and l.b) is hydrogen, methyl, ethyl, n-propyl, isopropyl, n- butyl, sec-butyl or tert-butyl.
- x is preferably 1 or 2.
- the polymer P1’ comprises less than 15% by weight, preferably less than 10% by weight, polymerized units of monomers different from monomers A’).
- the polymer P1’) is essentially uncrosslinked.
- the monomer composition M’) used for producing the polymer P1’) thus comprises in particular no added crosslinking monomers.
- crosslinking monomers are compounds with two or more than two polymerizable ethylenically unsaturated double bonds per molecule.
- the monomer composition M’ comprises, based on the total weight, less than 0.5% by weight, even more specifically less than 0.1 % by weight, of crosslinking monomers which have two or more than two free-radical ly polymerizable a,b-ethylenically unsaturated double bonds per molecule.
- the monomer composition M’ comprises no crosslinking monomers having two or more than two polymerizable a,b-ethylenically unsaturated double bonds per molecule.
- the polymer P1’ can be prepared by free-radical polymerization of a monomer composition M’). It is possible to work by any known free-radical polymerization process. In addition to polymerization in bulk, mention should be made especially of the processes of solution polymerization and emulsion polymerization, preference being given to solution polymerization.
- the polymerization is preferably performed in water as a solvent. However, it can also be undertaken in alcoholic solvents, especially Ci-C4-alcohols, such as methanol, ethanol and isopropanol, or mixtures of these solvents with water.
- alcoholic solvents especially Ci-C4-alcohols, such as methanol, ethanol and isopropanol, or mixtures of these solvents with water.
- the free-radical polymerization of the monomer composition M’) is preferably carried out in the feed procedure.
- at least the monomers are metered into the reaction mixture in liquid form.
- Monomers that are liquid under the addition conditions can be introduced into the reaction mixture without adding a solvent. Otherwise the monomers are used as solution in a suitable solvent.
- Suitable polymerization initiators are compounds which decompose thermally, by a redox mechanism or photochemically (photo initiators) to form free radicals.
- thermal initiators having a decomposition temperature in the range from 20 to 180°C, especially from 50 to 90°C.
- suitable thermal initiators are inorganic peroxo compounds such as perox- odisulfates (ammonium peroxodisulfate and preferably sodium peroxodisulfate), peroxosulfates, percarbonates and hydrogen peroxide; organic peroxo compounds such as diacetyl peroxide, di-tert-butyl peroxide, diamyl peroxide, 5-dioctanoyl peroxide, didecanoyl peroxide, dilauroyl peroxide, dibenzoyl peroxide, tert-butyl perneodecanoate, tert-butyl perbenzoate, tert-butyl perisobutyrate, tert-butyl perpivalate, tert-butyl
- initiators can be used in combination with reducing compounds as initiator/regulator sys- tems.
- reducing compounds include phosphorus compounds such as phosphorous acid, hypophosphites and phosphinates, sulfur compounds such as sodium hydrogen- sulfite, sodium sulfite and sodium formaldehyde- sulfoxylate, and hydrazine.
- redox initiator systems which consist of a peroxo compound, a metal salt and a reducing agent.
- peroxo compounds are hydrogen peroxide, peroxodisulfate (as the ammonium, sodium or potassium salt), peroxosulfates, and organic peroxo compounds such as tert-butyl hydroperoxide, cumene hydroperoxide or dibenzoyl per oxide.
- Suitable metal salts are in particular iron(ll) salts such as iron(ll) sulfate heptahydrate.
- Suitable reducing agents are sodium sulfite, the disodium salt of 2-hydroxy-2-sulfinatoacetic acid, the disodium salt of 2-hydroxy-2-sulfonatoacetic acid, sodium hydroxymethanesulfinate, ascorbic acid, isoascorbic acid or mixtures thereof.
- photoinitiators examples include benzophenone, acetophenone, benzyl dialkyl ketones and derivatives thereof.
- thermal initiators preferably inorganic peroxo compounds, espe cially sodium peroxodisulfate.
- the peroxo compounds are advantageously used in combination with sulfur-containing reducing agents, especially sodium hydrogensulfite, as the redox initiator system.
- sulfur-containing reducing agents especially sodium hydrogensulfite
- copolymers comprising sulfonate and/or sulfate as end groups are obtained, which are notable for exceptional cleaning power and scale- inhibiting action.
- phosphorus-containing regulator systems for example sodium hypophosphite and phosphinates.
- initiator/regulator system should be matched to the substances used in each case. If, for example, the peroxodisulfate/ hydrogensulfite system is used, typically 1 to 7% by weight, preferably 2 to 6% by weight, of peroxodisulfate and generally 3 to 25% by weight, preferably 4 to 15% by weight, of hydrogensulfite are used, based in each case on monomer com position M’).
- organic polymerization regulators are sulfur compounds such as mercaptoethanol, 2-ethylhexyl thioglycolate, thioglycolic acid and dodecyl mercaptan.
- sulfur compounds such as mercaptoethanol, 2-ethylhexyl thioglycolate, thioglycolic acid and dodecyl mercaptan.
- the amount thereof is generally 0.1 to 25% by weight, preferably 0.5 to 20% by weight and more preferably 1.0 to 15% by weight, based in each case on monomer composition M’).
- the polymerization temperature is generally 20 to 200°C, preferably 20 to 150°C and more preferably 20 to 120°C.
- the polymerization can be performed under atmospheric pressure, but is preferably undertaken in a closed system under the autogenous pressure which evolves.
- the polymerization can take place in the absence or in the presence of an inert gas.
- the polymerization is carried out in the presence of an inert gas, e.g. nitrogen.
- the weight-average molecular weight Mw of the polymer P1’ can be determined by means of gel permeation chromatography (GPC) in aqueous solution using neutralized polyacrylic acid as polymer standard.
- the polymer P1’) preferably has a weight-average molecular weight of from 1000 to 100 000 g/mol, more preferably 1500 to 50 000 g/mol, in particular 2000 to 20 000 g /mol.
- polymer P1’ has a polydispersity index (PDI) of from 1.2 to 6.0, more preferably 1.4 to 4.0, in particular 1.6 to 3.5.
- PDI polydispersity index
- the polymer P1’) can be obtained in the acidic state, but it can also, if desired be partly neutralized by addition of bases.
- bases are alkali metal hydroxides, like NaOH and KOH, alka line earth metal hydroxides, like Ca(OH)2 and Mg(OH)2, ammonia and amine bases, like mono- ethanol amine.
- bases are alkali metal hydroxides, like NaOH and KOH, alka line earth metal hydroxides, like Ca(OH)2 and Mg(OH)2, ammonia and amine bases, like mono- ethanol amine.
- sodium hydroxide is especially preferred. Neutralization can be performed as early as during the polymerization or after the polymerization has ended.
- step i) for providing the aqueous composition Prior to its use in step i) for providing the aqueous composition, at the most 30 mol% of the car- boxy groups of the polymer P1’) are in the deprotonated form. Preferably, at the most 25 mol%, more preferably at the most 15 mol%, of the carboxy groups of the polymer P1’) are in the deprotonated form. In a special embodiment, the acid groups of the polymer composition according to the invention are present in non-neutralized form.
- the polymer P1’) used in accordance with the invention can be used directly in the form of the aqueous solutions obtained in the course of preparation by means of solvent polymerization, or in dried form (obtained, for example, by spray drying, spray granulation such as fluid bed spray granulation or spouted bed spray granulation, roller drying or freeze drying).
- Suitable polymers P1’) are commercially available or are intermediates of commercially availa ble products.
- a commercially available polyacrylic acid is employed that is not crosslinked and not neutralized or only to a low extend neutralized.
- Suitable products are Sokalan ® CP 10 S, Sokalan ® CP 12 S, Sokalan ® CP 13 S, Sokalan ® PA 25 XS, Sokalan ® PA 80 S and Sokalan ® NR 2530 from BASF SE.
- the monomer composition M1) consists only of a, b-ethylenically un saturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
- the a,b-ethylenically unsaturated carboxylic acid is preferably selected from acrylic acid, meth- acrylic acid, ethacrylic acid maleic acid, fumaric acid, itaconic acid, a-chloroacrylic acid, crotonic acid, citraconic acid, mesaconic acid, glutaconic acid and aconitic acid.
- Suitable salts of the abovementioned acids are, in particular, the sodium, potassium and ammonium salts and the salts with amines or aminoalcohols.
- the monomers A) can be used as such or as mixtures with one another. The stated proportions by weight are all based on the acid form.
- the at least one a, b-ethylenically unsaturated carboxylic acid is preferably used in unneutral ized form for the polymerization. If the a, b-ethylenically unsaturated carboxylic acids are used in partially neutralized form for the polymerization, the acid groups are preferably neutralized to at most 50 mol%, more preferably to at most 30 mol%.
- the monomer A) is particularly preferably selected from acrylic acid, methacrylic acid, maleic acid, fumaric acid, itaconic acid, salts of the abovementioned carboxylic acids and mixtures thereof.
- the monomer A) is selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid and mixtures thereof.
- the monomer A) is preferably used in an amount of 50 to 100 wt .-%, particularly preferably 60 to 100 wt .-%, based on the total weight of the monomer composition M1.
- the monomer composition M1 comprises at least 50% by weight, preferably at least 80% by weight, in particular at least 90% by weight, based on the total weight of the monomer composition M1 ), of acrylic acid and / or acrylic acid salts
- the monomer composition M1) may comprise, in addition to the at least one monomer A), at least one monomer B) selected from olefinically unsaturated sulfonic acids, salts of olefinically unsaturated sulfonic acids, olefinically unsaturated phosphonic acids, salts of olefinically unsaturated phosphonic acids and mixtures thereof.
- the monomer composition M1 ) may comprise, in addition to the monomers A), at least one monomer B selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, un saturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures thereof.
- the monomer B) is preferably selected from 2-acrylamido-2-methylpropane-sulfonic acid, vinyl- sulfonic acid, allylsulfonic acid, sulfoethyl acrylate, sulfoethyl methacrylate, sulfopropyl acrylate, sulfopropyl methacrylate, 2-hydroxy-3-acryloxypropylsulfonic acid, 2-hydroxy-3-methacryloxy- propylsulfonic acid, styrenesulfonic acid, vinylphosphonic acid, allylphosphonic acid, salts of the aforementioned acids and mixtures thereof.
- Preferred monomer B) is 2-acrylamido-2-methylpropanesulfonic acid.
- Suitable salts of the abovementioned acids are in particular the sodium, potassium and ammo nium salts and the salts with amines.
- the monomers B) can be used as such or as mixtures with one another. The stated proportions by weight are all based on the acid form
- the monomer composition M1) additionally comprises at least one comonomer C) selected from
- x is 0, 1 or 2
- k and I are independently an integer from 0 to 100, where the sum of k and I is at least 2, preferably at least 5,
- R 1 is hydrogen or methyl
- R 2 is hydrogen or Ci-C 4 -alkyl, and mixtures of two or more than two of the aforementioned monomers C1 ) to C3).
- the monomer composition M1 based on the total weight, comprises less than 0.1 % by weight, preferably less than 0.05% by weight, especially less than 0.001 % by weight, of crosslinking monomers having two or more than two free-radically polymerizable a,b-ethylenically unsaturated double bonds per molecule.
- the monomer composition M1 does not comprise any crosslinking monomers having two or more than two free-radically polymerizable a,b-ethylenically unsaturated double bonds per molecule.
- the monomer composition M1 ) used for free-radical polymerization comprises or consists of acrylic acid and/or acrylic acid salts.
- the free-radical polymerization of the monomer composition M1 is conducted in the presence of at least one Ce-C-is-alkyl polyoxy- alkylene ether incorporating exclusively ethylene oxide units as alkylene oxide units and/or also in the presence of a polymer.
- the Ce-C-ie-alkyl polyoxyalkylene ethers mentioned above comprise an average of 3 to 10 ethylene oxide units per molecule, preferably an average of 5 to 9 ethylene oxide units per molecule.
- the polymer composition P1) is provided by
- step a) subjecting the monomer composition M1) provided in step a) to a free-radical polymerization in the presence of at least one Ce-Cie-alkyl polyoxyalkylene ether having 3 to 12 alkylene oxide units per molecule and optionally in the presence of at least one additive.
- the free-radical polymerization in step B) is effected in feed mode, wherein at least a portion of the Cs-Cis-alkyl polyoxyalkylene ether having 3 to 12 alkylene oxide units per molecule and optionally, if present, at least a portion of a solvent are initially charged, and at least a portion of the monomer composition M) provided in step a) and at least one free-radical initiator are fed into the initial charge.
- Suitable as polyether component PE are polyetherols having a number average molecular weight of at least 200 g/mol and their mono- and di-(Ci-C 6 -alkyl ethers).
- Suitable polyetherols and their mono- and di-(CrC 6 -alkyl ethers) may be linear or branched, preferably linear.
- Suitable polyetherols and their mono- and di-(C1-C6-alkyl ethers) generally have a number-average molecular weight in the range from about 200 to 100,000, preferably from 300 to 50,000, particularly preferably from 500 to 40,000.
- Suitable polyetherols are, for example, water-soluble or water-dispersible nonionic polymers which comprise alkylene oxide repeat units.
- the proportion of alkylene oxide repeating units is at least 30 % by weight, based on the total weight of the compound.
- Suitable polyetherols are polyalkylene gly cols, such as polyethylene glycols, polypropylene glycols, polytetrahydrofurans and alkylene oxide copolymers.
- Suitable alkylene oxides for the preparation of alkylene oxide copolymers are e.g. ethylene oxide, propylene oxide, epichlorohydrine, 1 ,2- and 2,3-butylene oxide.
- Suitable examples are copolymers of ethylene oxide and propylene oxide, copolymers of ethylene oxide and butylene oxide and copolymers of ethylene oxide, propylene oxide and at least one butylene oxide.
- the alkylene oxide copolymers may comprise randomly distributed alkylene oxide units or in copolymerized form in the form of blocks.
- the proportion of repeating units derived from ethylene oxide is 40 to 99% by weight.
- Particularly preferred as the polyether component PE are ethylene oxide homopolymers and ethylene oxide / propylene oxide copolymers.
- polyether component PE Also suitable as polyether component PE are the mono- and di-(Ci-C 6 -alkyl ethers) of the polyetherols described above. Preference is given to polyalkylene glycol monomethyl ether and pol yalkylene glycol dimethyl ether.
- polyether component PE Also suitable as polyether component PE are polyether-containing surfactants. Generally suit able are nonionic and ionic surfactants which have at least one nonpolar and at least one polar group and which comprise a polyether group.
- the polyether groups-containing surfactants PE are preferably selected from alkylpolyoxy- alkylenether, arylpolyoxyalkylenether, alkylarylpolyoxyalkylenether, alkoxylated animal and/or vegetable fats and/or oils, fatty amine alkoxylates, fatty acid amide alkoxylates, fatty acid dieth- anolamide alkoxylates, polyoxyethylenesorbitan fatty acid esters, alkylpolyethersulfates, ar- ylpolyethersulfates, alkylarylpolyethersulfates, alkylpolyethersulfonates, arylpolyethersulfonates, alkylarylpolyethersulfonates, alkylpolyether phosphateates, aryl polyether phosphates, alkylaryl polyether phosphates, glycerol ether sulfonates, glycerol ether sulfates, monogly
- the preferred nonionic polyether group-containing surfactants PE include, for example:
- Alkyl polyoxyalkylene ethers derived from C3-C6 low molecular weight alcohols or C7-C30 fatty alcohols.
- the ether component may be derived from ethylene oxide units, propylene oxide units, 1 ,2-butylene oxide units, 1 ,4-butylene oxide units, and random copolymers and block copolymers thereof.
- Suitable nonionic surfactants include, inter alia, surfactants of the general formula (VI)
- R 10 is a linear or branched alkyl radical having 6 to 22 C atoms
- R 11 and R 12 independently of one another are hydrogen or a linear or branched alkyl radical having 1 to 10 C atoms or H, wherein R 12 is preferably methyl, and
- x and y are independently 0 to 300.
- fatty alcohol alkoxylates and oxo alcohol alkoxylates such as iso- tridecyl alcohol and oleyl alcohol polyoxyethylene ethers.
- the sequence of the alkylene oxide units is arbitrary, s, t, u and v independently represent an integer from 0 to 500, the sum of s, t, u and v being > 0, R 13 and R 15 independently of one another represent a linear or branched, saturated Ci-C4o-alkyl radical or a mono- or polyunsaturated C 2 -C4o-alkenyl radical, and
- R 14 is selected from methyl, ethyl, n-propyl, isopropyl or n-butyl.
- the sum of s, t, u and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
- t and u are 0.
- the sum of s and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
- R 13 and R 15 are preferably, independently of one another, a linear or branched, saturated C 2 -C3o-alkyl radical.
- R 13 and R 15 may also be mixtures of different alkyl radicals.
- R 14 is preferably methyl or ethyl, in particular methyl.
- a preferred embodiment are hydroxyl-containing surfactants of the general formula
- s and v are independently an integer from 0 to 500, the sum of s and v being > 0, and
- R 13 and R 15 independently of one another represent a linear, saturated Ci-C3o-alkyl radical or a branched, saturated C3-C3o-alkyl radical or mono- or polyunsaturated C2-C3o-alkenyl radical.
- the sum of s and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
- nonionic surfactants include e.g. hydroxy mixed ethers of the general formula (C 6 -22-alkyl)-CH(OH)CH 2 O-(EO)20-i20-(C2-26-alkyl).
- R 16 and R 18 independently of one another represent a linear or branched, saturated Ci-C4o-alkyl radical or a mono- or polyunsaturated C2-C4o-alkenyl radical, and
- R 17 is selected from methyl, ethyl, n-propyl, isopropyl or n-butyl.
- the sum of p and q is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
- R 16 and R 18 independently of one another represent a linear or branched, saturated C 4 -C3o-alkyl radical.
- R 16 and R 18 may also be mixtures of different alkyl radicals.
- R 17 is preferably methyl or ethyl, in particular methyl.
- These include e.g. lauryl alcohol polyoxyethylene acetate. alkylarylalkoholpolyoxyethylenether, e.g. Octylphenol polyoxyethylene ether,
- alkoxylated animal and/or vegetable fats and/or oils e.g. corn oil ethoxylates, castor oil ethoxylates, tallow fat ethoxylates,
- alkyl phenol alkoxylates such as ethoxylated isooctyl-, octyl- or nonylphenol, tributylphe- nol polyoxyethylene ethers,
- fatty amine alkoxylates fatty acid amide- and fatty acid diethanolamide alkoxylates, especially their ethoxylates
- alkylpolyethersulfate sodium dodecylpoly (oxyethylene) sulfate (sodium lauryl ether sulfate, SLES).
- the polyether component PE is selected from Ce-C-ie-alkyl polyoxyalkylene ethers having an average of 3 to 12 alkylene oxide units per molecule.
- the polymer composition P1 may be prepared by free-radical polymerization of the monomer composition M1) in the presence of at least one Cs-C-is-alkyl polyoxyalkylene ether having an average of 3 to 12 alkylene oxide units per molecule. This affords specific polymer compositions P1 ) having advantageous properties. Without being bound to a theory, hydrogen bonds are able to form between the growing polymer and the alkylene oxide units, and these influence the properties of the resultant polymer composition.
- polymer compositions P1) having a high content of the Ce-C-ia-alkyl polyoxyalkylene ether can be attained; these cannot be prepared by mixing the separately prepared polymer with the C 8 -Ci 8 -alkyl polyoxyalkylene ether. Free- radical surfactant degradation advantageously does not take place here.
- the polymer compositions P1 For production of a washing- and cleaning-active multilayer films according to the invention, preference is given to using polymer compositions P1 ) having a low glass transition temperature T G .
- the polymer compositions P1) used for production of the washing- and cleaning- active multilayer films of the invention have a glass transition temperature T G in the range from 0 to 80°C, preferably from 0 to 60°C, especially 0 to 30°C.
- Tg glass transition temperatures described in the context of this application can be determined by means of differential scanning calorimetry (DSC).
- the polymer compositions P1) used for production of the washing- and cleaning-active multilayer films of the invention take the form of a transparent film.
- the multi-layered film further comprises at least one other layer which comprises at least one polymer P2) which is different from polymer composition P1 ) and is selected from
- homo- or copolymers comprising monomer units derivable from vinyl alcohol, vinylesters, alkoxylated vinyl alcohols, or mixtures thereof;
- homo-or copolymers comprising at least one monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinyl-pyridine, salts of N- vinylimidazole, salts of 2-vinylpyridine, salts of 4-vinyl-pyridine, vinylpyridine-N-oxide, N- carboxymethyl-4-vinylpyridine halogenides or mixtures thereof;
- homo- or copolymers of acrylic acid and /or methacrylic acid preferably copolymers corn- prising at least one acrylic acid monomer selected from acrylic acid, salts of acrylic acid or mixtures thereof and at least one maleic acid monomer selected from maleic acid, maleic acid anhydride, salts of maleic acid or mixtures thereof;
- copolymer comprising at least a (meth)acrylic acid monomer selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid or mixtures thereof and at least one hydrophobic monomer selected from CrCs alkylesters of (meth) acrylic acid, C2-
- polyalkyleneglycols mono-or diethers of polyalkyleneglycols
- polyalkyleneoxide such as polyethyleneoxide
- multifunctional alkoxylated diamines preferably alkoxylated diamines with 2 to 10 meth ylene groups, and
- the multi-layered film particularly preferably comprises at least one further layer which compris es at least one polymer P2) or consists of at least one polymer P2) which is selected from Cellulose ethers and cellulose esters,
- the multi-layered film comprises in particular at least one further layer which comprises at least one polymer P2) or consists of at least one polymer P2) selected from cellulose derivatives, preferably carboxyalkylcelluloses and salts thereof, sulfoalkylcelluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkylcelluloses, hydroxyalkylcelluloses, (hydroxyalkyl) alkylcellu- loses and mixtures of two or more of these cellulose derivatives.
- Polysaccharides suitable as polymers P2 are natural polysaccharides, e.g.
- cellulose hemicellu- lose, glycogen, starch (amylose and amylopectin), dextran, pectins, inulin, xanthan, chitin, cal- lose, thermally, hydrolytically or enzymatically degraded starch, e.g. maltodextrin etc
- Preferred modified polysaccharides are e.g. cellulose ethers, cellulose esters, cellulose amides, etc.
- Cellulose ethers are derivatives of cellulose that result from partial or total substitution of the hydrogen atoms in the hydroxy groups of the cellulose. Cellulose ethers from the reaction of cellulose with more than one etherifying agent are also referred to as cellulose mixed ethers.
- Preferred cellulose ethers are selected from alkylcelluloses, hydroxyalkylcelluloses, (hydroxy- alkyl) alkylcelluloses, carboxyalkylcelluloses and salts thereof, (carboxyalkyl) alkylcelluloses and salts thereof, (carboxyalkyl) (hydroxyalkyl) celluloses and salts thereof, (carboxyalkyl) (hydroxy- alkyl) alkylcelluloses and salts thereof, sulfoalkylcelluloses and salts thereof.
- Preferred carboxyalkyl radicals are the carboxymethyl radical and the carboxyethyl radical. Particularly preferred as carboxyalkyl radical is the carboxymethyl radical.
- Preferred as sulfoalkyl radical are the sulfomethyl radical and the sulfoethyl radical. Particularly preferred as sulfoalkyl radical is the sulfomethyl radical.
- Preferred salts are the sodium, potassium, calcium and ammonium salts.
- Particularly preferred cellulose ethers are selected from carboxymethylcellulose, carboxyethyl- cellulose, methylcellulose, ethylcellulose, n-propylcellulose, ethylmethylcellulose, hydroxyethyl- cellulose, hydroxypropylcellulose, hydroxybutylcellulose, hydroxyethylmethylcellulose, hydroxy- propylmethylcellulose, hydroxyethylethylcellulose, hydroxypropylethylcellulose, carboxymethyl- methylcellulose, carboxymethylethylcellulose, carboxymethylhydroxyethylcellulose, carbox- ymethylhydroxyethylmethylcellulose, carboxymethylhydroxyethylethylcellulose, sulfomethylcellu- lose and sulfoethylcellulose.
- the carboxyalkyl radicals and the sulfoalkyl radicals may also be present as salts.
- Cellulose esters are derivatives of cellulose which are formed by esterification of the hydroxy groups with acids.
- Preferred are the sulfuric acid esters of cellulose.
- the sulfuric acid is only subjected to a partial esterification, so that the resulting sulfuric acid es ters still have free acid groups or their salts.
- Particular preferred are sulfuric ester salts of cellulose. These are distinguished by their graying-inhibiting effect.
- Preferred modified polysaccharides are selected from methyl cellulose, ethyl cellulose, propyl cellulose, methyl/ethyl cellulose, ethyl/propyl cellulose, carboxymethyl cellulose, salts of carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, hydroxyethylmethyl cellulose, hydroxyethylethyl cellulose, hydroxypropylmethyl cellulose, hydroxypropylethyl cellulose, etc.
- the polymers P2) are selected from homo- and copolymers comprising repeating units derived from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof.
- Suitable vinyl esters are generally the esters of vinyl alcohol with C1-C15- carboxylic acids, preferably Ci-C8-carboxylic acids, more preferably Ci-C4-carboxylic acids.
- Preferred vinyl acylates are vinyl acetate, vinyl n-propionate, vinyl n-butyrate, vinyl 2-ethyl- hexanoate, vinyl laurate, etc. Particularly preferred is vinyl acetate.
- Partially or completely saponified (hydrolyzed) polyvinyl acetates are generally referred to as "polyvinyl alcohol (PVOH)".
- Partially hydrolysed polyvinyl acetates are obtained by incomplete hydrolysis of polyvinyl acetates, i.e. the partially hydrolyzed polymer has both ester groups and hydroxyl groups.
- the saponification of the polyvinyl acetates can be carried out in a manner known per se in alkaline or acidic, i.e. with the addition of acid or base.
- polyvinyl alcohols are determined inter alia by the degree of polymerization and the degree of hydrolysis (degree of saponification). As the degree of saponification increases, the solubility in water decreases. Polyvinyl alcohols with degrees of hydrolysis of up to about 90 mol% are generally soluble in cold water. Polyvinyl alcohols with degrees of hydrolysis of about 90 to about 99.9 mol% are generally no longer soluble in cold water, but are soluble in hot water.
- Polyvinyl alcohols suitable as polymers P2) preferably have a saponification degree of from 50 to 99.9 mol%, particularly preferably from 70 to 99 mol%, in particular from 80 to 98 mol%.
- polyvinyl alcohols can further be modified by the incorporation of additional monomers such as the sodium salts of 2-acrylamido-2-methylpropane sulfonic acid, vinyl- sulfonic acid or allylsulfonic acid.
- Polyvinyl alcohols suitable as polymers P2) preferably have a weight-average molecular weight of from 10,000 to 300,000 g/mol, more preferably from 15,000 to 250,000 g/mol.
- Polyvinylalcohol that can typically be used as polymers P2) are known under the tradename PovalTM from Kuraray company. Non limited examples are PovalTM 8-88, PovalTM 18-88, PovalTM 26-88, PovalTM 30-92, PovalTM 10-98, PovalTM 20-98 or PovalTM 28-99.
- blends comprising polyvinylalcohols of different molecular weight and degree of hydrolysis can be used.
- Non limited examples are a blend of PovalTM 26-88 (three parts) and PovalTM 20-98 (one part) or a blend of PovalTM 30-92 (two parts) and PovalTM 10-98 (one part).
- Polyvinyl alcohols suitable as polymers P2) preferably have a viscosity of 2 to 120 mPa s, more preferably of 7 to 70 mPa s and in particular of 15 to 60 mPa s, measured according to DIN 53015 on a 4% solution in water.
- the polymers P2) are selected from homopolymers and copolymers which comprise at least one monomer in copolymerized form, which is selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, salts thereof three latter monomers, vinylpyridine-N-oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof.
- N-vinylimidazole, 2-vinylpyridine and 4-vinylpyridine can be converted by protonation or quater- nization into the corresponding salts.
- Suitable acids are e.g. mineral acids such as sulfuric acid, hydrochloric acid and phosphoric acid, and carboxylic acids.
- Alkylating agents suitable for quaternization are C1-C4 alkyl halides or C1-C4 alkyl sulfates such as ethyl chloride, ethyl bromide, methyl chloride, methyl bromide, dimethyl sulfate and diethyl sulfate.
- polyvinylpyrrolidone homopolymers and copolymers which comprise copolymerized N-vinylpyrrolidone and another ethylenically unsaturated monomer different therefrom.
- Suitable N-vinylpyrrolidone copolymers are generally neutral, anionic, cationic and amphoteric polymers.
- N-vinylpyrrolidone copolymers are selected from
- the polymers P2) are selected from homopolymers and copolymers of acrylic acid and/or methacrylic acid.
- the polymer P2) used is an acrylic acid homopolymer.
- Acrylic acid homopolymers P2) preferably have a number-average molecular weight in the range from 800 to 70,000 g/mol, more preferably from 900 to 50,000 g/mol, in particular from 1000 to 20,000 g/mol, especially from 1000 to 10,000 g/mol.
- the term acrylic acid homopolymer also encompasses polymers in which the carboxylic acid groups are partially or completely neutralized. These include acrylic acid homopolymers in which the carboxylic acid groups are present partially or completely in the form of alkali metal salts or ammonium salts.
- acrylic acid homopolymers in which the carboxylic acid groups are protonated or in which the carboxylic acid groups are present partially or completely in the form of sodium salts.
- Homopolymers of acrylic acid which are particularly suitable as polymers P2) are the Sokalan ® PA grades from BASF SE.
- the polymer P2) used is a copolymer comprising at least one acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof and at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form.
- acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof
- maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form.
- These preferably have a number-average molecular weight in the range from 2500 to 150,000 g/mol, more preferably from 2800 to 70,000 g/mol, in particular from 2900 to 50,000 g/mol, more particularly from 3000 to 30,000 g/mol.
- copoly-mers in which the carboxylic acid groups are partially or completely neutralized.
- monomers in salt form either for the polymerization or the resulting copolymer is subjected to a partial or complete neutralization.
- copolymers in which the carboxylic acid groups are protonated or partially or completely present in the form of alkali metal salts or ammonium salts.
- Preferred alkali metal salts are the sodium or potassium salts, especially the sodium salts.
- Preferred polymers P2) are copolymers of maleic acid (or maleic acid monomers) and acrylic acid (or acrylic acid monomers) in a weight ratio of 10:90 to 95: 5, particularly preferably in a weight ratio of 30:70 to 90:10.
- Preferred polymers P2) are also terpolymers of maleic acid (or maleic acid monomers), acrylic acid (or acrylic acid monomers) and a vinyl ester of a C1-C3 carboxylic acid in a weight ratio of 10 (maleic acid) : 90 (acrylic acid + vinyl ester) to 95 (maleic acid) : 10 (acrylic acid + vinyl ester).
- the weight ratio of acrylic acid to vinyl ester is preferably in a range of 30:70 to 70:30.
- Particularly suitable polymers P2) based on acrylic acid monomers and maleic acid monomers are the corresponding Sokalan ® CP grades from BASF SE.
- the polymer P2) is a copolymer, which comprises at least one (meth) acrylic acid monomer selected from (meth) acrylic acid, (meth) acrylic acid salts and mixtures thereof and at least one hydrophobic monomer.
- the hydrophobic monomer is especially selected from Ci-Cs alkyl esters of (meth) acrylic acid such as e.g. the methyl, ethyl, n- and iso-propyl, n-butyl and 2-ethylhexyl esters of (meth) acrylic acid and C 2 -Cio-olefins, e.g. ethene, propene, 1 ,2-butene, isobutene, disobutene, styrene and a-methylstyrene.
- the polymer P2) used is a copolymer of at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof with at least one C 2 -C 8 -olefin.
- copolymers which comprise at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form at least one C2-Cs-olefin and at least one other comonomer which is different therefrom.
- copolymers which comprise at least one maleic acid monomer select ed from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof and at least one C 2 -C 8 -olefin copolymerized as sole monomers. These preferably have a number average molecular weight in the range from 3000 to 150,000 g/mol, particularly preferably from 5000 to 70,000 g/mol, in particular from 8000 to 50,000 g/mol, more particularly from 10,000 to 30,000 g/mol. Included therein are also copolymers in which the carboxylic acid groups are partially or completely neutralized.
- maleic acid salts can be used for the polymerization or the resulting copolymer is subjected to a partial or complete neutralization.
- Preferred alkali metal salts are the sodium or potassium salts, especially the sodium salts.
- a specific embodiment are copolymers of maleic acid with C2-C8 olefins in a molar ratio of 40:60 to 80:20, whereby copolymers of maleic acid with ethylene, propylene, isobutene, diisobutene or styrene are particularly preferred.
- Particularly suitable polymeric carboxylic acid group- containing compounds based on olefins and maleic acid are likewise the corresponding Soka- lan ® CP grades from BASF SE.
- copolymers comprising at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, at least one C2-C8 olefin and at least one acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof, in copolymerized form.
- a further preferred embodiment is copolymers which comprise at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, at least one C2-C8 olefin and at least one ester of (meth) acrylic acid in copolymerized form.
- the ester of (meth) acrylic acid is then in particular selected from C2-Cs-alkyl esters of (meth) acrylic acid, e.g. the methyl, ethyl, n- and iso-propyl, n-butyl and 2-ethylhexyl esters of (meth) acrylic acid.
- the polymers P2) are selected from homopolymers and co polymers which comprise, in polymerized form, at least one monomer selected from acrylamide, methacrylamide and mixtures thereof. These polymers P2) are preferably water-soluble or water-dispersible. In particular, these polymers P2) are water-soluble.
- the polymers P2) are selected from homopolymers of acrylamide or methacrylamide.
- the polymers P2) are selected from copolymers of acrylamide and/or methacrylamide. These comprise at least one comonomer in copolymerized form, which is selected from acrylamide and methacrylamide different hydrophilic monomers (A1 ), monoeth- ylenically unsaturated, amphiphilic monomers (A2) and other ethylenically unsaturated monomers (A3).
- Suitable hydrophilic, monoethylenically unsaturated monomers (A1 ) are neutral monomers, such as N-methyl (meth) acrylamide, N, N'-dimethyl (meth) acrylamide or N-methylol (meth) acrylamide, monomers comprising hydroxyl and/or ether groups, such as e.g.
- N-vinyl derivatives can be hydrolyzed after polymerization to vinylamine units, vinyl esters to vinyl alcohol units.
- Suitable hydrophilic, monoethylenically unsaturated monomers (A1 ) are furthermore monomers which comprise at least one acidic group or salts thereof. These include acrylic acid, methacrylic acid, crotonic acid, itaconic acid, maleic acid, fumaric acid, vinylsulfonic acid, allylsulfonic acid, 2-acrylamido-2-methylpropanesulfonic acid, 2-methacrylamido-2-methylpropanesulfonic acid, 2-acrylamidobutanesulfonic acid, 3-acryl- amido-3-methylbutanesulfonic acid, 2-acrylamido-2,4,4-trimethylpentanesulfonic acid, vi- nylphosphonic acid, allylphosphonic acid, N-(meth) acrylamidoalkylphosphonic acids, (meth) acryloyloxyalkylphosphonic acids and salts and mixtures thereof.
- the other monoethylenically unsaturated hydrophilic monomers may be hydrophilic cationic monomers.
- Suitable cationic monomers (A1 c) include, in particular, ammonium-group containing monomers, in particular ammonium derivatives of N-(u)-aminoalkyl) (meth) acrylamides or w-aminoalkyl (meth) acrylic esters.
- amphiphilic monomers (A2) are preferably monoethylenically unsaturated monomers which have at least one hydrophilic group and at least one, preferably terminal, hydrophobic group.
- the monomers (A3) may be e.g. monoethylenically unsaturated monomers which have a more hydrophobic character than the hydrophilic monomers (A1) and which accordingly are only slightly water-soluble.
- monomers include N-alkyl and N, N'-dialkyl (meth) acrylamides wherein the number of carbon atoms in the alkyl groups together is at least 3, preferably at least 4.
- monomers include N-butyl (meth) acrylamide, N-cyclohexyl (meth) acrylamide or N-benzyl (meth) acrylamide.
- the polymers P2) are selected from polyamino acids.
- Suita ble polyamino acids are in principle compounds, which comprise at least one amino acid, such as aspartic acid, glutamic acid, lysine, glycine, etc. in copolymerized form.
- the polyamino acids also include the derivatives obtainable by polymer-analogous reaction, such as esterification, amidation, etc.
- Preferred polyamino acids are polyaspartic acid, polyaspartic acid derivatives, polyglutamic acid, polyglutamic acid derivatives and mixtures thereof.
- Polyaspartic acid may e.g. by alkaline hydrolysis of polysuccinimide (PSI, anhydropolyaspartic acid).
- PSI polysuccinimide
- Polysuccinimide can be prepared by thermal condensation of aspartic acid or from ammonia and maleic acid.
- Polyaspartic acid may e.g. be used as a biodegradable complexing agent and cobuilder in detergents and cleaners.
- Polyamino acids having surfactant properties can be obtained by at least partially converting the free carboxylic acid groups of polyaspartic acid or polyglutamic acid into N-alkylamides and/or into esters.
- Polyaspartic acid amides can also be prepared by reacting polysuccinimide with amines.
- hydroxyethylaspartamides the ring opening of polysuccinimide can be carried out with ethanolamine.
- DE 37 00 128 A and EP 0 458 079 A describe the subsequent esterification of such hydroxyethyl derivatives with carboxylic acid derivatives.
- Copolymers of polyaspartic ester are, as described in DE 195 45 678 A, obtainable by condensation of monoalkyl esters of maleic or fumaric acid with addition of ammonia.
- copolymeric polyaspartic esters are accessible by reaction of polysuccin- imide with alcohols and optionally subsequent hydrolysis.
- polyaspartic esters in addition to their bio degradability, are distinguished by excellent properties as stabilizers for O / W and W / O emulsions, foam-stabilizing and foam-enhancing cosurfactants in detergents and cleaners and as complexing agents for metal cations.
- the polymers P2) are selected from polyalkylene glycols and mono- or diethers of polyalkylene glycols.
- Preferred polyalkylene glycols have a number aver age molecular weight in the range from 1000 to 4,000,000 g/mol, particularly preferably from 1 ,500 to 1 ,000,000 g/mol
- Suitable polyalkylene glycols and their mono- or diethers may be linear or branched, preferably linear.
- Suitable polyalkylene glycols are e.g. water-soluble or water-dispersible nonionic polymers, which comprise alkylene oxide repeat units. The proportion of alkylene oxide repeating units is preferably at least 30% by weight, preferably at least 50% by weight, in particular at least 75% by weight, based on the total weight of the compound.
- Suitable polyalkylene glycols are polyethylene glycols, polypropylene glycols, polytetrahydrofurans and alkylene oxide copolymers.
- Suitable alkylene oxides for the preparation of alkylene oxide copolymers are, for.
- ethylene oxide, propylene oxide, epichlorohydrin, 1 ,2- and 2,3-butylene oxide Suitable examples are copolymers of ethylene oxide and propylene oxide, copolymers of ethylene oxide and butylene oxide and copolymers of ethylene oxide, propylene oxide and at least one butylene oxide.
- the alkylene oxide copolymers may comprise randomly distributed alkylene oxide units or in copolymerized form in the form of blocks.
- the proportion of repeating units derived from ethylene oxide is 40 to 99% by weight.
- Particularly preferred are ethylene oxide homopolymers and ethylene oxide / propylene oxide copolymers.
- Suitable mono- and diethers of polyalkylene glycols are the mono (C1-C18 alkyl ethers) and di (C1-C18 alkyl ethers).
- Preferred mono- and diethers of polyalkylene glycols are the mono (C1-C6 alkyl ethers) and di (C1-C6 alkyl ethers).
- Especially preferred are the mono (C1-C2 alkyl ethers) and di (C1-C2 alkyl ethers).
- Particularly preferred are polyalkylene glycol monomethyl ether and polyalkylene glycol dimethyl ether.
- At least one of the layers comprises or consists of at least one compound selected from the group consisting of (i) vinyl- imidazole containing polymers, preferably vinylpyrrolidone/vinylimidazole copolymers with a molecular weight Mw in the range of 10000 to 100000 g/mol, (ii) polyvinylpyrrolidones with a molecular weight Mw in the range of 10000 to 100000 g/mol, (iii) polyethylene imine ethox- ylates, (iv) multifunctional diamines and (v) amphoteric modified starch, and mixtures thereof.
- vinyl- imidazole containing polymers preferably vinylpyrrolidone/vinylimidazole copolymers with a molecular weight Mw in the range of 10000 to 100000 g/mol
- polyvinylpyrrolidones with a molecular weight Mw in the range of 10000 to 100000 g/mol
- At least one of the layers comprises at least one additive and/or at least one additive is present between at least two layers, said additive preferably being selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, enzymes, bases, corrosion inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluores- cers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, corrosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and anti
- At least two of the layers preferably two of the layers, comprise at least one type of enzyme EN) each.
- two of the layers comprise one enzyme EN) each, wherein the enzymes EN) comprised in the different layers are different from each other, and preferably are incompatible with each other (as defined above).
- At least two of the layers comprise one enzyme EN) each, and wherein the layers comprising one enzyme EN) each are spatially separated by at least one layer comprising or consisting of composition P1 ) or P2), and wherein the separating layer does not contain enzymes, and wherein the enzymes EN) comprised in the different layers are preferably different from each other, and further preferably are incompatible with each other.
- At least one enzyme EN) is incorporated in one of the layers comprising or consisting of a composition P2), wherein this layer comprising or consisting of a composition P2) preferably comprises polyvinyl alcohol.
- all of the enzymes EN) are incorporated in any one of the layers comprising or consisting of a composition P2).
- At least one layer contains protease as enzyme EN1 ) (preferably as the only enzyme in this layer), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease and preferably different from protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1 ) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
- none of the layers contains a protease inhibitor (as defined above).
- the water-soluble multilayer film is derived from a wash active layer based on a at least one polymer chosen from P2), preferred a polymer blend, more preferred chosen from polymer composition P1 ), which is used as adhesion layer in-between two enzyme containing layers, optionally in a lamination process.
- Multilayer films can be produced e.g. by a lamination method. Lamination methods in which two or more film layers are bonded to one another over their area are known to those skilled in the art. Lamination involves pressing two or more than two films together under elevated pressure and/or at elevated temperature. Multilayer films can also be produced by a wet-on-wet application method. In addition, multilayer films can also be produced by using combinations of the aforementioned production methods and the application method described hereinafter.
- the multilayer film is produced by a process in which at least one free-flowing composition capable of film formation is applied to a carrier material, wherein the carrier material and/or the at least one free-flowing composition comprises or consists of the polymer composition P1 ) as defined above and hereinafter, or comprises a polymer P1’) and a polyoxyalkylene ether PE) as defined above and hereinafter.
- the process for producing a multilayer film preferably comprises the steps of
- a first free-flowing or pourable composition capable of film formation is applied to a carrier material to obtain a first layer
- the first layer applied to the carrier material is optionally subjected to an increase in viscosity
- a second free-flowing or pourable composition capable of film formation is applied to the first layer obtained in step H ) or in step i2) to obtain a second layer,
- the second layer is optionally subjected to an increase in viscosity
- step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to repeat steps i3) and i4) once or more than once,
- the layers applied to the carrier material are optionally subjected to a further increase in viscosity
- the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing or pourable compositions each comprise a component which is capable of film formation and is independently selected from at least one polymer composition P1 , at least one polymer P2 or a mixture thereof, and with the proviso that the carrier material and/or the at least one free-flowing or pourable composition comprises or consists of a polymer composition P1 as defined above and hereinafter.
- the application of two or more than two of the pourable compositions can also be applied partly or fully simultaneously.
- the application of the (n+1)th composition can be commenced before the application of the nth composition has completely ended.
- the production of the multilayer film proceeds from a carrier material which already comprises the first film layer and optionally also already comprises fur ther film layers of the multilayer film.
- a carrier material which already comprises the first film layer and optionally further film layers of the multilayer film is used in step i1 ).
- the carrier material forms part of the multilayer film and remains in the multilayer film after the application of all the further layers. This means that the further layers applied to the carrier material are not subsequently detached again from the carrier material. In this embodiment, there is therefore no step i7) of the above-described process.
- the viscosity of the free-flowing composition is matched to the technical demands of the production method and is determined by factors including the concentration of the components capable of film formation, the solvent content (water), the additives added and the temperature.
- the pourable compositions capable of film formation are applied in steps i 1 ) , i3) and i5) general- ly by means of standard methods, for example by means of pre-metered and self-metered methods selected from airblade coating, knife coating, airknife coating, squeegee coating, impregnation coating, dip coating, reverse roll coating, transfer roll coating, gravure coating, kiss coating, flow coating, cascade flow coating, slide coating, curtain coating, mono- and multilami- nar slot die coating, spray coating, spin coating, or printing methods such as relief printing, intaglio printing, rotogravure printing, flexographic printing, offset printing, inkjet printing, letter- press printing, pad printing, heatseal printing or screenprinting methods.
- the application can also be continuous or semicontinuous, for example when the carrier material is moving, for example a permanently or intermittently moving belt.
- Suitable carrier materials are firstly all materials which enable simple detachment of the finished multilayer film. Examples of these include glass, metals such as galvanized steel sheet or stainless steel, polymers such as silicones or polyethylene terephthalate, polymer-coated paper, such as silicone paper, etc. Suitable carrier materials are secondly monolaminar or multilaminar polymer films which remain as film layers in the multilayer film of the invention. With regard to the composition of these carrier materials, reference is made to the disclosure relating to the polymer composition P1 and the disclosure relating to polymers P2.
- the increase in viscosity in layers i2), i4) and i6) can be effected by means of standard methods and generally depends on the form in which pourable compositions capable of film formation have been applied in steps i1 ), i3) and i5). If they have been applied as a melt, for example, there is generally already an increase in viscosity in the course of cooling.
- the cooling can be effected by simply leaving the carrier material to stand or by active cooling, such as cooling of the carrier material, jetting with a cool gas (jet), cooling in a cold room/refrigerator and the like.
- the free-flowing composition capable of film formation has been applied in the form of a solution or dispersion, it is generally necessary to remove at least some of the solvent, which can be effected, for example, by simply leaving the carrier material to stand, drying with an air jet or hot air jet, drying in drying cabinets, heating of the carrier material, application of a reduced pressure, optionally with simultaneous supply of heat, IR irradiation, microwave radiation, for exam ple in a corresponding oven, and the like.
- the composition be curable, for example because the polymers present therein comprise as yet unconverted polymerizable/condensable groups, the increase in viscosity can alternatively or additionally be effected by curing the poly mer.
- ethylenically unsaturated crosslinkable groups are especially cured by UV radiation; condensable groups, by contrast, generally cure either by being left to stand or with supply of heat.
- the heat can again be supplied as described above, i.e., for example, by incidence of warm or hot air or other warm or hot gases, drying in drying cabinets, heating of the carrier material, IR irradiation and the like. It is also possible to gel the solution or dispersion applied by cooling, in the sense of forming a physical network extended over macroscopic di- mensions, which likewise results in an increase in viscosity.
- the pourable compositions capable of film formation for two or more than two of the layers that form the multilayer film are applied by a wet-on-wet application method.
- the application in i3), i5) etc. can thus be effected wet-on-wet, meaning that the next layer can also be applied to the layer applied in step i 1 ), i3) and/or i5) without an explicit step for increasing viscosity having been conducted beforehand. This is especially true when the layer to which the next polymer layer is applied is sufficiently thin, such that it solidifies sufficiently even without being explicitly left to stand, dried, heated, cured, etc. before the next layer is applied, and there is no complete mixing with the components of the next layer.
- the polymers applied in steps i 1 ), i3), i5) etc. are film-forming polymers.
- One or more than one of the layers comprising film-forming polymers may additionally comprise at least one additive.
- any film-forming polymers are especially layers comprising components (functional materials) connected to the desired end use of the multi layer film.
- these optional further layers may comprise surfactants, builders, cobuilders, bleaches, enzymes, graying inhibitors, optical brighteners, fragrances, dyes, etc.
- surfactants may, like the polymer layers too, be applied in solution/dispersion or melt. Suitable application techniques here too are those mentioned above.
- This can be effected by means of standard embossing, printing, stamping and punching tools.
- the process of the invention allows the production of multilayer films without a complex lamina- tion method in which the individual films have to be bonded to one another.
- the multilayer films of the invention can also be produced, as described above, by bond ing two or more than two film layers to one another by laminating.
- multilaminar polymer films which serve as carrier material for application of further film layers may be provided by bonding two or more than two film layers to one another by laminating.
- a component which is capable of film formation and is selected from polymer compositions P1 , at least one polymer P2, optionally after addition of at least one additive, is melted or dissolved in a suitable solvent or solvent mixture, the pourable composition thus obtained is poured out to form a layer and the solvent or solvent mixture is optionally removed by evaporation.
- the solvent is preferably selected from water, ethanol, n-propanol, isopropanol, ethylene glycol, diethylene glycol, 1 ,2-propylene glycol, 1 ,2-dipropylene glycol and mixtures thereof.
- the solvent used is selected from water and a mixture of water and at least one solvent other than water, selected from ethanol, n-propanol, isopropanol, ethylene glycol, diethylene glycol, 1 ,2-propylene glycol, 1 ,2-dipropylene glycol and mixtures thereof.
- the multilayer film can be applied to a steel belt or a heated roller using single or multi-layer casting or coating tools such as slot nozzles, doctor blade, curtain coating, cascade casting, etc.
- one or more layers can be applied simultaneously and the other layers optionally on a different position of the steel strip or the roller.
- another layer can be applied in a post-drying step on the freestanding film after detaching from the carrier material (steel strip or roller). Roller-based coating processes are particularly suitable for this subsequent coating.
- a lamination step can also be carried out with a pre viously prepared or commercially available film.
- the laminating step of the films may be carried out before detaching a film, immediately after detaching the film and before drying of the freestanding film, during the drying of the freestanding film or after the drying, but before the wind ing.
- a separate lamination of two films is also possible.
- lamination is possible solely by means of a targeted adjustment of the residual moisture in the film and correspondingly selected line loads.
- a specific embodiment is a process for producing a washing- and cleaning-active single layer or multilayer polymer film, which comprises at least one additive.
- Additives can be added before or during the film formation in step b). Whether the addition takes place before or during step b) depends on the type and effect of the particular additive.
- additives can be added to the aqueous composition before and/or during the film production.
- an individual layer or a plurality of but not all the layers or all the layers may each comprise one or more than one additive.
- at least one additive is present between at least two layers.
- the additives may be auxiliaries for adjustment of the properties of the pourable compositions capable of film formation, typical additives of the washing and cleaning compositions or mixtures thereof.
- a special embodiment is a single layer film that comprises at least one additive.
- a further special embodiment is a multilayer film in which at least one of the layers includes an additive. Particular preference is given to single layer and multilayer films in which at least one of the layers includes an additive which is a constituent customary for washing and cleaning compositions.
- the additive is preferably selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, bleach activators, bleach catalysts, enzymes, bases, corrosion inhibitors, foam inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, bitter agents such as Bitrex ® , antiyellowing agents, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, bitter substances, fluorescers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, anti-yellowing agents, cor rosion inhibitors, antistats, ironing aids, hydrophob
- wash-active layer comprising or consisting of P1 ) or P2), may serve not only the purpose of being wash-active, but also can be used as lamination adhesive, due to their special compo sitions and associated properties (tackiness).
- the residual moisture of the wash-active layer comprising or consisting of P1 ) or P2, is prefer ably lower than 15 % by weight, more preferably equal to or lower than 10 % by weight.
- the temperature during the lamination process is preferably lower than 100 °C, more preferably lower than 80 °C, even more preferably lower than 50 °C and most preferably lower than 30 °C.
- at least one layer, preferably an enzyme-containing layer is laminated at room temperature onto any of the other layers.
- plasticizers can be added to them before or during production.
- plasticizers preferably 0.5% to 30% by weight, more preferably 2% to 20% by weight and especially 3% to 15% by weight of plasticizer is used, based on the total weight of the composition.
- Suitable plasticizers are alkyleneamines, alkanolamines, polyols, such as alkylene glycols and oligoalkylene glycols, e.g. 2-methyl-1 ,3-propanediol, 3-methyl-1 ,5-pentadiol, hydroxypropylglyc- erol, neopentyl glycol, alkoxylated glycerol (such as e.g. Voranol ® from Dow Chemicals), water- soluble polyesterpolyols (such as e.g. TriRez from Geo Specialty Chemicals) and mixtures thereof.
- alkyleneamines alkanolamines
- polyols such as alkylene glycols and oligoalkylene glycols, e.g. 2-methyl-1 ,3-propanediol, 3-methyl-1 ,5-pentadiol, hydroxypropylglyc- erol, neopen
- Suitable plasticizers are also polyetherpolyols, which are available under the name Lu- pranol ® from BASF SE.
- alkyleneamines refers to condensation products of alka- nolamines with ammonia or primary amines, e.g. ethyleneamines are obtained by reaction of monoethanolamine with ammonia in the presence of a catalyst.
- ethylenediamine, piperazine, diethylenetriamine and aminoethylethanola- mine are also polyetherpolyols, which are available under the name Lu- pranol ® from BASF SE.
- alkyleneamines refers to condensation products of alka- nolamines with ammonia or primary amines, e.g. ethyleneamines are obtained by reaction of monoethanolamine with ammonia in the presence of a catalyst.
- main components ethylenediamine, piperazine, diethylenetriamine and aminoethylethanola- mine.
- the plasticizers are selected from glycerol, diglycerol, propylene glycols with a weight-average molecular weight of up to 400, e.g. dipropylene glycol, ethylene glycol, diethylene glycol, triethylene glycol, tetraethylene glycol, sorbitol, isopentyldiol, polyethylene glycol, trimethylolpropane, diethylenetriamine, triethylenepentamine, triethanolamine and mixtures thereof.
- glycerol diglycerol
- propylene glycols with a weight-average molecular weight of up to 400, e.g. dipropylene glycol, ethylene glycol, diethylene glycol, triethylene glycol, tetraethylene glycol, sorbitol, isopentyldiol, polyethylene glycol, trimethylolpropane, diethylenetriamine, triethylenepentamine, triethanolamine and mixtures thereof.
- scavengers capture molecules
- Suitable scavengers are polyamines, polymeric polyamines, such as polyethyleneimines,
- poly(amidoamines) and polyamides are also possible to use ammonium sulfate, primary and secondary amines with a low vapor pressure, such as ethanolamines, amino acid and salts thereof, and also polyamino acid and salts thereof, fatty amines, glucosamines and other aminated sugars.
- reducing agents such as sulfites, bisulfites, thiosulfites, thiosulfates, iodides, nitrites and antioxidants such as carbamates, ascorbates and mixtures thereof can be used.
- At least one surface or both surfaces of the single and multilayer films of the invention may be subject to at least partial coating with at least one additive.
- a treatment may serve, for example, to provide the surface with particular properties, such as nonstick action, antistatic action, hydrophilic or hydrophobic properties, etc.
- the single and multilayer films for example, with better detachment properties from the carrier material used in the production, better roll-off properties, better glide properties, reduced tack, better compatibility with particular components ensheathed or coated therewith, etc.
- the application can be effected by standard methods, for example by spraying, dipping, powder application, etc.
- Suitable additives for coating of the sur face of the multilayer films of the invention are, for example, talc, surfactants such as silicone- containing surfactants, waxes, etc.
- a further subject of the present invention is a process for producing a water-soluble container comprising the steps of:
- At least one of the first or second water-soluble films is a multi-layered film as above, and wherein before the sealing step the second water-soluble film covering the filled pouch is contacted with water.
- an inventive multilayer film or obtainable by an inventive process, as a washing composition or as a cleaning composition is a subject of the present invention.
- a further inventive subject is the use of a multilayer film as defined above or obtainable by a process as defined above, for at least partial ensheathing of a liquid and/or solid washing and cleaning composition.
- Another inventive subject is a sheath or coating for a washing composition portion or cleaning composition portion, comprising or consisting of a multilayer film as defined above or obtainable by a process as defined above.
- a subject of the invention is also a washing or cleaning composition
- a washing or cleaning composition comprising:
- At least one sheath and/or coating comprising or consisting of a washing- and cleaning- active multilayer film as defined above or obtainable by a process as defined above,
- further additive preferably selected from enzymes, bases, corro- sion inhibitors, defoamers, dyes, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluores- cers, hydrotropes
- the enzyme EN is preferably selected from an oxidoreductase (EC 1), a transferase (EC 2), a hydrolase (EC 3), a lyase (EC 4), a Isomerase (EC 5), or a Ligase (EC 6) (EC-numbering according to Enzyme Nomenclature, Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology in cluding its supplements published 1993-1999).
- EC 1 oxidoreductase
- EC 2 transferase
- hydrolase EC 3
- a lyase EC 4
- Isomerase EC 5
- Ligase EC 6
- the enzyme is a hydrolase (EC 3), preferably, a glycosidase (EC 3.2) or a pep tidase (EC 3.4).
- Especially preferred enzymes are enzymes selected from the group consisting of an amylase (in particular an alpha-amylase (EC 3.2.1.1 )), a cellulase (EC 3.2.1.4), a lactase (EC 3.2.1 .108), a mannanase (EC 3.2.1.25), a lipase (EC 3.1.1.3), a phytase (EC 3.1.3.8), a nuclease (EC 3.1 .1 1 to EC 3.1.31 ), and a protease (EC 3.4).
- an amylase in particular an alpha-amylase (EC 3.2.1.1 )
- a cellulase EC 3.2.1.4
- a lactase EC 3.2.1 .108
- a mannanase
- the enzyme EN is preferably selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
- Enzymes are generally produced commercially by using recombinant cells which express the desired enzyme by cultivation of the same under conditions suitable for expression of the desired enzyme.
- the term“recombinant cell” (also called“genetically modified cell” herein) refers to a cell which has been genetically altered, modified or engineered such that it exhibits an altered, modified or different genotype as compared to the wild-type cell which it was derived from.
- The“recombinant cell” may comprise an exogenous polynucleotide.
- the recombinant cell may comprise exogenous polynucleotide encoding for a certain protein or enzyme and therefore may express said protein or enzyme.
- heterologous or exogenous or foreign or recombinant polypeptide is defined herein as a polypeptide that is not native to the host cell, a polypeptide native to the host cell in which structural modifications, e.g., deletions, substitutions, and/or insertions, have been made to alter the native polypeptide, or a polypeptide native to the host cell whose expression is quantitatively altered or whose expression is directed from a genomic location different from the native host cell as a result of manipulation of the DNA of the host cell by recombinant DNA techniques, e.g., a stronger promoter.
- heterologous refers to a polynucleotide that is not native to the host cell, a polynucleotide native to the host cell in which structural modifications, e.g., deletions, substitutions, and/or insertions, have been made to alter the native polynucleotide, or a polynucleotide native to the host cell whose expression is quantitatively altered as a result of manipulation of the regulatory elements of the polynucleotide by recombinant DNA techniques, e.g., a stronger promoter, or a polynucleotide native to the host cell, but integrated not within its natural genetic environment as a result of genetic manipulation by recombinant DNA techniques.
- heterologous is used to characterized that the two or more polynucleotide sequences or two or more amino acid sequences are naturally not occurring in the specific combination with each other.
- nucleotide or polypeptide refers to the cell or organism as found in nature and to the polynucleotide or polypeptide in question as found in a cell in its natural form and genetic environment, respectively (i.e., without there being any human intervention).
- Cultivation normally takes place in a suitable nutrient medium allowing the recombinant host cells to grow (this process may be called fermentation) and express the desired protein.
- fermentation broth is collected and may be further processed, wherein the fermentation broth comprises a liquid fraction and a solid fraction.
- the desired protein or enzyme may be secreted (into the liquid fraction of the fermentation broth) or may not be secreted from the host cells (and therefore is comprised in the solid frac tion of the fermentation broth). Depending on this, the desired protein or enzyme may be recovered from the liquid fraction of the fermentation broth or from cell lysates. Recovery of the de- sired enzyme uses methods known to those skilled in the art. Suitable methods for recovery of proteins or enzymes from fermentation broth include but are not limited to collection, centrifugation, filtration, extraction, and precipitation.
- the isolated polypeptide may then be further purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, chroma- tofocusing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focus- ing (IEF), differential solubility (e.g., ammonium sulfate precipitation), or extraction (see, e.g., Protein Purification, J.-C. Janson and Lars Ryden, editors, VCH Publishers, New York, 1989).
- the purified polypeptide may then be concentrated by procedures known in the art including, but not limited to, ultrafiltration and evaporation, in particular, thin film evaporation.
- the final enzyme-comprising product may be liquid or aqueous and may be called enzyme concentrate.
- Liquid enzyme-comprising products may be dried to stabilize enzyme(s).
- dried enzymes need to be re-solved in solvent such as water or water-containing buffer prior to use.
- solvent such as water or water-containing buffer prior to use.
- enzyme-comprising products are often aqueous before they are used in applications.
- Liquid enzyme concentrate herein means any liquid enzyme-comprising product comprising at least one type of enzyme.“Liquid” in the context of enzyme concentrate is related to the physi cal appearance at 20°C and 101.3 kPa.
- Liquid enzyme concentrates may comprise amounts of enzyme in the range of 0.1 % to 40% by weight, or 0.5% to 30% by weight, or 1 % to 25% by weight, all relative to the total weight of the enzyme concentrate.
- the liquid enzyme concentrate may comprise more than one type of enzyme.
- liquid enzyme concentrate is an aqueous enzyme concentrate.
- Aqueous enzyme concentrate herein means any aqueous enzyme-comprising product comprising at least one type of enzyme, which may result e.g. from fermentation.
- Aqueous enzyme concentrate may also mean that at least one type of enzyme in its solid state has been dissolved in aqueous solvent.
- Aqueous enzyme concentrates of the invention may comprise water in amounts of more than about 50% by weight, more than about 60% by weight, more than about 70% by weight, or more than about 80% by weight, all relative to the total weight of the enzyme concentrate.
- Liquid enzyme concentrate of the invention may comprise residual components such as salts originating from the fermentation medium, cell debris originating from the production host cells, metabolites produced by the production host cells during fermentation.
- residual components may be comprised in liquid enzyme concentrates in amounts less than 30% by weight, less than 20% by weight less, than 10% by weight, or less than 5% by weight, all relative to the total weight of the aqueous enzyme concentrate.
- the water-soluble multilayer film of the invention comprises at least one lipase.“Lipases”,“lipolytic enzyme”,“lipid esterase”, all refer to an enzyme of EC class 3.1.1 (“carboxylic ester hydrolase”).
- Such an enzyme may have lipase activity (or lipolytic activity; triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; enzymes having cutinase ac- tivity may be called cutinase herein), sterol esterase activity (EC 3.1.1.13) and/or wax-ester hydrolase activity (EC 3.1.1.50).
- Lipases include those of bacterial or fungal origin.
- lipase enzymes include but are not limited to those sold under the trade names LipolaseTM, LipexTM, LipolexTM and LipocleanTM (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM).
- a suitable lipase is selected from the following: lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa ( T. lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. inso/ens as described in WO 96/13580,
- Bacillus lipases e.g. as disclosed in WO 00/60063, lipases from B. subtilis es disclosed in Dartois et al. (1992), Biochemica et Biophysica Acta, 1 131 , 253-360 or WO 201 1/084599, B. stearothermophilus (JP S64-074992) or B. pumi/us (WO 91/16422).
- Suitable lipases include also those referred to as acyltransferases or perhydrolases, e.g. acyl- transferases with homology to Candida antarctica lipase A (WO 2010/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO 2005/056782), perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant (WO 2010/100028).
- acyltransferases or perhydrolases e.g. acyl- transferases with homology to Candida antarctica lipase A (WO 2010/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO 2005/056782), perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant
- Suitable lipases include also those which are variants of the above described lipases and/or cutinases which have lipolytic activity.
- Such suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105.
- Suitable lipases/cutinases include also those, which are variants of the above described lipas- es/cutinases which have lipolytic activity.
- Suitable lipase/cutinase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
- lipase/cutinase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent en- zyme as disclosed above.
- the invention relates to lipase/cutinase variants comprising conservative mutations not pertaining the functional domain of the respective lipase/cutinase.
- Li pase/cutinase variants of this embodiment having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least
- Enzyme variants may be defined by their sequence identity when compared to a parent en- zyme. Sequence identity usually is provided as“% sequence identity” or“% identity”. To determine the percent-identity between two amino acid sequences in a first step a pairwise sequence alignment is generated between those two sequences, wherein the two sequences are aligned over their complete length (i.e., a pairwise global alignment). The alignment is generated with a program implementing the Needleman and Wunsch algorithm (J. Mol. Biol. (1979) 48, p.
- the preferred alignment for the purpose of this invention is that alignment, from which the highest sequence identity can be determined.
- %-identity (identical residues / length of the alignment region which is showing the respective sequence of this invention over its complete length) * 100.
- sequence identity in relation to comparison of two amino acid sequences according to this embodiment is calculated by dividing the number of identical residues by the length of the alignment region which is showing the re spective sequence of this invention over its complete length. This value is multiplied with 100 to give“%-identity”.
- the pairwise alignment shall be made over the complete length of the coding region from start to stop codon excluding introns.
- the pairwise alignment shall be made over the complete length of the sequence of this invention, so the complete sequence of this invention is compared to another sequence, or regions out of another sequence.
- Seq B GATCTGA length: 7 bases
- sequence B is sequence B.
- the ⁇ ” symbol in the alignment indicates identical residues (which means bases for DNA or amino acids for proteins). The number of identical residues is 6.
- the symbol in the alignment indicates gaps.
- the number of gaps introduced by alignment within the Seq B is 1.
- the number of gaps introduced by alignment at borders of Seq B is 2, and at borders of Seq A is 1.
- the alignment length showing the aligned sequences over their complete length is 10.
- the alignment length showing the shorter sequence over its complete length is 8 (one gap is present which is factored in the alignment length of the shorter sequence).
- the alignment length showing Seq A over its complete length would be 9 (meaning Seq A is the sequence of the invention).
- the alignment length showing Seq B over its complete length would be 8 (meaning Seq B is the sequence of the invention).
- Enzyme variants may be defined by their sequence similarity when compared to a parent en zyme. Sequence similarity usually is provided as“% sequence similarity” or“%-similarity”. For calculating sequence similarity in a first step a sequence alignment has to be generated as described above. In a second step, the percent-similarity has to be calculated, whereas percent sequence similarity takes into account that defined sets of amino acids share similar properties, e.g., by their size, by their hydrophobicity, by their charge, or by other characteristics.
- the exchange of one amino acid with a similar amino acid is referred to as‘‘conservative muta tion”. Enzyme variants comprising conservative mutations appear to have a minimal effect on protein folding resulting in certain enzyme properties being substantially maintained when compared to the enzyme properties of the parent enzyme.
- %-similarity For determination of %-similarity according to this invention the following applies, which is also in accordance with the BLOSUM62 matrix, which is one of the most used amino acids similarity matrix for database searching and sequence alignments
- Amino acid A is similar to amino acids S
- Amino acid D is similar to amino acids E; N
- Amino acid E is similar to amino acids D; K; Q
- Amino acid F is similar to amino acids W; Y
- Amino acid H is similar to amino acids N; Y
- Amino acid I is similar to amino acids L; M; V;
- Amino acid K is similar to amino acids E; Q; R
- Amino acid L is similar to amino acids I; M; V
- Amino acid M is similar to amino acids I; L; V
- Amino acid N is similar to amino acids D; H; S;
- Amino acid Q is similar to amino acids E; K; R
- Amino acid R is similar to amino acids K; Q
- Amino acid S is similar to amino acids A; N; T
- Amino acid T is similar to amino acids S
- Amino acid V is similar to amino acids I; L; M
- Amino acid W is similar to amino acids F; Y
- Amino acid Y is similar to amino acids F; H; W.
- Conservative amino acid substitutions may occur over the full length of the sequence of a poly peptide sequence of a functional protein such as an enzyme. In one embodiment, such mutations are not pertaining the functional domains of an enzyme. In another embodiment conservative mutations are not pertaining the catalytic centers of an enzyme.
- %-similarity [ (identical residues + similar residues) / length of the alignment region which is showing the respective sequence of this invention over its complete length ] * 100.
- se quence similarity in relation to comparison of two amino acid sequences herein is calculated by dividing the number of identical residues plus the number of similar residues by the length of the alignment region which is showing the respective sequence of this invention over its complete length. This value is multiplied with 100 to give“%-similarity”.
- variant enzymes comprising conservative mutations which are at least m percent similar to the respective parent sequences with m being an integer between 50 and 100, prefer ably 50, 55, 60, 65, 70, 75, 80, 85, 90, 91 , 92, 93, 94, 95, 96, 97, 98 or 99 compared to the full length polypeptide sequence, are expected to have essentially unchanged enzyme properties.
- Variant enzymes described herein with m percent-similarity when compared to a parent en- zyme have enzymatic activity.
- Lipases according to the invention have“lipolytic activity”.
- the methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71).
- the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl palmitate (pNP-Palmitate, C:16) and releases pNP which is yellow and can be detected at 405 nm.
- Lipase variants may have lipolytic activity according to the present invention when said lipase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the lipolytic activity of the re spective parent lipase.
- the water-soluble multilayer film of the invention comprises at least one protease.
- Enzymes having proteolytic activity are called“proteases” or peptidases in the context of the invention and are members of class EC 3.4.
- Preferred proteases are further classified as aminopeptidases (EC 3.4.11 ), dipeptidases (EC 3.4.13), dipeptidyl-peptidases and tripeptidyl-peptidases (EC 3.4.14), peptidyl-dipeptidases (EC 3.4.15), serine-type carboxypeptidases (EC 3.4.16), metallocarboxypeptidases (EC 3.4.17), cysteine-type carboxypeptidases (EC 3.4.18), omega peptidases (EC 3.4.19), serine endopep- tidases (EC 3.4.21 ), cysteine endopeptidases (EC 3.4.22), aspartic endopeptidases (EC 3.4.23), metallo-endopeptidases (EC 3.4.24), threonine endopeptidases (EC 3.4.25), endopep tidases of unknown catalytic mechanism (EC 3.4.99).
- aminopeptidases EC 3.4.11
- protease in the context of the present invention may be an endopeptidase of any kind or a mixture of endopeptidases of any kind.
- protease according to the invention is selected from serine protease (EC 3.4.21).
- Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction.
- a ser ine protease according to the invention is selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71 ), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21 .79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118, or EC 3.4.21.119,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5,) and subtilisin (also known as subtilopeptidase, e.g., EC 3.4.21.62), the latter hereinafter also being referred to as“subtilisin”.
- protease activity In general, the three main types of protease activity (proteolytic activity) are: trypsin-like, where there is cleavage of amide substrates following Arg (N) or Lys (K) at P1 , chymotrypsin-like where cleavage occurs following one of the hydrophobic amino acids at P1 , and elastase-like with cleavage following an Ala (A) at P1.
- subtilases A sub-group of the serine proteases tentatively designated subtilases has been proposed by Siezen et al. (1991), Protein Eng. 4:719-737 and Siezen et al. (1997), Protein Science 6:501 - 523. They are defined by homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases. A subtilisin was previously often defined as a serine protease produced by Gram-positive bacteria or fungi, and according to Siezen et al. now is a subgroup of the subtilases. A wide variety of subtilases have been identified, and the amino acid sequence of a number of subtilases has been determined. For a more detailed description of such subtilases and their amino acid sequences reference is made to Siezen et al. (1997), Protein Science 6:501 -523.
- the subtilases may be divided into 6 sub-divisions, i.e. the subtilisin family, thermitase family, the proteinase K family, the lantibiotic peptidase family, the kexin family and the pyrolysin family.
- subtilisins which are serine proteases from the family S8 as defined by the MEROPS database (http://merops.sanger.ac.uk).
- Peptidase family S8 con tains the serine endopeptidase subtilisin and its homologues.
- subfamily S8A the active site residues frequently occurs in the motifs Asp-Thr/Ser-Gly (which is similar to the sequence motif in families of aspartic endopeptidases in clan AA), His-Gly-Thr-His and Gly-Thr-Ser-Met-Ala- Xaa-Pro.
- Most members of the family are active at neutral-mildly alkali pH.
- Many peptidases in the family are thermostable.
- Casein is often used as a protein substrate and a typical synthetic substrate is Suc-Ala-Ala-Pro-Phe-NHPhN02.
- Prominent members of family S8, subfamily A are:
- subtilisin related class of serine proteases shares a common amino acid sequence defining a catalytic triad which distinguishes them from the chymotrypsin related class of serine proteases.
- subtilisin In the subtilisin related proteases the relative order of these amino acids, reading from the amino to carboxy-terminus is aspartate-histidine-serine. In the chymotrypsin related proteases the relative order, however is histidine-aspartate-serine.
- subtilisin herein refers to a serine protease having the catalytic triad of subtilisin related proteases. Examples include the subtilisins as described in WO 89/06276 and EP 0283075, WO 89/06279, WO 89/09830, WO 89/09819, WO 91/06637 and WO 91/02792.
- Parent proteases of the subtilisin type (EC 3.4.21.62) and variants may be bacterial proteases.
- Said bacterial protease may be a Gram-positive bacterial polypeptide such as a Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacitius, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. co/i, Flavobacterium, Fusobacterium, Helicobacter, Hyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaptasma protease.
- protease enzymes include those sold under the trade names Alcalase®, Blaze®, DuralaseTM, DurazymTM, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Pri- mase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Co- ronase® Ultra, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect® Prime, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Ultimase®, Opticlean®, Effectenz®, Preferenz® and Optimase®
- the parent enzymes and variants may be a Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circuians, Bacillus c/ausii, Bacillus coagu- lans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus Hcheniformis, Bacillus megaterium, Bacillus pumiius, Bacillus sphaericus , Bacillus stearothermophilus, Bacil lus subti!is, or Bacillus thuringiensis protease.
- subtilase is selected from the following:
- subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. Volume 159, p. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 1 1 , p. 791 1-7925),
- subtilisin from Bacillus Hcheniformis subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191 , and Jacobs et al. (1985) in Nucl. Ac- ids Res, Vol 13, p. 8913-8926),
- subtilisin PB92 original sequence of the alkaline protease PB92 is described in EP 283075 A2)
- subtilisin 147 and/or 309 (Esperase®, Savinase®) as disclosed in GB 1243784, subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus
- subtilisin from Bacillus gibsonii ⁇ DSM 14391 as disclosed in WO 2003/054184, subtilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003/056017,
- subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003/055974,
- subtilisin having SEQ ID NO: 4 as described in WO 2005/063974 or a subtilisin which is at least 40% identical thereto and having proteolytic activity,
- subtilisin having SEQ ID NO: 4 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity
- subtilisin having SEQ ID NO: 7 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity
- subtilisin having SEQ ID NO: 2 as described in application DE 102005028295.4 or subtil isin which is this at least 66% identical thereto and having proteolytic activity.
- Examples of useful proteases in accordance with the present invention comprise the variants described in: WO 92/19729, WO 95/23221 , WO 96/34946, WO 98/20115, WO 98/20116, WO 99/1 1768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 201 1/036263, WO 2011/036264, and WO 201 1/072099.
- Suitable exam ples comprise especially protease variants of subtilisin protease derived from SEQ ID NO:22 as described in EP 1921 147 (which is the sequence of mature alkaline protease from Bacillus len tus DSM 5483) with amino acid substitutions in one or more of the following positions: 3, 4, 9,
- subtilisin protease is not mutated at positions Asp32, His64 and Ser221 (according to BPN’ numbering).
- the subtilisin has SEQ ID NO:22 as described in EP 1921 147, or a subtilisin which is at least 80% identical thereto and has proteolytic activity.
- a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is charac terized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity.
- subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by having amino acid glutamic acid (E), or aspartic acid (D), at position 101 (according to BPN’ numbering) and has proteolytic activity.
- Such a subtilisin variant may comprise an amino acid substitution at position 101 , such as R101 E or R101 D, alone or in combination with one or more substitutions at positions 3, 4, 9, 15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 131 , 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and/or 274 (according to BPN’ numbering) and has proteolytic activity.
- a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising at least the following amino acids (according to BPN’ numbering) and has proteolytic activity:
- a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising one amino acid (according to (a)-(h)) or combinations according to (i) together with the amino acid 101 E, 101 D, 101 N, 101 Q, 101 A, 101 G, or 101 S (according to BPN’ numbering) and has proteolytic activity.
- a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and is characterized by comprising the mutation (according to BPN’ numbering) R101 E, or S3T + V4I + V205I, or S3T + V4I + V199M + V205I + L217D, and has proteolytic activity.
- the subtilisin comprises an amino acid sequence having at least 80% identity to SEQ ID NO:22 as described in EP 1921147 and being further characterized by com prising R101 E and S3T, V4I, and V205I (according to the BPN’ numbering) and has proteolytic activity.
- a subtilisin comprises an amino acid sequence having at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and being further characterized by comprising R101 E, and one or more substitutions selected from the group consisting of S156D, L262E, Q137H, S3T, R45E,D,Q, P55N, T58W,Y,L, Q59D,M,N,T, G61 D,R, S87E, G97S, A98D,E,R, S106A,W, N1 17E, H120V,D,K,N, S125M, P129D, E136Q, S144W, S161 T,
- subtilisin variant enzymes as disclosed above which are at least n% identical to the respective parent sequences include variants with n being at least 40 to 100.
- subtilisin variants in one embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme.
- subtilisin variants comprising conservative mu tations not pertaining the functional domain of the respective subtilisin protease.
- subtilisin variants of this embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
- proteolytic activity or “protease activity” or“proteolytic activity”.
- This property is related to hydrolytic activity of a pro- tease (proteolysis, which means hydrolysis of peptide bonds linking amino acids together in a polypeptide chain) on protein containing substrates, e.g. casein, haemoglobin and BSA.
- proteolytic activity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a defined course of time.
- the methods for analyzing proteolytic activity are well-known in the literature (see e.g. Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381 - 395).
- proteolytic activity as such can be determined by using Succinyl-Ala- Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate.
- pNA is cleaved from the substrate molecule by proteo- lytic cleavage, resulting in release of yellow color of free pNA which can be quantified by meas- uring OD405.
- Other methods are known to those skilled in the art.
- Protease variants may have proteolytic activity according to the present invention when said protease variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the proteolytic activity of the respective parent protease.
- the pi value (isoelectric point) of the subtilisin protease is between pH 7.0 and pH 10.0, preferably between pH 8.0 and pH 9.5.
- the water-soluble multilayer film of the invention comprises at least one amylase.“Amylases” according to the invention (alpha and/or beta) include those of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively). Chemically modified or protein engineered mutants are included.
- amylase enzymes include but are not limited to those sold under the trade names DuramylTM, TermamylTM, FungamylTM, StainzymeTM, Stainzyme PlusTM, Natala- seTM, Liquozyme X and BANTM (from Novozymes A/S), and RapidaseTM, PurastarTM,
- amylase is a parent or variant enzyme which is selected from the following:
- Suitable variants are those which are at least 90% identical to SEQ ID NO: 2 as described in WO 95/10603 and/or comprising one or more substitutions in the following positions:
- Suitable variants of SEQ ID NO:6 include those which is at least 90% identical thereto and/or further comprise a deletion in positions 181 and/or 182 and/or a substitution in position 193.
- Suitable amylases are comprising amino acids 1 to 485 of SEQ ID NO:2 as described in WO 00/60060 or amylases comprising an amino acid sequence which is at least 96% identical with amino acids 1 to 485 of SEQ ID NO:2 which have amylolytic activity.
- Suitable amylases are those having SEQ ID NO: 12 as described in WO 2006/002643 or amylases having at least 80% identity thereto and have amylolytic activity.
- Suitable amylases include those having at least 80% identity compared to SEQ ID NO:12 and/or comprising the substitutions at positions Y295F and M202LITV and have amylolytic activity.
- Suitable amylases include those having SEQ ID NO:6 as described in WO 2011/098531 or am ylases having at least 80% identity thereto having amylolytic activity. Suitable amylases include those having at least 80% identity compared to SEQ ID NO:6 and/or comprising a substitution at one or more positions selected from the group consisting of 193 [G,A,S,T or M], 195
- Suitable amylases are those having SEQ ID NO:1 as described in WO 2013/001078 or amylas es having at least 85% identity thereto having amylolytic activity.
- Suitable amylases include those having at least 85% identity compared to SEQ ID NO:1 and/or comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 and having amylolytic activity.
- amylases are those having SEQ ID NO:2 as described in WO 2013/001087 or amylases having at least 85% identity thereto and having amylolytic activity.
- Suitable amylases include those having at least 85% identity compared to SEQ ID NO:2 and/or comprising a dele- tion of positions 181 +182, or 182+183, or 183+184, which have amylolytic activity.
- Suitable am ylases include those having at least 85% identity compared to SEQ ID NO:2 and/or comprising a deletion of positions 181 +182, or 182+183, or 183+184, which comprise one or two or more modifications in any of positions corresponding to W140, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476 and G477 and have amylolytic activity.
- Amylases also include hybrid a-amylase from above mentioned amylases as for example as described in WO 2006/066594.
- Suitable amylases include also those which are variants of the above described amylases which have amylolytic activity.
- amylase variants in one embodiment may be those which are least 40 to 100% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
- amylase variants having amylolytic activity may be at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
- amylase variants comprising conservative mutations not pertaining the functional domain of the respective amylase.
- amylase variants in this embodiment may be amylases have amylolytic activity which may be least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
- Amylases according to the invention have“amylolytic activity” or“amylase activity” according to the invention involves (endo)hydrolysis of glucosidic linkages in polysaccharides
- a-amylase activity may be determined by assays for measurement of a-amylase activity which are known to those skilled in the art. Examples for assays measuring a-amylase activity are: a-amylase activity can be determined by a method employing Phadebas tablets as substrate (Phadebas Amylase Test, supplied by Magle Life Science). Starch is hydrolyzed by the a- amylase giving soluble blue fragments.
- the absorbance of the resulting blue solution, measured spectrophotometrically at 620 nm, is a function of the a-amylase activity.
- the measured absorbance is directly proportional to the specific activity (activity/mg of pure a-amylase protein) of the a-amylase in question under the given set of conditions.
- a-amylase activity can also be determined by a method employing the Ethyliden-4-nitrophenyl- a-D-maltoheptaosid (EPS).
- EPS Ethyliden-4-nitrophenyl- a-D-maltoheptaosid
- D-maltoheptaoside is a blocked oligosaccharide which can be cleaved by an endo-amylase.
- kits containing EPS substrate and a- glucosidase is manufactured by Roche Costum Biotech (cat. No. 10880078103).
- the slope of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the a-amylase in question under the given set of conditions.
- Amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the amylolytic activity of the respective parent amylase.
- the water-soluble multilayer film of the invention comprises at least one perhydrolase.
- Suitable“perhydrolases” are capable of catalyzing a perhydrolysis reaction that results in the production of a peracid from a carboxylic acid ester (acyl) substrate in the pres ence of a source of peroxygen (e.g., hydrogen peroxide). While many enzymes perform this reaction at low levels, perhydrolases exhibit a high perhydrolysis:hydrolysis ratio, often greater than 1.
- Suitable perhydrolases may be of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
- useful perhydrolases include naturally occurring Mycobacterium perhydrolase enzymes, or variants thereof.
- An exemplary enzyme is derived from Mycobacterium smegmatis. Such enzyme, its enzymatic properties, its structure, and variants thereof, are described in WO 2005/056782, WO 2008/063400, US 2008145353, and US 2007167344.
- the water-soluble multilayer film of the invention comprises at least one mannanase.
- “Mannanase” may be an alkaline mannanase of Family 5 or 26. It may be a wild- type from Bacillus or Humicoia, particularly B. agaradhaerens, B. Hcheniformis, B. haiodurans,
- Mannaway® Novozymes AIS
- the water-soluble multilayer film of the invention comprises at least one peroxidase and/or oxidase.
- Suitable peroxidases and oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
- An oxidase according to the invention include, in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1 .10.3.1 ), an o-aminophenol oxidase (EC 1 .10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
- a catechol oxidase EC 1 .10.3.1
- an o-aminophenol oxidase EC 1 .10.3.4
- a bilirubin oxidase EC 1.3.3.5
- Preferred laccase enzymes are enzymes of microbial origin.
- the enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g. N. crassa, Podospora, Botrytis, Collybia, Fames , Lentinus, P/eurotus, Tra metes, e.g. T. villosa and T. versicolor, Rhi- zoctonia, e.g. R. so!ani, Coprinopsis, e.g. C. cinerea, C. comatus, C. friesii, and C.
- a laccase may be derived from Coprinopsis or Myceliophthora.
- a laccase is derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora ther- mophiia, as disclosed in WO 95/33836.
- the laccase may be a bacterial laccase, e.g. the laccase may be a Gram positive bacterial pol ypeptide such as a Bacillus, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, or OceanobaciHus laccase, or a Gram negative bacterial polypeptide such as an E. coH, Pseudomonas, Salmonella, Campylobacter, Heli cobacter, Fiavobacterium, Fusobacterium, Hyobacter, Neisseria, or Ureap!asma laccase.
- a Gram positive bacterial pol ypeptide such as a Bacillus, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, or OceanobaciHus laccase
- laccase is selected from those as described in SEQ ID NO: 2, 4, 6, and 8 of WO 2009/127702 and variants thereof.
- laccase activity is defined herein as covered by enzyme classification EC 1 .10.3.2, or a similar activity, such as a catechol oxidase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen.
- enzyme classification EC 1 .10.3.2 or a similar activity, such as a catechol oxidase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen.
- “Laccase activity” is determined by oxidation of syringaldazin under aerobic conditions. The violet colour produced is measured at 530 nm. The analytical conditions are 19 mM syringaldazin, 23 mM Tris/maleate buffer, pH 7.5, 30°C, and 1 min reaction time.
- Oxidases and their corresponding substrates may be used as hydrogen peroxide generating enzyme systems, and thus a source of hydrogen peroxide.
- enzymes such as pe- roxidases, haloperoxidases and perhydrolases, require a source of hydrogen peroxide.
- Peroxidases utilize hydrogen peroxide as substrate.
- useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, WO 98/10060 and WO 98/15257.
- peroxidases include GuardzymeTM (Novozymes A/S), PrimaGreenTM
- Peroxidase activity may be measured by the ABTS method as described in Childs et al. 1975 (Biochemical J, 145, p. 93-103) and commercial kits are available from different suppliers. Other measuring methods are known to those known in the art.
- a peroxidase for use in the invention also include a haloperoxidase enzyme, such as chlo- roperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxi- dase activity.
- haloperoxidases are classified according to their specificity for halide ions. Chlo- roperoxidases (E.C. 1.1 1.1.10) catalyze formation of hypochlorite from chloride ions.
- the haloperoxidase is a chloroperoxidase. In one embodiment, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. In one embodiment of the present invention the vanadate-containing haloperoxidase is combined with a source of chloride ion.
- Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caidariomyces, e.g., C. fumago, Aiternaria, Cur- vularia, e.g., C. verrucuiosa and C. inaequa/is, Drechslera, Ulocladium and Botrytis.
- Haloperox idases have also been isolated from bacteria such as Pseudomonas , e.g. P. pyrrocinia, and Streptomyces, e.g. S. aureofaciens.
- the haloperoxidase is from Curvularia sp., in particular Curvularia verrucu- losa or Curvularia inaequaiis, such as C. inaequa/is CBS 102.42 as described in WO 95/27046; or C. verrucuiosa CBS 147.63 or C.
- the water-soluble multilayer film of the invention comprises at least one lyase.“Lyase” may be a pectate lyase derived from Bacillus, particularly B. iicheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084, WO 2002/006442, WO 2002/092741 , WO 2003/095638.
- lyase may be a pectate lyase derived from Bacillus, particularly B. iicheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084, WO 2002/006442, WO 2002/092741 , WO 2003/095638.
- pectate lyases are XpectTM, PectawashTM and PectawayTM (Novozymes A/S); PrimaGreenTM, EcoScour (DuPont).
- the water-soluble multilayer film of the invention comprises at least one enzyme selected from the group of pectinases, and/or arabinases, and/or galactanases, and/or xylanases.
- Suitable pectinases, and/or arabinases, and/or galactanases, and/or xylanases are known to those skilled in the art.
- Nuclease (EC 3.1.21.1 ) also known as Deoxyribonuclease I, or DNase preforms endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
- Nuclease enzymes have been described in patents and published patent applications including, but not limited to: US3451935, GB1300596, DE10304331 , WO2015155350, WO2015155351 , WO2015166075, WO2015181287, and WO2015181286.
- Oxo alcohol and water were initially charged and the initial charge was heated to 75 ° C with stirring at 100 rpm.
- the feeds 1 , 2 and 3 were then added in 4 hours and the reaction mixture was polymerized for an additional hour. Then the mixture was allowed to cool to room temperature.
- the polymer composition was obtained in the form of a transparent and viscous solution. 100 g of the polymer composition was heated to 80°C. After adding 4.2 g of glycerol, the concentration of the polymer composition was diluted to 65% wt% with deionized water. The appli- cation solution was well mixed and tempered at 80°C until the stirred-in air had completely escaped.
- Time 0 of the shelf life aging tests is the instant when the enzyme containing polymer solution is prepared.
- Film sample preparation coating and dry ing at room temperature and humidity typically takes 1 -2 days with subsequent enzyme activity determination by protease or lipase assay.
- protease acitivty was determined using Succinyl - Ala - Ala - Pro - Phe - p-Nitroanilide (Suc-AAPF-pNA, short : AAPF) as substrate.
- pNA is cleaved from the substrate molecule at 30°C, pH 8.6 TRIS buffer.
- the rate of cleavage can be determined by the increase of the yellow color of free pNA in the solution by measuring OD405, the optical density at 405 nm.
- Lipase activity is determined by a method employing para Nitrophenol-valerate (pNP-C5). Fol- lowing cleavage, a free pNP molecule is liberated with an absorption increase that can be moni tored at a wavelength of 405 nm.
- the sample to be analyzed is diluted in residual activity buffer (100 mM Tris pH 8.0, 2% w/w Arabic gum, 0.01 % Triton X100). The dilution is as such that the final dilution is in the linear range of the assay.
- the slope (absorbance increase at 405 nm per minute) of the time dependent absorption-curve is directly proportional to the activity of the lipase.
- the enzyme activity in films has been determined by adding a solid piece of film into a microtiter plate. Activity evolution in aging tests at 37°C is measured during film dissolution over a period of time (typically 15min) until the activity value has reached a constant value. Activies might spread (100% plus, minus 10%) due to residual moisture in the films which impact the activity values of sample amounts determined gravimetrically .
- Example 1 Preparation of protease and amylase containing films based on the color transfer inhibitor polymer Sokalan HP56 (BASF SE) (application solution B):
- an automatic film applicator and a universal applicator from Zehntner were used.
- the application solution B was applied to a PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
- the gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
- Table 2 Change of normalized protease and amylase activity over time in single layer film based on color transfer inhibitor polymer stored at 37°C conditions:
- Example 2 Preparation of protease and lipase containing single layer films based on PVOH and glycerol (application solution A4):
- an automatic film applicator and a universal applicator from Zehntner were used.
- the application solution A4 was applied to a PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
- the gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
- Example 3 Preparation of 2-layer films containing a lipase top-layer on a layer comprising both protease and amylase based on PVOH, propane-1 ,2-diol and glycerol (application solution A1 & A2):
- an automatic film applicator and a universal applicator from Zehntner were used.
- the application solution A2 was applied to a PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
- the gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
- the application solution A1 was applied.
- the gap width of the doctor blade was adjusted so that after drying at room temperature, the total layer thickness of the film is 40 pm.
- Example 4 Preparation of 3-layer films containing wash active polymer composition as adhesion layer in-between lipase top-layer and the combination of protease and amylase as bottom- layer based on PVOH, propane-1 ,2-diol and glycerol (application solution A1 & A3):
- an automatic film applicator and a universal applicator from Zehntner were used.
- the application solution A2 was applied to a first PET substrate (Hostaph an ® , Mitsubishi Polyester Film).
- the gap width of the doctor blade was chosen so that the layer 1 after drying at room temperature has a thickness of 30 pm.
- the application solution C of the wash active polymer composition heated to 80°C was applied.
- the gap width of the doctor blade was adjusted so that after drying at room temperature, the total layer thick ness of the first film comprising layer 1 and 2 is 110 pm.
- the application solution A1 was applied on a second PET substrate (Hostaphan ® , Mitsubishi Polyester Film).
- Table 4 Change of normalized protease and amylase activity over time in layer 1 stored at 37°C conditions:
- Table 5 Change of normalized lipase activity over time in layer 3 stored at 37°C conditions:
- wash performance tests have been conducted.
- the films were stored for 8 weeks at 37 °C in a heating cabinet.
- the wash performance of the films was determined directly and after 2, 6 and 8 weeks.
- the different enzymes had to be tested on varying stains.
- test fabric was washed at 25°C in the presence of cotton ballast fabric with addition of the film. After the wash cycle, the test fabric was rinsed, spun and dried. In order to determine the washing effect, the L * , a * and b * values of the test fabric were determined by photometry before and after the wash cycle. The values for the protease and amylase relevant stains were determined with a Datacolor (Elrepho 2000) photometer. The values for the lipase relevant stains were determind by MACH 5. The Delta E values were calculated from the L * , a * and b * values before and after wash.
- Protease and amylase embedded in the film are stable over 8 weeks stored at 37 °C
- Table C Wash result for wash active polymer composition layer 2 and layer 3 containing li pase, stored at 37°C and washed in formulation 2 at 25 °C on a multi stain set (sum of delta E values)
- the examples show that in case of the combination of protease and lipase, it is not possible to embed both incompatible enzymes (example 2) in different layers of a 2-layer film, since during film manufacturing of subsequent coating and drying the bottom enzyme migrates into the top layer (example 3).
- both enzyme containing layers are laminated with each other.
- the properties of the wash active polymer composition layer matches exactly with requirements for an adhesive layer and makes a lamination process feasible. By this process, including the wash active polymer composition layer as an adhesive interlayer in-between both enzyme layers mi- gration processes are prevented and enzyme activity of the individual layers is preserved (ex ample 4).
- wash performance tests show that the demonstrated wash active multilayer films not only exhibit enzyme activity but also provide additional wash performance if such films are used in addition to typical liquid detergent pouch formulation (example 4).
- the wash tests show the enzymes embedded in the film exhibit a very high storage stability.
- a water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1 ) obtainable by physical blending of a at least one polymer PT) and at least one polyether component PE), or free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically un saturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic ac ids and mixtures thereof, in the presence of at least one polyether component PE), select ed from polyether alcohols with a number average molecular weight Mn of at least 200 g/mol, mono and di-(Ci to C 6 -alkyl)ethers of such polyether alcohols, polyether groups- containing surfactants or mixtures thereof, and/or
- a water-soluble multilayer film according to item 1 wherein the film comprises at least one layer comprising or consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
- the enzyme EN is selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
- a water-soluble multilayer film according to any one of items 1 to 8, wherein at least one layer contains protease as enzyme EN1 ), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
- Water soluble multilayer film according to any one of items 1 to 10, derived from a wash active layer based on a at least one polymer chosen from P2, preferred a polymer blend, more preferred chosen from polymer composition P 1 , which is used as adhesion layer in- between two enzyme containing layers, optionally in a lamination process.
- homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
- homo- and copolymers comprising at least one copolymerized monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole,
- homo- and copolymers of acrylic acid and/or methacrylic acid especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
- copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least one copolymerized hydrophobic monomer selected from Ci-Cs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
- copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C 2 -C 8 olefin,
- polyalkylene glycols mono- or diethers of polyalkylene glycols
- multifunctional alkoxylated diamines preferably alkoxylated diamines with 2 to 10 methylene groups
- cellulose derivatives preferably cellulose ethers, cellulose esters, carboxyalkyl cellu- loses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
- amphoteric modified starch and
- a first free-flowing composition capable of film formation is applied to a carrier material to obtain a first layer
- the first layer applied to the carrier material is optionally subjected to an increase in viscosity
- a second free-flowing composition capable of film formation is applied to the first layer obtained in step i1 ) or in step i2) to obtain a second layer
- the second layer is optionally subjected to an increase in viscosity
- step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to re peat steps i3) and i4) once or more than once,
- the layers applied to the carrier material are optionally subjected to a further in crease in viscosity
- the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing compositions each comprise a component which is ca pable of film formation and is independently selected from at least one polymer composition P1 ), at least one polymer P2) or a mixture thereof, and with the proviso that at least one of the free-flowing compositions and/or the carrier material comprises or consists of a polymer composition P 1 ) as defined in any of the preceding claims,
- Washing composition comprising a multilayer film according to any of items 1 to 13 or obtainable by a process as defined in item 14.
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Abstract
The present invention relates to water-soluble multilayer films containing wash active chemicals and enzymes, their production and use.
Description
Water soluble multilayer films containing wash active chemicals and enzymes
The present invention relates to water soluble multilayer films containing wash active chemicals and enzymes, their production and use.
Multilayer films, for example wash active films, as described for example in unpublished patent applications PCT/EP2017/083133 and PCT/EP2017/083127, usually comprise acidic compo- nents (as mentioned in US 20160369210 A1 ).
The wash active films described in the above publications, due to their acidic nature, offer an environment which is not suitable for enzyme integration into such films.
However, laundry products usually comprise enzymes, in order to enhance washing perfor- mance. In addition, laundry products have to withstand considerable storage periods (for example when a laundry product is stored in a supermarket, and subsequently in the home of a consumer), under variable storage conditions, for example varying temperatures and humidities.
Previous efforts are described in the following publications.
WO2013/148492: Use of enzymes for preparing water-soluble films, enzymes+polyol for preparation of water soluble film containing PVA, PEO, glycerol, MPG, CaCh, protease; film used for unit dose products
W014152547: Detergent pouch with enzymatic water-soluble film, enzyme in the film is different from enzyme in the detergent (protease or lipase in film); architecture of pouch film, compartments and ingredients; several layers are described having or not having enzyme for pro tecting enzyme from detergent
W014186464: Stabilized Lipase in water soluble aims, water-soluble film containing lipase (sequence claimed); lipase in in solid, particulate form; film comprises 35-90% PVA with 75-99% degree of hydrolysis and 10-50% polyols; use of film for preparing a detergent unit dose product
It becomes clear that the aim of stable incorporation of at least one enzyme into a wash active film has not been achieved yet.
Moreover, the incorporation of two or more enzymes into a multilayer film (for example a wash active multilayer film) may present additional challenges, since some enzymes are incompatible with each other.
Incompatible in the sense that the enzymes used within a single layer are harmful to each other, such that their wash activity is hampered (enzyme-enzyme incompatibility or enzyme- polymer/surfactant incompatibility), and/or in the sense that the resulting film/layer is not optically clear/transparent due to poor mixing behavior (polymer-polymer phase separation, polymer- surfactant phase separation, precipitation or salt formation in the transition from solution to dry film).
For example, when incorporating protease, problems with the stability of other enzymes (or even with the stability of protease itself) arise (or in general in the case of incompatible en zymes). According to the state of the art, in case of using protease and at least one different enzyme, such as amylase, it becomes necessary to include a protease inhibitor in order to prevent rapid decomposition of the different enzyme, (see EP2799533, W014152674) This may hold true also in case of protease alone, which also decomposes itself, in the presence of water, in particular at relatively high mass fractions of protease.
This is, for example, described in WO 14152674, where a water-soluble film containing protease and a protease inhibitor is disclosed.
In general, protease inhibitors inhibit protease’s proteolytic activity, such that protease is prevented from decomposing proteins, like for example other enzymes (and itself).
Common protease inhibitors include boron-containing compounds. Suitable boron-containing compounds are selected from boric acid or its derivatives and from boronic acid or its derivatives such as aryl boronic acids or its derivatives, from salts thereof, and from mixtures thereof. Furthermore, peptide aldehydes like di-, tri- or tetrapeptide aldehydes or aldehyde analogues may also be used to inhibit protease.
There was therefore a need in the art to find a way to incorporate enzymes, preferably at least two enzymes, into water-soluble multilayer films, for example wash active films, without negative impacts on enzyme stability.
Furthermore, it would be desirable to get rid of protease inhibitors in the multilayer film, since protease inhibitors, for example boron-containing compounds as mentioned above, lead to environmental stress and are costly.
Thus, an object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage.
Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least two enzymes, preferably two en zymes incompatible with each other, wherein the enzymes should be stable on storage.
Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing protease and at least one further enzyme, wherein the enzymes should be stable on storage.
Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing protease and at least one further enzyme, wherein the enzymes should be stable on storage, and wherein it is possible to refrain from using a protease inhibitor.Furthermore, an object of the present invention was to provide a water- soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least
one enzyme, wherein the enzyme should be stable on storage, and wherein at least one of the films would be wash active in itself (so that additional cost and environmental stress by adding another wash-active layer can be avoided).
Another object of the present invention was to provide a water-soluble multilayer film, preferably a wash and cleaning active multilayer film, containing at least one enzyme, wherein the enzyme should be stable on storage and wherein the washing and/or cleaning performance should be at least stable compared to a comparable wash and cleaning active multilayer film without any enzyme, preferably improved compared to a comparable wash and cleaning active multilayer film without any enzyme.
Another object of the present invention was to provide a process for manufacturing a water- soluble multilayer film, preferably a wash and cleaning active multilayer film, as described above and below.
The inventors of this invention have now surprisingly found that the problems mentioned above can be solved by multilayer film architecture (two or more layers), wherein non-acidic layers are carrying enzymes.
In addition, the newly found multilayer concept allows for the separation of incompatible en zymes from each other, for example separation of protease and enzymes that suffer under the presence of protease, such as lipase, into at least two discrete layers, making protease inhibi tors unnecessary.
In a preferred embodiment, at least two enzymes incompatible with each other are incorporated into two discrete layers, and in addition, the two discrete layers are spatially separated by a fur ther layer devoid of any enzyme.
In the context of the present invention, the term“polymer film” refers to a flat structure which has an essentially two-dimensional extension. The thickness of the films according to the inven tion is preferably 0.5 pm to 20 mm, particularly preferably 1 pm to 10 mm. The thickness of the polymer films of the invention is small in relation to the length and width. Preferably, the thick ness of the polymer films is smaller by a factor of at least 2, more preferably of at least 5 and especially of at least 10 than the length of the greatest longitudinal axis. In a specific embodi ment, the thickness of the polymer films is smaller by a factor of at least 20, more specifically at least 50, even more specifically at least 100 and very specifically at least 500 than the length of the greatest longitudinal axis. In principle, the upper value for the greatest longitudinal extent of the polymer films of the invention is uncritical. The polymer films of the invention can be pro- duced, for example, in the form of film rolls, where the greatest length may even be in the region of 100 m or higher.
The polymer films of the invention can be in form of single layer films or multilayer films.
The term“multi-layered film” in connection with the present invention defines a self-supporting planar construction which comprises at least two film layers. A multi-layered film according to
the present invention is a film composite which comprises at least two films which are perma- nently connected with a substantial part of their surface over its entire surface. Thereby, it is understood that at least two films are permanently connected with at least 50% of their surface over its entire surface. If two films of different sizes are connected to each other, at least the film with the smaller surface is permanently connected over its entire surface to at least 50% of its surface. Thus the multi-layered films used in the process of the present invention differ from films used for the production of water-soluble container known in the art in which a single film or two or more films are connected by means of a seal seam. Those films known in the art are only connected over their entire surfaces to not more than 50% of their surfaces.
Since it is desirable that the overall film thickness be comparable to state of the art polyvinyl alcohol (PVA) films for unit dose pod/pouch fabrication process reasons, the thickness of enzyme containing layers is usually below that of today’s single layer PVA films. Due to this reduced enzyme formulation space, the enzyme concentration in the film needs to be higher compared to state of the art. Approaches as described by Monosol/Novozymes, e. g. in W013/148492 or W014/186464, cause additional challenges to enzyme stability.
In general, the resulting enzyme containing wash active multilayer films shows better wash performance than enzyme containing PVOH films according to the state of the art, due to the additional wash active polymers which could not be formulated into the liquid detergent up to now (e.g. poly acrylic acid).
Thus, in one aspect, the present invention is directed at a water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1) obtainable by physical blending of at least one polymer P1 ') obtainable by by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A‘) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, and at least one polyether component PE), or by free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically unsaturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic acids and mixtures thereof, in the presence of at least one polyether component PE), selected from polyether alcohols with a number average molecular weight Mn of at least 200 g/mol, mono and di-(Ci to C6-alkyl)ethers of such polyether alcohols, polyether groups- containing surfactants or mixtures thereof, and/or at least one layer comprising or consisting of a composition P2) selected from natural and modified polysaccharides,
homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
homo- and copolymers comprising at least one copolymerized monomer selected from N- vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, salts of the three latter monomers, vinylpyridine N-oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof,
homo- and copolymers of acrylic acid and/or methacrylic acid, especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least one copoly- merized hydrophobic monomer selected from C-i-Cs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C2-C8 olefin,
homo- and copolymers of acrylamide and/or methacrylamide,
polyamino acids,
water-soluble or water-dispersible polyamides,
polyalkylene glycols, mono- or diethers of polyalkylene glycols,
polyethylene imine alkoxylates,
multifunctional alkoxylated diamines, preferably alkoxylated diamines with 2 to 10 methylene groups,
cellulose derivatives, preferably cellulose ethers, cellulose esters, carboxyalkyl celluloses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
amphoteric modified starch, and mixtures thereof,
wherein at least two of the layers, preferably two of the layers, comprise at least one type of enzyme EN) each.
In an embodiment of the inventive multilayer film, the film comprises at least one layer compris ing or consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
Polymer P1’V
The polymer P1’) can be prepared by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A‘) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, optionally at least one monomer B’) which is selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, unsaturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures thereof, and
optionally at least one monomer C’), different from A’) and B’).
Monomer composition M’):
Monomer A’):
The monomer composition M’) used for producing the polymer P1’) comprises at least one monomer A’) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
In a specific embodiment, the monomer composition M’) consists only of a,b-ethylenically un- saturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
The a,b-ethylenically unsaturated carboxylic acid is preferably selected from acrylic acid, meth- acrylic acid, ethacrylic acid, maleic acid, fumaric acid, itaconic acid, a-chloroacrylic acid, croton- ic acid, citraconic acid, mesaconic acid, glutaconic acid and aconitic acid. Suitable salts of the aforementioned acids are, in particular, the sodium, potassium and ammonium salts, and the salts with amines. The monomers A’) can be used as such or as mixtures with one another. The stated weight fractions all refer to the acid form.
Preferably, the at least one a,b-ethylenically unsaturated carboxylic acid is used for the polymerization in non-neutralized form. If the a,b-ethylenically unsaturated carboxylic acids are used for the polymerization in partially neutralized form, then the acid groups are neutralized preferably to at most 50 mol%, particularly preferably to at most 30 mol%.
Particularly preferably, the monomer A’) is selected from acrylic acid, methacrylic acid, maleic acid, fumaric acid, itaconic acid, salts of the aforementioned carboxylic acids and mixtures thereof.
In particular, the monomer A’) is selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid and mixtures thereof.
In a specific embodiment, exclusively acrylic acid is used as monomer A’).
The monomer A’) is used preferably in an amount of from 50 to 100% by weight, particularly preferably 60 to 100% by weight, based on the total weight of the monomer composition M’).
In a preferred embodiment, the monomer composition M’) consists to at least 50% by weight, preferably to at least 80% by weight, in particular to at least 90% by weight, based on the total weight of the monomer composition M’), of acrylic acid and/or acrylic acid salts.
Monomer B’):
The monomer composition M’) can comprise, in addition to the monomers A’), at least one monomer B’) which is selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, unsaturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures there of.
The monomer B’) is preferably selected from 2-acrylamido-2-methylpropanesulfonic acid, vinyl- sulfonic acid, allylsulfonic acid, sulfoethyl acrylate, sulfoethyl methacrylate, sulfopropyl acrylate, sulfopropyl methacrylate, 2-hydroxy-3-acryloxypropylsulfonic acid, 2-hydroxy-3- methacryloxypropylsulfonic acid, styrenesulfonic acid, vinylphosphonic acid, allylphosphonic acid, salts of the aforementioned acids, and mixtures thereof.
2-Acrylamido-2-methylpropanesulfonic acid is preferred as monomer B’).
Suitable salts of the aforementioned acids are in particular the sodium, potassium and ammoni um salts, and the salts with amines. The monomers B’) can be used as such or as mixtures with one another. The stated weight fractions all refer to the acid form.
Preferably, the monomer composition M’) then consists to at least 50% by weight, particularly preferably to at least 80% by weight, in particular to at least 90% by weight, based on the total weight of the monomer composition M’), of monomers A’) and B’). If the monomer composition M’) comprises at least one monomer B’), then this is used preferably in an amount of from 0.1 to 50% by weight, particularly preferably 1 to 25% by weight, based on the total weight of the monomer composition M’).
Further monomers C’):
The monomer composition M’) can additionally comprise at least one further monomer different from the monomers containing acid groups and salts thereof.
Preferably, the monomer composition M’) additionally comprises at least one comonomer C’) selected from
C1’) nitrogen heterocycles with a free-radically polymerizable a,b-ethylenically unsaturated double bond,
C2’) monomers containing amide groups,
C3’) compounds of the general formulae (l.a’) and (l.b’)
in which
the order of the alkylene oxide units is arbitrary,
x is 0, 1 or 2,
k and I, independently of one another, are an integer from 0 to 100, where the sum of k and I is at least 2, preferably at least 5,
R1 is hydrogen or methyl,
R2 is hydrogen, C1-C4-alkyl,
and mixtures of two or more than two of the aforementioned monomers C1’) to C3’).
The monomer composition M’) can comprise the further monomers C1’) to C3’) in each case preferably in an amount of from 0 to 30% by weight, particularly preferably 0 to 20% by weight, in particular 0 to 10% by weight, based on the total weight of the monomer composition M’). If the monomer composition M’) comprises at least one monomer selected from C1’) to C3’), then in each case preferably in an amount of from 0.1 to 30% by weight, particularly preferably 1 to 20% by weight, in particular 1.5 to 10% by weight, based on the total weight of the monomer composition M’). In a specific embodiment, the monomer composition M’) comprises no further comonomers apart from the monomers A’).
Monomer C1’):
Preferred nitrogen heterocycles with a free-radically polymerizable a,b-ethylenically unsaturated double bond C1’) are selected from 1-vinylimidazole (N-vinylimidazole), vinyl- and allyl-substitu- ted nitrogen heterocycles different from 1 -vinylimidazole, and mixtures thereof.
From the amine nitrogens of the aforementioned compounds it is possible to generate charged cationic groups either by protonation with acids or by quaternization with alkylating agents. Suitable monomers C1’) are also the compounds obtained by protonation or quaternization of 1 - vinylimidazole and vinyl- and allyl-substituted nitrogen heterocycles different therefrom. Acids suitable for the protonation are e.g. carboxylic acids, such as lactic acid, or mineral acids, such as phosphoric acid, sulfuric acid and hydrochloric acid. Alkylating agents suitable for the quaternization are Ci-C4-alkyl halides or di(Ci-C4-alkyl) sulfates, such as ethyl chloride, ethyl bromide, methyl chloride, methyl bromide, dimethyl sulfate and diethyl sulfate. A protonation or quaternization can generally take place either before or after the polymerization. Preferably, a protonation or quaternization takes place after the polymerization. Examples of such charged monomers C1’) are quaternized vinylimidazoles, in particular 3-methyl-1 -vinylimidazolium chloride, methosulfate and ethosulfate.
Preferred monomers C1’) are furthermore vinyl- and allyl-substituted nitrogen heterocycles different from vinylimidazoles selected from 2-vinylpyridine, 4-vinylpyridine, 2-allylpyridine, 4-allyl- pyridine and the salts thereof obtained by protonation or by quaternization.
In particular, the monomer composition M’) comprises at least one comonomer C1’) selected from 1-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, 2-allylpyridine, 4-allylpyridine and the salts thereof obtained by protonation or by quaternization. Specifically, the monomer composition M’) comprises 1 -vinylimidazole as comonomer C1’).
Monomer C2’):
in which
one of the radicals R3 to R5 is a group of the formula CH2=CR6- where R6 = H or CrC4-alkyl and the other radicals R6 to R8, independently of one another, are H or C-i-Cz-alkyl,
where R3 and R4, together with the amide group to which they are bonded, can also be a lactam having 5 to 8 ring atoms,
where R4 and R5, together with the nitrogen atom to which they are bonded, can also be a five- to seven-membered heterocycle.
Preferably, the monomers C2’) are selected from primary amides of a,b-ethylenically unsaturat ed monocarboxylic acids, N-vinylamides of saturated monocarboxylic acids, N-vinyllactams, N-alkyl- and N,N-dialkylamides, a,b-ethylenically unsaturated monocarboxylic acids and mixtures thereof.
Preferred monomers C2’) are N-vinyllactams and derivatives thereof, which can have, e.g., one or more C1-C6-alkyl substituents, such as methyl, ethyl, n-propyl, isopropyl, n-butyl, sec-butyl, tert-butyl, etc. These include, e.g., N-vinylpyrrolidone, N-vinylpiperidone, N-vinylcaprolactam, N-vinyl-5-methyl-2-pyrrolidone, N-vinyl-5-ethyl-2-pyrrolidone, N-vinyl-6-methyl-2-piperidone, N-vinyl-6-ethyl-2-piperidone, N-vinyl-7-methyl-2 -caprolactam and N-vinyl-7-ethyl-2-caprolactam.
Particular preference is given to using N-vinylpyrrolidone and/or N-vinylcaprolactam.
Suitable monomers C2’) are furthermore acrylamide and methacrylamide.
N-Alkyl- and N,N-dialkylamides of a,b-ethylenically unsaturated monocarboxylic acids suitable as monomers C2’) are, for example, methyl(meth)acrylamide, methylethacrylamide, ethyl(meth)acrylamide, ethylethacrylamide, n-propyl(meth)acrylamide, isopropyl(meth)acryl- amide, n-butyl(meth)acrylamide, tert-butyl(meth)acrylamide, tert-butylethacrylamide, and mixtures thereof.
Open-chain N-vinylamide compounds suitable as monomers C2’) are, for example, N-vinylfor- mamide, N-vinyl-N-methylformamide, N-vinylacetamide, N-vinyl-N-methylacetamide, N-vinyl-N- ethylacetamide, N-vinylpropionamide, N-vinyl-N-methylpropionamide, N-vinylbutyramide and mixtures thereof. Preference is given to using N-vinylformamide.
Ether-group-containing monomer C3’):
The monomer composition M’) can additionally comprise at least one monomer C3’) selected from compounds of the general formulae (I. a) and (l.b), as defined above.
In the formulae I. a) and l.b), k is preferably an integer from 1 to 100, particularly preferably 2 to 50, in particular 3 to 30. Preferably, I is an integer from 0 to 50.
Preferably, R2 in the formulae I. a) and l.b) is hydrogen, methyl, ethyl, n-propyl, isopropyl, n- butyl, sec-butyl or tert-butyl.
In the formula l.b), x is preferably 1 or 2.
Preferably, the polymer P1’) comprises less than 15% by weight, preferably less than 10% by weight, polymerized units of monomers different from monomers A’).
The polymer P1’) is essentially uncrosslinked. The monomer composition M’) used for producing the polymer P1’) thus comprises in particular no added crosslinking monomers. In the context of the invention, crosslinking monomers are compounds with two or more than two polymerizable ethylenically unsaturated double bonds per molecule.
Specifically, the monomer composition M’) comprises, based on the total weight, less than 0.5% by weight, even more specifically less than 0.1 % by weight, of crosslinking monomers which have two or more than two free-radical ly polymerizable a,b-ethylenically unsaturated double bonds per molecule.
In a preferred embodiment, the monomer composition M’) comprises no crosslinking monomers having two or more than two polymerizable a,b-ethylenically unsaturated double bonds per molecule.
The polymer P1’) can be prepared by free-radical polymerization of a monomer composition M’). It is possible to work by any known free-radical polymerization process. In addition to polymerization in bulk, mention should be made especially of the processes of solution polymerization and emulsion polymerization, preference being given to solution polymerization.
As regards the monomer composition M’) used for the preparation of P1’), reference is made to the aforementioned suitable and preferred monomers in their entirety.
The polymerization is preferably performed in water as a solvent. However, it can also be undertaken in alcoholic solvents, especially Ci-C4-alcohols, such as methanol, ethanol and isopropanol, or mixtures of these solvents with water.
The free-radical polymerization of the monomer composition M’) is preferably carried out in the feed procedure. Here, in general at least the monomers are metered into the reaction mixture in liquid form. Monomers that are liquid under the addition conditions can be introduced into the reaction mixture without adding a solvent. Otherwise the monomers are used as solution in a suitable solvent.
Suitable polymerization initiators are compounds which decompose thermally, by a redox mechanism or photochemically (photo initiators) to form free radicals.
Among the polymerization initiators that can be thermally activated, preference is given to initiators having a decomposition temperature in the range from 20 to 180°C, especially from 50 to 90°C. Examples of suitable thermal initiators are inorganic peroxo compounds such as perox- odisulfates (ammonium peroxodisulfate and preferably sodium peroxodisulfate), peroxosulfates, percarbonates and hydrogen peroxide; organic peroxo compounds such as diacetyl peroxide, di-tert-butyl peroxide, diamyl peroxide, 5-dioctanoyl peroxide, didecanoyl peroxide, dilauroyl peroxide, dibenzoyl peroxide, tert-butyl perneodecanoate, tert-butyl perbenzoate, tert-butyl perisobutyrate, tert-butyl perpivalate, tert-butyl peroctoate, tert-butyl peroxide, tert-butyl hydrop eroxide, cumene hydroperoxide, tert-butylperoxy-2-ethylhexanoate and 10-diisopropyl peroxydi- carbamate; azo compounds such as 2,2'-azobisisobutyronitrile, 2,2'-azobis(2-methylbuty- ronitrile) and azobis(2-amidopropane) dihydrochloride.
These initiators can be used in combination with reducing compounds as initiator/regulator sys- tems. Examples of such reducing compounds include phosphorus compounds such as phosphorous acid, hypophosphites and phosphinates, sulfur compounds such as sodium hydrogen- sulfite, sodium sulfite and sodium formaldehyde- sulfoxylate, and hydrazine.
Also frequently used are redox initiator systems which consist of a peroxo compound, a metal salt and a reducing agent. Examples of suitable peroxo compounds are hydrogen peroxide, peroxodisulfate (as the ammonium, sodium or potassium salt), peroxosulfates, and organic peroxo compounds such as tert-butyl hydroperoxide, cumene hydroperoxide or dibenzoyl per oxide. Suitable metal salts are in particular iron(ll) salts such as iron(ll) sulfate heptahydrate. Suitable reducing agents are sodium sulfite, the disodium salt of 2-hydroxy-2-sulfinatoacetic acid, the disodium salt of 2-hydroxy-2-sulfonatoacetic acid, sodium hydroxymethanesulfinate, ascorbic acid, isoascorbic acid or mixtures thereof.
Examples of suitable photoinitiators are benzophenone, acetophenone, benzyl dialkyl ketones and derivatives thereof.
Preference is given to using thermal initiators, preferably inorganic peroxo compounds, espe cially sodium peroxodisulfate. The peroxo compounds are advantageously used in combination with sulfur-containing reducing agents, especially sodium hydrogensulfite, as the redox initiator system. In the case of use of this initiator/regulator system, copolymers comprising sulfonate and/or sulfate as end groups are obtained, which are notable for exceptional cleaning power and scale- inhibiting action.
Alternatively, it is also possible to use phosphorus-containing regulator systems, for example sodium hypophosphite and phosphinates.
The amounts of initiator/regulator system should be matched to the substances used in each case. If, for example, the peroxodisulfate/ hydrogensulfite system is used, typically 1 to 7% by
weight, preferably 2 to 6% by weight, of peroxodisulfate and generally 3 to 25% by weight, preferably 4 to 15% by weight, of hydrogensulfite are used, based in each case on monomer com position M’).
If desired, it is also possible to use organic polymerization regulators. Suitable examples are sulfur compounds such as mercaptoethanol, 2-ethylhexyl thioglycolate, thioglycolic acid and dodecyl mercaptan. When polymerization regulators are used, the amount thereof is generally 0.1 to 25% by weight, preferably 0.5 to 20% by weight and more preferably 1.0 to 15% by weight, based in each case on monomer composition M’).
The polymerization temperature is generally 20 to 200°C, preferably 20 to 150°C and more preferably 20 to 120°C.
The polymerization can be performed under atmospheric pressure, but is preferably undertaken in a closed system under the autogenous pressure which evolves.
The polymerization can take place in the absence or in the presence of an inert gas. Usually, the polymerization is carried out in the presence of an inert gas, e.g. nitrogen.
The weight-average molecular weight Mw of the polymer P1’) can be determined by means of gel permeation chromatography (GPC) in aqueous solution using neutralized polyacrylic acid as polymer standard. The polymer P1’) preferably has a weight-average molecular weight of from 1000 to 100 000 g/mol, more preferably 1500 to 50 000 g/mol, in particular 2000 to 20 000 g /mol.
Preferably, polymer P1’) has a polydispersity index (PDI) of from 1.2 to 6.0, more preferably 1.4 to 4.0, in particular 1.6 to 3.5.
The polymer P1’) can be obtained in the acidic state, but it can also, if desired be partly neutralized by addition of bases. Suitable bases are alkali metal hydroxides, like NaOH and KOH, alka line earth metal hydroxides, like Ca(OH)2 and Mg(OH)2, ammonia and amine bases, like mono- ethanol amine. Especially preferred is sodium hydroxide. Neutralization can be performed as early as during the polymerization or after the polymerization has ended.
Prior to its use in step i) for providing the aqueous composition, at the most 30 mol% of the car- boxy groups of the polymer P1’) are in the deprotonated form. Preferably, at the most 25 mol%, more preferably at the most 15 mol%, of the carboxy groups of the polymer P1’) are in the deprotonated form. In a special embodiment, the acid groups of the polymer composition according to the invention are present in non-neutralized form.
The polymer P1’) used in accordance with the invention can be used directly in the form of the aqueous solutions obtained in the course of preparation by means of solvent polymerization, or in dried form (obtained, for example, by spray drying, spray granulation such as fluid bed spray granulation or spouted bed spray granulation, roller drying or freeze drying).
Suitable polymers P1’) are commercially available or are intermediates of commercially availa ble products. In a preferred embodiment, a commercially available polyacrylic acid is employed that is not crosslinked and not neutralized or only to a low extend neutralized. Suitable products are Sokalan® CP 10 S, Sokalan® CP 12 S, Sokalan® CP 13 S, Sokalan® PA 25 XS, Sokalan® PA 80 S and Sokalan® NR 2530 from BASF SE.
In a specific embodiment, the monomer composition M1) consists only of a, b-ethylenically un saturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof.
The a,b-ethylenically unsaturated carboxylic acid is preferably selected from acrylic acid, meth- acrylic acid, ethacrylic acid maleic acid, fumaric acid, itaconic acid, a-chloroacrylic acid, crotonic acid, citraconic acid, mesaconic acid, glutaconic acid and aconitic acid. Suitable salts of the abovementioned acids are, in particular, the sodium, potassium and ammonium salts and the salts with amines or aminoalcohols. The monomers A) can be used as such or as mixtures with one another. The stated proportions by weight are all based on the acid form.
The at least one a, b-ethylenically unsaturated carboxylic acid is preferably used in unneutral ized form for the polymerization. If the a, b-ethylenically unsaturated carboxylic acids are used in partially neutralized form for the polymerization, the acid groups are preferably neutralized to at most 50 mol%, more preferably to at most 30 mol%.
The monomer A) is particularly preferably selected from acrylic acid, methacrylic acid, maleic acid, fumaric acid, itaconic acid, salts of the abovementioned carboxylic acids and mixtures thereof.
In particular, the monomer A) is selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid and mixtures thereof.
In a specific embodiment, only acrylic acid is used as monomer A).
The monomer A) is preferably used in an amount of 50 to 100 wt .-%, particularly preferably 60 to 100 wt .-%, based on the total weight of the monomer composition M1.
In a preferred embodiment, the monomer composition M1 ) comprises at least 50% by weight, preferably at least 80% by weight, in particular at least 90% by weight, based on the total weight of the monomer composition M1 ), of acrylic acid and / or acrylic acid salts
Monomer B)
According to the invention, the monomer composition M1) may comprise, in addition to the at least one monomer A), at least one monomer B) selected from olefinically unsaturated sulfonic acids, salts of olefinically unsaturated sulfonic acids, olefinically unsaturated phosphonic acids, salts of olefinically unsaturated phosphonic acids and mixtures thereof.
The monomer composition M1 ) may comprise, in addition to the monomers A), at least one monomer B selected from unsaturated sulfonic acids, salts of unsaturated sulfonic acids, un saturated phosphonic acid, salts of unsaturated phosphonic acids and mixtures thereof.
The monomer B) is preferably selected from 2-acrylamido-2-methylpropane-sulfonic acid, vinyl- sulfonic acid, allylsulfonic acid, sulfoethyl acrylate, sulfoethyl methacrylate, sulfopropyl acrylate, sulfopropyl methacrylate, 2-hydroxy-3-acryloxypropylsulfonic acid, 2-hydroxy-3-methacryloxy- propylsulfonic acid, styrenesulfonic acid, vinylphosphonic acid, allylphosphonic acid, salts of the aforementioned acids and mixtures thereof.
Preferred monomer B) is 2-acrylamido-2-methylpropanesulfonic acid.
Suitable salts of the abovementioned acids are in particular the sodium, potassium and ammo nium salts and the salts with amines. The monomers B) can be used as such or as mixtures with one another. The stated proportions by weight are all based on the acid form
In one embodiment of the inventive multilayer film, the monomer composition M1) additionally comprises at least one comonomer C) selected from
C1 ) nitrogen heterocycles having a free-radically polymerizable a,b-ethylenically unsaturated double bond,
C2) monomers containing amide groups,
C3) compounds of the general formulae (I. a) and (l.b)
in which the sequence of the alkylene oxide units is arbitrary, x is 0, 1 or 2,
k and I are independently an integer from 0 to 100, where the sum of k and I is at least 2, preferably at least 5,
R1 is hydrogen or methyl,
R2 is hydrogen or Ci-C4-alkyl, and mixtures of two or more than two of the aforementioned monomers C1 ) to C3).
In a further inventive embodiment, the monomer composition M1 ), based on the total weight, comprises less than 0.1 % by weight, preferably less than 0.05% by weight, especially less than 0.001 % by weight, of crosslinking monomers having two or more than two free-radically polymerizable a,b-ethylenically unsaturated double bonds per molecule.
In another embodiment of the inventive multilayer film, the monomer composition M1 ) does not comprise any crosslinking monomers having two or more than two free-radically polymerizable a,b-ethylenically unsaturated double bonds per molecule.
In a further inventive embodiment, the monomer composition M1 ) used for free-radical polymerization comprises or consists of acrylic acid and/or acrylic acid salts.
In a further embodiment of the inventive multilayer film, the free-radical polymerization of the monomer composition M1 ) is conducted in the presence of at least one Ce-C-is-alkyl polyoxy- alkylene ether incorporating exclusively ethylene oxide units as alkylene oxide units and/or also in the presence of a polymer.
In a further embodiment of the inventive multilayer film, the Ce-C-ie-alkyl polyoxyalkylene ethers mentioned above comprise an average of 3 to 10 ethylene oxide units per molecule, preferably an average of 5 to 9 ethylene oxide units per molecule.
In an embodiment of the inventive process, the polymer composition P1) is provided by
A) providing a monomer composition M1 ) comprising at least one monomer A) selected from a, b-ethylenically unsaturated mono- and dicarboxylic acids, salts of a, b -ethylenically un saturated mono- and dicarboxylic acids, anhydrides of a, b-ethylenically unsaturated mono- and dicarboxylic acids and mixtures thereof,
B) subjecting the monomer composition M1) provided in step a) to a free-radical polymerization in the presence of at least one Ce-Cie-alkyl polyoxyalkylene ether having 3 to 12 alkylene oxide units per molecule and optionally in the presence of at least one additive.
In a further embodiment of the inventive process for producing a water-soluble multilayer film, the free-radical polymerization in step B) is effected in feed mode, wherein at least a portion of the Cs-Cis-alkyl polyoxyalkylene ether having 3 to 12 alkylene oxide units per molecule and optionally, if present, at least a portion of a solvent are initially charged, and at least a portion of the monomer composition M) provided in step a) and at least one free-radical initiator are fed into the initial charge.
Polyether component PE):
Suitable as polyether component PE) are polyetherols having a number average molecular weight of at least 200 g/mol and their mono- and di-(Ci-C6-alkyl ethers).
Suitable polyetherols and their mono- and di-(CrC6-alkyl ethers) may be linear or branched, preferably linear. Suitable polyetherols and their mono- and di-(C1-C6-alkyl ethers) generally have a number-average molecular weight in the range from about 200 to 100,000, preferably from 300 to 50,000, particularly preferably from 500 to 40,000. Suitable polyetherols are, for example, water-soluble or water-dispersible nonionic polymers which comprise alkylene oxide repeat units. Preferably, the proportion of alkylene oxide repeating units is at least 30 % by weight, based on the total weight of the compound. Suitable polyetherols are polyalkylene gly cols, such as polyethylene glycols, polypropylene glycols, polytetrahydrofurans and alkylene oxide copolymers. Suitable alkylene oxides for the preparation of alkylene oxide copolymers are e.g. ethylene oxide, propylene oxide, epichlorohydrine, 1 ,2- and 2,3-butylene oxide. Suitable examples are copolymers of ethylene oxide and propylene oxide, copolymers of ethylene oxide and butylene oxide and copolymers of ethylene oxide, propylene oxide and at least one butylene oxide. The alkylene oxide copolymers may comprise randomly distributed alkylene oxide units or in copolymerized form in the form of blocks. Preferably, in the ethylene oxide / propylene oxide copolymers, the proportion of repeating units derived from ethylene oxide is 40 to 99% by weight. Particularly preferred as the polyether component PE are ethylene oxide homopolymers and ethylene oxide / propylene oxide copolymers.
Also suitable as polyether component PE) are the mono- and di-(Ci-C6-alkyl ethers) of the polyetherols described above. Preference is given to polyalkylene glycol monomethyl ether and pol yalkylene glycol dimethyl ether.
Also suitable as polyether component PE) are polyether-containing surfactants. Generally suit able are nonionic and ionic surfactants which have at least one nonpolar and at least one polar group and which comprise a polyether group.
The polyether groups-containing surfactants PE) are preferably selected from alkylpolyoxy- alkylenether, arylpolyoxyalkylenether, alkylarylpolyoxyalkylenether, alkoxylated animal and/or vegetable fats and/or oils, fatty amine alkoxylates, fatty acid amide alkoxylates, fatty acid dieth- anolamide alkoxylates, polyoxyethylenesorbitan fatty acid esters, alkylpolyethersulfates, ar- ylpolyethersulfates, alkylarylpolyethersulfates, alkylpolyethersulfonates, arylpolyethersulfonates, alkylarylpolyethersulfonates, alkylpolyether phosphateates, aryl polyether phosphates, alkylaryl polyether phosphates, glycerol ether sulfonates, glycerol ether sulfates, monoglyceride (ether) sulfates, fatty acid amide ether sulfates, polyoxyalkylene sorbitan fatty acid esters, and mixtures thereof.
The preferred nonionic polyether group-containing surfactants PE) include, for example:
Alkyl polyoxyalkylene ethers derived from C3-C6 low molecular weight alcohols or C7-C30 fatty alcohols. Here, the ether component may be derived from ethylene oxide units, propylene oxide
units, 1 ,2-butylene oxide units, 1 ,4-butylene oxide units, and random copolymers and block copolymers thereof. Suitable nonionic surfactants include, inter alia, surfactants of the general formula (VI)
R10-O-(CH2CH2O)x-(CHR11CH2O)y-R12
(VI),
wherein
R10 is a linear or branched alkyl radical having 6 to 22 C atoms,
R11 and R12 independently of one another are hydrogen or a linear or branched alkyl radical having 1 to 10 C atoms or H, wherein R12 is preferably methyl, and
x and y are independently 0 to 300. Preferably, x = 1 to 100 and y = 0 to 30.
These include, in particular, fatty alcohol alkoxylates and oxo alcohol alkoxylates, such as iso- tridecyl alcohol and oleyl alcohol polyoxyethylene ethers.
Hydroxyl-containing surfactants of the general formula (VII)
R13-0-(CH2CH20)s-(CH2CH2CH20)r(CH2CH2CH2CH20)u-(CH2CHR140)v-CH2CH(0H)R15
(vii)
wherein
in the compounds of the formula (VII) the sequence of the alkylene oxide units is arbitrary, s, t, u and v independently represent an integer from 0 to 500, the sum of s, t, u and v being > 0, R13 and R15 independently of one another represent a linear or branched, saturated Ci-C4o-alkyl radical or a mono- or polyunsaturated C2-C4o-alkenyl radical, and
R14 is selected from methyl, ethyl, n-propyl, isopropyl or n-butyl.
In the compounds of the general formula (VII), the sum of s, t, u and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
Preferably, t and u are 0. Then the sum of s and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
In the compounds of the general formula (VII), R13 and R15 are preferably, independently of one another, a linear or branched, saturated C2-C3o-alkyl radical. R13 and R15 may also be mixtures of different alkyl radicals.
In the compounds of the general formula (VII), R14 is preferably methyl or ethyl, in particular methyl.
A preferred embodiment are hydroxyl-containing surfactants of the general formula
R13-0-(CH2CH20)S-(CH2CH(CH3)0)V-CH2CH(0H)R15
(VII.1)
wherein the order of the - (CH2CH2O)- and the (CH2CH(CH3)0) units is arbitrary,
s and v are independently an integer from 0 to 500, the sum of s and v being > 0, and
R13 and R15 independently of one another represent a linear, saturated Ci-C3o-alkyl radical or a branched, saturated C3-C3o-alkyl radical or mono- or polyunsaturated C2-C3o-alkenyl radical.
In the compounds of the general formula (VI 1.1 ), the sum of s and v is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
The group of these nonionic surfactants include e.g. hydroxy mixed ethers of the general formula (C6-22-alkyl)-CH(OH)CH2O-(EO)20-i20-(C2-26-alkyl).
Alcohol polyoxyalkylene esters of the general formula (VIII)
R16-0-(CH2CH20)p-(CH2CHR170)q-C(=0)R18
(VIII)
wherein in the compounds of the formula (VIII) the sequence of the alkylene oxide units is arbitrary, p and q independently of one another represent an integer from 0 to 500, the sum of p and q being > 0,
R16 and R18 independently of one another represent a linear or branched, saturated Ci-C4o-alkyl radical or a mono- or polyunsaturated C2-C4o-alkenyl radical, and
R17 is selected from methyl, ethyl, n-propyl, isopropyl or n-butyl.
In the compounds of the general formula (VIII), the sum of p and q is preferably from 10 to 300, particularly preferably from 15 to 200 and in particular from 20 to 150.
In the compounds of the general formula (VIII), preferably R16 and R18 independently of one another represent a linear or branched, saturated C4-C3o-alkyl radical. R16 and R18 may also be mixtures of different alkyl radicals.
In the compounds of the general formula (VIII), R17 is preferably methyl or ethyl, in particular methyl.
These include e.g. lauryl alcohol polyoxyethylene acetate. alkylarylalkoholpolyoxyethylenether, e.g. Octylphenol polyoxyethylene ether,
alkoxylated animal and/or vegetable fats and/or oils, e.g. corn oil ethoxylates, castor oil ethoxylates, tallow fat ethoxylates,
alkyl phenol alkoxylates, such as ethoxylated isooctyl-, octyl- or nonylphenol, tributylphe- nol polyoxyethylene ethers,
fatty amine alkoxylates, fatty acid amide- and fatty acid diethanolamide alkoxylates, especially their ethoxylates,
polyoxyalkylenesorbitan fatty acid esters.
An example of an alkylpolyethersulfate is sodium dodecylpoly (oxyethylene) sulfate (sodium lauryl ether sulfate, SLES). A preferred commercially available modified fatty alcohol polyglycol ether is a double ending CxH2x+i/CyH2y+i-terminated polyethylene oxide having a free OH group and x, y = 6-14.
In an embodiment of the inventive water-soluble multilayer film, the polyether component PE) is selected from Ce-C-ie-alkyl polyoxyalkylene ethers having an average of 3 to 12 alkylene oxide units per molecule.
The polymer composition P1 ) may be prepared by free-radical polymerization of the monomer composition M1) in the presence of at least one Cs-C-is-alkyl polyoxyalkylene ether having an average of 3 to 12 alkylene oxide units per molecule. This affords specific polymer compositions P1 ) having advantageous properties. Without being bound to a theory, hydrogen bonds are able to form between the growing polymer and the alkylene oxide units, and these influence the properties of the resultant polymer composition. Thus, polymer compositions P1) having a high content of the Ce-C-ia-alkyl polyoxyalkylene ether can be attained; these cannot be prepared by mixing the separately prepared polymer with the C8-Ci8-alkyl polyoxyalkylene ether. Free- radical surfactant degradation advantageously does not take place here.
For production of a washing- and cleaning-active multilayer films according to the invention, preference is given to using polymer compositions P1 ) having a low glass transition temperature TG. Preferably, the polymer compositions P1) used for production of the washing- and cleaning- active multilayer films of the invention have a glass transition temperature TG in the range from 0 to 80°C, preferably from 0 to 60°C, especially 0 to 30°C.
The glass transition temperatures (Tg) described in the context of this application can be determined by means of differential scanning calorimetry (DSC).
In a preferred embodiment, the polymer compositions P1) used for production of the washing- and cleaning-active multilayer films of the invention take the form of a transparent film.
Polymer P2):
As already discussed above the multi-layered film further comprises at least one other layer which comprises at least one polymer P2) which is different from polymer composition P1 ) and is selected from
natural or modified polysaccharides;
homo- or copolymers comprising monomer units derivable from vinyl alcohol, vinylesters, alkoxylated vinyl alcohols, or mixtures thereof;
homo-or copolymers comprising at least one monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinyl-pyridine, salts of N- vinylimidazole, salts of 2-vinylpyridine, salts of 4-vinyl-pyridine, vinylpyridine-N-oxide, N- carboxymethyl-4-vinylpyridine halogenides or mixtures thereof;
homo- or copolymers of acrylic acid and /or methacrylic acid, preferably copolymers corn- prising at least one acrylic acid monomer selected from acrylic acid, salts of acrylic acid or mixtures thereof and at least one maleic acid monomer selected from maleic acid, maleic acid anhydride, salts of maleic acid or mixtures thereof;
copolymer comprising at least a (meth)acrylic acid monomer selected from acrylic acid, methacrylic acid, salts of acrylic acid, salts of methacrylic acid or mixtures thereof and at least one hydrophobic monomer selected from CrCs alkylesters of (meth) acrylic acid, C2-
C10 olefins, styrene or omethyl-styrene;
homo- or copolymers of acrylamide and or methacrylamide;
polyaminoacids;
water-soluble or water-dispersible polyamides;
polyalkyleneglycols, mono-or diethers of polyalkyleneglycols;
polyalkyleneoxide such as polyethyleneoxide;
polyethylene imine alkoxylates,
multifunctional alkoxylated diamines, preferably alkoxylated diamines with 2 to 10 meth ylene groups, and
mixtures thereof.
The multi-layered film particularly preferably comprises at least one further layer which compris es at least one polymer P2) or consists of at least one polymer P2) which is selected from Cellulose ethers and cellulose esters,
Homo- and copolymers containing repeating units derived from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
Polymers selected from polyvinylpyrrolidone homopolymers, polyvinylimidazole homopolymers, copolymers compriseing copolymerized vinylpyrrolidone and vinylimidazole, polyvinylpyridine-N- oxide, poly-N-carboxymethyl-4-vinylpyridium halides, mixtures thereof.
The multi-layered film comprises in particular at least one further layer which comprises at least one polymer P2) or consists of at least one polymer P2) selected from cellulose derivatives, preferably carboxyalkylcelluloses and salts thereof, sulfoalkylcelluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkylcelluloses, hydroxyalkylcelluloses, (hydroxyalkyl) alkylcellu- loses and mixtures of two or more of these cellulose derivatives.
Polysaccharides suitable as polymers P2 are natural polysaccharides, e.g. cellulose, hemicellu- lose, glycogen, starch (amylose and amylopectin), dextran, pectins, inulin, xanthan, chitin, cal- lose, thermally, hydrolytically or enzymatically degraded starch, e.g. maltodextrin etc
Preferred modified polysaccharides are e.g. cellulose ethers, cellulose esters, cellulose amides, etc.
Cellulose ethers are derivatives of cellulose that result from partial or total substitution of the hydrogen atoms in the hydroxy groups of the cellulose. Cellulose ethers from the reaction of cellulose with more than one etherifying agent are also referred to as cellulose mixed ethers.
Preferred cellulose ethers are selected from alkylcelluloses, hydroxyalkylcelluloses, (hydroxy- alkyl) alkylcelluloses, carboxyalkylcelluloses and salts thereof, (carboxyalkyl) alkylcelluloses and salts thereof, (carboxyalkyl) (hydroxyalkyl) celluloses and salts thereof, (carboxyalkyl) (hydroxy- alkyl) alkylcelluloses and salts thereof, sulfoalkylcelluloses and salts thereof.
Preferred carboxyalkyl radicals are the carboxymethyl radical and the carboxyethyl radical. Particularly preferred as carboxyalkyl radical is the carboxymethyl radical. Preferred as sulfoalkyl radical are the sulfomethyl radical and the sulfoethyl radical. Particularly preferred as sulfoalkyl radical is the sulfomethyl radical. Preferred salts are the sodium, potassium, calcium and ammonium salts.
Particularly preferred cellulose ethers are selected from carboxymethylcellulose, carboxyethyl- cellulose, methylcellulose, ethylcellulose, n-propylcellulose, ethylmethylcellulose, hydroxyethyl- cellulose, hydroxypropylcellulose, hydroxybutylcellulose, hydroxyethylmethylcellulose, hydroxy- propylmethylcellulose, hydroxyethylethylcellulose, hydroxypropylethylcellulose, carboxymethyl- methylcellulose, carboxymethylethylcellulose, carboxymethylhydroxyethylcellulose, carbox- ymethylhydroxyethylmethylcellulose, carboxymethylhydroxyethylethylcellulose, sulfomethylcellu- lose and sulfoethylcellulose. The carboxyalkyl radicals and the sulfoalkyl radicals may also be present as salts.
Cellulose esters are derivatives of cellulose which are formed by esterification of the hydroxy groups with acids. Preferred are the sulfuric acid esters of cellulose. In a specific embodiment, the sulfuric acid is only subjected to a partial esterification, so that the resulting sulfuric acid es ters still have free acid groups or their salts. Particular preferred are sulfuric ester salts of cellulose. These are distinguished by their graying-inhibiting effect.
Preferred modified polysaccharides are selected from methyl cellulose, ethyl cellulose, propyl cellulose, methyl/ethyl cellulose, ethyl/propyl cellulose, carboxymethyl cellulose, salts of carboxymethyl cellulose, hydroxyethyl cellulose, hydroxypropyl cellulose, hydroxyethylmethyl cellulose, hydroxyethylethyl cellulose, hydroxypropylmethyl cellulose, hydroxypropylethyl cellulose, etc.
In a further preferred embodiment, the polymers P2) are selected from homo- and copolymers comprising repeating units derived from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof.
Suitable vinyl esters (vinyl acylates) are generally the esters of vinyl alcohol with C1-C15- carboxylic acids, preferably Ci-C8-carboxylic acids, more preferably Ci-C4-carboxylic acids. Preferred vinyl acylates are vinyl acetate, vinyl n-propionate, vinyl n-butyrate, vinyl 2-ethyl- hexanoate, vinyl laurate, etc. Particularly preferred is vinyl acetate.
Partially or completely saponified (hydrolyzed) polyvinyl acetates (PVA) are generally referred to as "polyvinyl alcohol (PVOH)". Partially hydrolysed polyvinyl acetates are obtained by incomplete hydrolysis of polyvinyl acetates, i.e. the partially hydrolyzed polymer has both ester groups and hydroxyl groups. The saponification of the polyvinyl acetates can be carried out in a manner known per se in alkaline or acidic, i.e. with the addition of acid or base.
The performance properties of polyvinyl alcohols are determined inter alia by the degree of polymerization and the degree of hydrolysis (degree of saponification). As the degree of saponification increases, the solubility in water decreases. Polyvinyl alcohols with degrees of hydrolysis of up to about 90 mol% are generally soluble in cold water. Polyvinyl alcohols with degrees of hydrolysis of about 90 to about 99.9 mol% are generally no longer soluble in cold water, but are soluble in hot water.
Polyvinyl alcohols suitable as polymers P2) preferably have a saponification degree of from 50 to 99.9 mol%, particularly preferably from 70 to 99 mol%, in particular from 80 to 98 mol%.
The properties of polyvinyl alcohols can further be modified by the incorporation of additional monomers such as the sodium salts of 2-acrylamido-2-methylpropane sulfonic acid, vinyl- sulfonic acid or allylsulfonic acid.
Polyvinyl alcohols suitable as polymers P2) preferably have a weight-average molecular weight of from 10,000 to 300,000 g/mol, more preferably from 15,000 to 250,000 g/mol.
Polyvinylalcohol that can typically be used as polymers P2) are known under the tradename Poval™ from Kuraray company. Non limited examples are Poval™ 8-88, Poval™ 18-88, Poval™ 26-88, Poval™ 30-92, Poval™ 10-98, Poval™ 20-98 or Poval™ 28-99.
To tune the performance properties according to the specific need of the application blends comprising polyvinylalcohols of different molecular weight and degree of hydrolysis can be used. Non limited examples are a blend of Poval™ 26-88 (three parts) and Poval™ 20-98 (one part) or a blend of Poval™ 30-92 (two parts) and Poval™ 10-98 (one part).
Polyvinyl alcohols suitable as polymers P2) preferably have a viscosity of 2 to 120 mPa s, more preferably of 7 to 70 mPa s and in particular of 15 to 60 mPa s, measured according to DIN 53015 on a 4% solution in water.
In a further preferred embodiment, the polymers P2) are selected from homopolymers and copolymers which comprise at least one monomer in copolymerized form, which is selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole, 2-vinylpyridine, 4-vinylpyridine, salts
thereof three latter monomers, vinylpyridine-N-oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof.
N-vinylimidazole, 2-vinylpyridine and 4-vinylpyridine can be converted by protonation or quater- nization into the corresponding salts. Suitable acids are e.g. mineral acids such as sulfuric acid, hydrochloric acid and phosphoric acid, and carboxylic acids. Alkylating agents suitable for quaternization are C1-C4 alkyl halides or C1-C4 alkyl sulfates such as ethyl chloride, ethyl bromide, methyl chloride, methyl bromide, dimethyl sulfate and diethyl sulfate.
Preferred are polyvinylpyrrolidone homopolymers and copolymers which comprise copolymerized N-vinylpyrrolidone and another ethylenically unsaturated monomer different therefrom. Suitable N-vinylpyrrolidone copolymers are generally neutral, anionic, cationic and amphoteric polymers.
Particularly preferred N-vinylpyrrolidone copolymers are selected from
Copolymers of N-vinylpyrrolidone and vinyl acetate,
Copolymers of N-vinylpyrrolidone and vinyl propionate,
Copolymers of N-vinylpyrrolidone, vinyl acetate and vinyl propionate,
Copolymers of N-vinylpyrrolidone and vinyl acrylate,
Copolymers of N-vinylpyrrolidone, ethyl methacrylate and methacrylic acid,
Copolymers of N-vinylpyrrolidone and N-vinylimidazole and their derivatives obtained by protonation and/or quaternization,
Copolymers of N-vinylpyrrolidone and dimethylaminoethyl methacrylate and their derivatives obtained by protonation and/or quaternization,
Copolymers of N-vinylpyrrolidone, N-vinylcaprolactam and N-vinylimidazole and their derivatives obtained by protonation and/or quaternization.
In a further preferred embodiment, the polymers P2) are selected from homopolymers and copolymers of acrylic acid and/or methacrylic acid.
In a first specific embodiment of the homopolymers and copolymers of acrylic acid and/or methacrylic acid, the polymer P2) used is an acrylic acid homopolymer. Acrylic acid homopolymers P2) preferably have a number-average molecular weight in the range from 800 to 70,000 g/mol, more preferably from 900 to 50,000 g/mol, in particular from 1000 to 20,000 g/mol, especially from 1000 to 10,000 g/mol. The term acrylic acid homopolymer also encompasses polymers in which the carboxylic acid groups are partially or completely neutralized. These include acrylic acid homopolymers in which the carboxylic acid groups are present partially or completely in the form of alkali metal salts or ammonium salts. Preference is given to acrylic acid homopolymers in which the carboxylic acid groups are protonated or in which the carboxylic acid groups are present partially or completely in the form of sodium salts. Homopolymers of acrylic acid which are particularly suitable as polymers P2) are the Sokalan® PA grades from BASF SE.
In a second specific embodiment of the homo- and copolymers of acrylic acid and/or methacrylic acid, the polymer P2) used is a copolymer comprising at least one acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof and at least one maleic acid
monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form. These preferably have a number-average molecular weight in the range from 2500 to 150,000 g/mol, more preferably from 2800 to 70,000 g/mol, in particular from 2900 to 50,000 g/mol, more particularly from 3000 to 30,000 g/mol. Included here are also copoly- mers in which the carboxylic acid groups are partially or completely neutralized. For this pur pose, it is possible to use monomers in salt form either for the polymerization or the resulting copolymer is subjected to a partial or complete neutralization. Preferred are copolymers in which the carboxylic acid groups are protonated or partially or completely present in the form of alkali metal salts or ammonium salts. Preferred alkali metal salts are the sodium or potassium salts, especially the sodium salts.
Preferred polymers P2) are copolymers of maleic acid (or maleic acid monomers) and acrylic acid (or acrylic acid monomers) in a weight ratio of 10:90 to 95: 5, particularly preferably in a weight ratio of 30:70 to 90:10.
Preferred polymers P2) are also terpolymers of maleic acid (or maleic acid monomers), acrylic acid (or acrylic acid monomers) and a vinyl ester of a C1-C3 carboxylic acid in a weight ratio of 10 (maleic acid) : 90 (acrylic acid + vinyl ester) to 95 (maleic acid) : 10 (acrylic acid + vinyl ester). The weight ratio of acrylic acid to vinyl ester is preferably in a range of 30:70 to 70:30.
Particularly suitable polymers P2) based on acrylic acid monomers and maleic acid monomers are the corresponding Sokalan® CP grades from BASF SE.
In a third specific embodiment of the homo- and copolymers of acrylic acid and/or methacrylic acid, the polymer P2) is a copolymer, which comprises at least one (meth) acrylic acid monomer selected from (meth) acrylic acid, (meth) acrylic acid salts and mixtures thereof and at least one hydrophobic monomer. The hydrophobic monomer is especially selected from Ci-Cs alkyl esters of (meth) acrylic acid such as e.g. the methyl, ethyl, n- and iso-propyl, n-butyl and 2-ethylhexyl esters of (meth) acrylic acid and C2-Cio-olefins, e.g. ethene, propene, 1 ,2-butene, isobutene, disobutene, styrene and a-methylstyrene.
In a further preferred embodiment, the polymer P2) used is a copolymer of at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof with at least one C2-C8-olefin. Also suitable are copolymers which comprise at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, in copolymerized form at least one C2-Cs-olefin and at least one other comonomer which is different therefrom.
Particularly preferred are copolymers, which comprise at least one maleic acid monomer select ed from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof and at least one C2-C8-olefin copolymerized as sole monomers. These preferably have a number average molecular weight in the range from 3000 to 150,000 g/mol, particularly preferably from 5000 to 70,000 g/mol, in particular from 8000 to 50,000 g/mol, more particularly from 10,000 to 30,000 g/mol. Included therein are also copolymers in which the carboxylic acid groups are partially or
completely neutralized. For this purpose, either maleic acid salts can be used for the polymerization or the resulting copolymer is subjected to a partial or complete neutralization. Preferred are copolymers in which the carboxylic acid groups are protonated or partially or completely present in the form of alkali metal salts or ammonium salts. Preferred alkali metal salts are the sodium or potassium salts, especially the sodium salts.
A specific embodiment are copolymers of maleic acid with C2-C8 olefins in a molar ratio of 40:60 to 80:20, whereby copolymers of maleic acid with ethylene, propylene, isobutene, diisobutene or styrene are particularly preferred. Particularly suitable polymeric carboxylic acid group- containing compounds based on olefins and maleic acid are likewise the corresponding Soka- lan® CP grades from BASF SE.
Another preferred embodiment is copolymers comprising at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, at least one C2-C8 olefin and at least one acrylic acid monomer selected from acrylic acid, acrylic acid salts and mixtures thereof, in copolymerized form.
A further preferred embodiment is copolymers which comprise at least one maleic acid monomer selected from maleic acid, maleic anhydride, maleic acid salts and mixtures thereof, at least one C2-C8 olefin and at least one ester of (meth) acrylic acid in copolymerized form. The ester of (meth) acrylic acid is then in particular selected from C2-Cs-alkyl esters of (meth) acrylic acid, e.g. the methyl, ethyl, n- and iso-propyl, n-butyl and 2-ethylhexyl esters of (meth) acrylic acid.
In a further preferred embodiment, the polymers P2) are selected from homopolymers and co polymers which comprise, in polymerized form, at least one monomer selected from acrylamide, methacrylamide and mixtures thereof. These polymers P2) are preferably water-soluble or water-dispersible. In particular, these polymers P2) are water-soluble.
In a specific embodiment, the polymers P2) are selected from homopolymers of acrylamide or methacrylamide.
In a further specific embodiment, the polymers P2) are selected from copolymers of acrylamide and/or methacrylamide. These comprise at least one comonomer in copolymerized form, which is selected from acrylamide and methacrylamide different hydrophilic monomers (A1 ), monoeth- ylenically unsaturated, amphiphilic monomers (A2) and other ethylenically unsaturated monomers (A3).
Suitable hydrophilic, monoethylenically unsaturated monomers (A1 ) are neutral monomers, such as N-methyl (meth) acrylamide, N, N'-dimethyl (meth) acrylamide or N-methylol (meth) acrylamide, monomers comprising hydroxyl and/or ether groups, such as e.g. hydroxyethyl (meth) acrylate, hydroxypropyl (meth) acrylate, allyl alcohol, hydroxyvinylethyl ether, hydroxyvi- nylpropyl ether, hydroxyvinylbutyl ether, polyethylene glycol (meth) acrylate, N-vinylformamide, N-vinylacetamide, N-vinylpyrrolidone or N-vinylcaprolactam and vinyl esters, such as vinyl formate or vinyl acetate. N-vinyl derivatives can be hydrolyzed after polymerization to vinylamine
units, vinyl esters to vinyl alcohol units. Suitable hydrophilic, monoethylenically unsaturated monomers (A1 ) are furthermore monomers which comprise at least one acidic group or salts thereof. These include acrylic acid, methacrylic acid, crotonic acid, itaconic acid, maleic acid, fumaric acid, vinylsulfonic acid, allylsulfonic acid, 2-acrylamido-2-methylpropanesulfonic acid, 2-methacrylamido-2-methylpropanesulfonic acid, 2-acrylamidobutanesulfonic acid, 3-acryl- amido-3-methylbutanesulfonic acid, 2-acrylamido-2,4,4-trimethylpentanesulfonic acid, vi- nylphosphonic acid, allylphosphonic acid, N-(meth) acrylamidoalkylphosphonic acids, (meth) acryloyloxyalkylphosphonic acids and salts and mixtures thereof. The other monoethylenically unsaturated hydrophilic monomers may be hydrophilic cationic monomers. Suitable cationic monomers (A1 c) include, in particular, ammonium-group containing monomers, in particular ammonium derivatives of N-(u)-aminoalkyl) (meth) acrylamides or w-aminoalkyl (meth) acrylic esters.
The amphiphilic monomers (A2) are preferably monoethylenically unsaturated monomers which have at least one hydrophilic group and at least one, preferably terminal, hydrophobic group.
The monomers (A3) may be e.g. monoethylenically unsaturated monomers which have a more hydrophobic character than the hydrophilic monomers (A1) and which accordingly are only slightly water-soluble. Examples of such monomers include N-alkyl and N, N'-dialkyl (meth) acrylamides wherein the number of carbon atoms in the alkyl groups together is at least 3, preferably at least 4. Examples of such monomers include N-butyl (meth) acrylamide, N-cyclohexyl (meth) acrylamide or N-benzyl (meth) acrylamide.
In a further preferred embodiment, the polymers P2) are selected from polyamino acids. Suita ble polyamino acids are in principle compounds, which comprise at least one amino acid, such as aspartic acid, glutamic acid, lysine, glycine, etc. in copolymerized form. The polyamino acids also include the derivatives obtainable by polymer-analogous reaction, such as esterification, amidation, etc. Preferred polyamino acids are polyaspartic acid, polyaspartic acid derivatives, polyglutamic acid, polyglutamic acid derivatives and mixtures thereof.
Polyaspartic acid may e.g. by alkaline hydrolysis of polysuccinimide (PSI, anhydropolyaspartic acid). Polysuccinimide can be prepared by thermal condensation of aspartic acid or from ammonia and maleic acid. Polyaspartic acid may e.g. be used as a biodegradable complexing agent and cobuilder in detergents and cleaners.
Polyamino acids having surfactant properties can be obtained by at least partially converting the free carboxylic acid groups of polyaspartic acid or polyglutamic acid into N-alkylamides and/or into esters. Polyaspartic acid amides can also be prepared by reacting polysuccinimide with amines. For the preparation of hydroxyethylaspartamides the ring opening of polysuccinimide can be carried out with ethanolamine. DE 37 00 128 A and EP 0 458 079 A describe the subsequent esterification of such hydroxyethyl derivatives with carboxylic acid derivatives. Copolymers of polyaspartic ester are, as described in DE 195 45 678 A, obtainable by condensation of monoalkyl esters of maleic or fumaric acid with addition of ammonia. In DE 195 45 678 A is further described that copolymeric polyaspartic esters are accessible by reaction of polysuccin-
imide with alcohols and optionally subsequent hydrolysis. Depending on the degree of esterification and hydrophobicity of the alcohol component, polyaspartic esters, in addition to their bio degradability, are distinguished by excellent properties as stabilizers for O / W and W / O emulsions, foam-stabilizing and foam-enhancing cosurfactants in detergents and cleaners and as complexing agents for metal cations.
In a further preferred embodiment, the polymers P2) are selected from polyalkylene glycols and mono- or diethers of polyalkylene glycols. Preferred polyalkylene glycols have a number aver age molecular weight in the range from 1000 to 4,000,000 g/mol, particularly preferably from 1 ,500 to 1 ,000,000 g/mol
Suitable polyalkylene glycols and their mono- or diethers may be linear or branched, preferably linear. Suitable polyalkylene glycols are e.g. water-soluble or water-dispersible nonionic polymers, which comprise alkylene oxide repeat units. The proportion of alkylene oxide repeating units is preferably at least 30% by weight, preferably at least 50% by weight, in particular at least 75% by weight, based on the total weight of the compound. Suitable polyalkylene glycols are polyethylene glycols, polypropylene glycols, polytetrahydrofurans and alkylene oxide copolymers. Suitable alkylene oxides for the preparation of alkylene oxide copolymers are, for. For example, ethylene oxide, propylene oxide, epichlorohydrin, 1 ,2- and 2,3-butylene oxide. Suitable examples are copolymers of ethylene oxide and propylene oxide, copolymers of ethylene oxide and butylene oxide and copolymers of ethylene oxide, propylene oxide and at least one butylene oxide. The alkylene oxide copolymers may comprise randomly distributed alkylene oxide units or in copolymerized form in the form of blocks. Preferably, in the ethylene oxide / propylene oxide copolymers, the proportion of repeating units derived from ethylene oxide is 40 to 99% by weight. Particularly preferred are ethylene oxide homopolymers and ethylene oxide / propylene oxide copolymers.
Suitable mono- and diethers of polyalkylene glycols are the mono (C1-C18 alkyl ethers) and di (C1-C18 alkyl ethers). Preferred mono- and diethers of polyalkylene glycols are the mono (C1-C6 alkyl ethers) and di (C1-C6 alkyl ethers). Especially preferred are the mono (C1-C2 alkyl ethers) and di (C1-C2 alkyl ethers). Particularly preferred are polyalkylene glycol monomethyl ether and polyalkylene glycol dimethyl ether.
In another embodiment of the inventive water-soluble multilayer film, at least one of the layers comprises or consists of at least one compound selected from the group consisting of (i) vinyl- imidazole containing polymers, preferably vinylpyrrolidone/vinylimidazole copolymers with a molecular weight Mw in the range of 10000 to 100000 g/mol, (ii) polyvinylpyrrolidones with a molecular weight Mw in the range of 10000 to 100000 g/mol, (iii) polyethylene imine ethox- ylates, (iv) multifunctional diamines and (v) amphoteric modified starch, and mixtures thereof.
In a further embodiment, at least one of the layers comprises at least one additive and/or at least one additive is present between at least two layers, said additive preferably being selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid
and the sodium and potassium salts thereof, bleaches, enzymes, bases, corrosion inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluores- cers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, corrosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and antislip agents, plasticizers, scavengers, polymers other than the polymer compositions P1 ) and the polymers P2), agents for modification of gas permeability and water vapor permeability, antistats, glidants, slip agents, bitter agent, anti-yellowing agents and UV absorbers and mixtures thereof.
Preferably, in the inventive water-soluble multilayer film, at least two of the layers, preferably two of the layers, comprise at least one type of enzyme EN) each.
In a preferred embodiment, two of the layers comprise one enzyme EN) each, wherein the enzymes EN) comprised in the different layers are different from each other, and preferably are incompatible with each other (as defined above).
In a further preferred embodiment of the inventive water-soluble multilayer film, at least two of the layers, preferably two of the layers, comprise one enzyme EN) each, and wherein the layers comprising one enzyme EN) each are spatially separated by at least one layer comprising or consisting of composition P1 ) or P2), and wherein the separating layer does not contain enzymes, and wherein the enzymes EN) comprised in the different layers are preferably different from each other, and further preferably are incompatible with each other.
Preferably, at least one enzyme EN) is incorporated in one of the layers comprising or consisting of a composition P2), wherein this layer comprising or consisting of a composition P2) preferably comprises polyvinyl alcohol.
Further preferably, all of the enzymes EN) are incorporated in any one of the layers comprising or consisting of a composition P2).
In one embodiment of the inventive multilayer film, at least one layer contains protease as enzyme EN1 ) (preferably as the only enzyme in this layer), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease and preferably different from protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1 ) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
In a preferred embodiment of the invention, none of the layers contains a protease inhibitor (as defined above).
I another embodiment of the invention, the water-soluble multilayer film is derived from a wash active layer based on a at least one polymer chosen from P2), preferred a polymer blend, more
preferred chosen from polymer composition P1 ), which is used as adhesion layer in-between two enzyme containing layers, optionally in a lamination process.
Multilayer films can be produced e.g. by a lamination method. Lamination methods in which two or more film layers are bonded to one another over their area are known to those skilled in the art. Lamination involves pressing two or more than two films together under elevated pressure and/or at elevated temperature. Multilayer films can also be produced by a wet-on-wet application method. In addition, multilayer films can also be produced by using combinations of the aforementioned production methods and the application method described hereinafter.
In a preferred embodiment, the multilayer film is produced by a process in which at least one free-flowing composition capable of film formation is applied to a carrier material, wherein the carrier material and/or the at least one free-flowing composition comprises or consists of the polymer composition P1 ) as defined above and hereinafter, or comprises a polymer P1’) and a polyoxyalkylene ether PE) as defined above and hereinafter.
Reference is made to the aqueous composition obtained by step i) as defined above and hereinafter for the production of the washing- and cleaning-active polymer film of one embodiment.
The process for producing a multilayer film preferably comprises the steps of
11 ) a first free-flowing or pourable composition capable of film formation is applied to a carrier material to obtain a first layer,
12) the first layer applied to the carrier material is optionally subjected to an increase in viscosity,
13) a second free-flowing or pourable composition capable of film formation is applied to the first layer obtained in step H ) or in step i2) to obtain a second layer,
14) the second layer is optionally subjected to an increase in viscosity,
15) step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to repeat steps i3) and i4) once or more than once,
16) the layers applied to the carrier material are optionally subjected to a further increase in viscosity,
17) the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing or pourable compositions each comprise a component which is capable of film formation and is independently selected from at least one polymer composition P1 , at least one polymer P2 or a mixture thereof, and with the proviso that the carrier material and/or the at least one free-flowing or pourable composition comprises or consists of a polymer composition P1 as defined above and hereinafter.
In a specific embodiment, the application of two or more than two of the pourable compositions can also be applied partly or fully simultaneously. For this purpose, for example, the application
of the (n+1)th composition can be commenced before the application of the nth composition has completely ended.
In a further specific embodiment, the production of the multilayer film proceeds from a carrier material which already comprises the first film layer and optionally also already comprises fur ther film layers of the multilayer film. In other words, a carrier material which already comprises the first film layer and optionally further film layers of the multilayer film is used in step i1 ). In this case, the carrier material forms part of the multilayer film and remains in the multilayer film after the application of all the further layers. This means that the further layers applied to the carrier material are not subsequently detached again from the carrier material. In this embodiment, there is therefore no step i7) of the above-described process.
The viscosity of the free-flowing composition is matched to the technical demands of the production method and is determined by factors including the concentration of the components capable of film formation, the solvent content (water), the additives added and the temperature.
The pourable compositions capable of film formation are applied in steps i 1 ) , i3) and i5) general- ly by means of standard methods, for example by means of pre-metered and self-metered methods selected from airblade coating, knife coating, airknife coating, squeegee coating, impregnation coating, dip coating, reverse roll coating, transfer roll coating, gravure coating, kiss coating, flow coating, cascade flow coating, slide coating, curtain coating, mono- and multilami- nar slot die coating, spray coating, spin coating, or printing methods such as relief printing, intaglio printing, rotogravure printing, flexographic printing, offset printing, inkjet printing, letter- press printing, pad printing, heatseal printing or screenprinting methods. The application can also be continuous or semicontinuous, for example when the carrier material is moving, for example a permanently or intermittently moving belt.
Suitable carrier materials are firstly all materials which enable simple detachment of the finished multilayer film. Examples of these include glass, metals such as galvanized steel sheet or stainless steel, polymers such as silicones or polyethylene terephthalate, polymer-coated paper, such as silicone paper, etc. Suitable carrier materials are secondly monolaminar or multilaminar polymer films which remain as film layers in the multilayer film of the invention. With regard to the composition of these carrier materials, reference is made to the disclosure relating to the polymer composition P1 and the disclosure relating to polymers P2.
The increase in viscosity in layers i2), i4) and i6) can be effected by means of standard methods and generally depends on the form in which pourable compositions capable of film formation have been applied in steps i1 ), i3) and i5). If they have been applied as a melt, for example, there is generally already an increase in viscosity in the course of cooling. The cooling can be effected by simply leaving the carrier material to stand or by active cooling, such as cooling of the carrier material, jetting with a cool gas (jet), cooling in a cold room/refrigerator and the like. If the free-flowing composition capable of film formation has been applied in the form of a solution or dispersion, it is generally necessary to remove at least some of the solvent, which can be effected, for example, by simply leaving the carrier material to stand, drying with an air jet or hot
air jet, drying in drying cabinets, heating of the carrier material, application of a reduced pressure, optionally with simultaneous supply of heat, IR irradiation, microwave radiation, for exam ple in a corresponding oven, and the like. Should the composition be curable, for example because the polymers present therein comprise as yet unconverted polymerizable/condensable groups, the increase in viscosity can alternatively or additionally be effected by curing the poly mer. The measures suitable for curing depend on the polymerizable/condensable groups present. For instance, ethylenically unsaturated crosslinkable groups are especially cured by UV radiation; condensable groups, by contrast, generally cure either by being left to stand or with supply of heat. The heat can again be supplied as described above, i.e., for example, by incidence of warm or hot air or other warm or hot gases, drying in drying cabinets, heating of the carrier material, IR irradiation and the like. It is also possible to gel the solution or dispersion applied by cooling, in the sense of forming a physical network extended over macroscopic di- mensions, which likewise results in an increase in viscosity.
In a specific embodiment, the pourable compositions capable of film formation for two or more than two of the layers that form the multilayer film are applied by a wet-on-wet application method. The application in i3), i5) etc. can thus be effected wet-on-wet, meaning that the next layer can also be applied to the layer applied in step i 1 ), i3) and/or i5) without an explicit step for increasing viscosity having been conducted beforehand. This is especially true when the layer to which the next polymer layer is applied is sufficiently thin, such that it solidifies sufficiently even without being explicitly left to stand, dried, heated, cured, etc. before the next layer is applied, and there is no complete mixing with the components of the next layer. This is also true when the two layers, i.e. those to which application is effected, and the layer applied subsequently do not have any strong tendency to mix, for example because one layer is based on an aqueous polymer solution/dispersion and the other on a hydrophobic organic solution/dispersion or a hydrophobic melt.
The polymers applied in steps i 1 ), i3), i5) etc. are film-forming polymers. One or more than one of the layers comprising film-forming polymers may additionally comprise at least one additive.
In a particular embodiment, after steps i1 ), i2), i3), i4), i5) and/or a6), it is also possible to apply one or more layers that do not comprise any film-forming polymers. These are especially layers comprising components (functional materials) connected to the desired end use of the multi layer film. Should the film serve, for example, in or as a washing composition or as a sheath for washing compositions, these optional further layers may comprise surfactants, builders, cobuilders, bleaches, enzymes, graying inhibitors, optical brighteners, fragrances, dyes, etc. These components may, like the polymer layers too, be applied in solution/dispersion or melt. Suitable application techniques here too are those mentioned above.
The application of these layers may also be followed by a step of increasing the viscosity, or the next layer can be applied wet-on-wet. The statements made above apply analogously.
If the above-described layers that are applied do not comprise any film-forming polymers but do comprise components connected to the desired end use of the multilayer film, it is possible after
steps M ), i2), i3), i4), i5) and/or i6), especially after steps M ), i3) and/or i5), to emboss or punch the polymer layer, so as to give rise to recesses in which the functional materials applied at a later stage can be accommodated in relatively large amounts. This can be effected by means of standard embossing, printing, stamping and punching tools.
The process of the invention allows the production of multilayer films without a complex lamina- tion method in which the individual films have to be bonded to one another. It will be appreciated that the multilayer films of the invention can also be produced, as described above, by bond ing two or more than two film layers to one another by laminating. For instance, multilaminar polymer films which serve as carrier material for application of further film layers may be provided by bonding two or more than two film layers to one another by laminating.
For provision of the compositions applied in steps i1 ), i3), i5) etc., for example, a component which is capable of film formation and is selected from polymer compositions P1 , at least one polymer P2, optionally after addition of at least one additive, is melted or dissolved in a suitable solvent or solvent mixture, the pourable composition thus obtained is poured out to form a layer and the solvent or solvent mixture is optionally removed by evaporation.
Suitable solvents and solvent mixtures are known to the person skilled in the art. The solvent is preferably selected from water, ethanol, n-propanol, isopropanol, ethylene glycol, diethylene glycol, 1 ,2-propylene glycol, 1 ,2-dipropylene glycol and mixtures thereof. In a specific embodiment, the solvent used is selected from water and a mixture of water and at least one solvent other than water, selected from ethanol, n-propanol, isopropanol, ethylene glycol, diethylene glycol, 1 ,2-propylene glycol, 1 ,2-dipropylene glycol and mixtures thereof.
The multilayer film can be applied to a steel belt or a heated roller using single or multi-layer casting or coating tools such as slot nozzles, doctor blade, curtain coating, cascade casting, etc. In this case, one or more layers can be applied simultaneously and the other layers optionally on a different position of the steel strip or the roller. In another embodiment, another layer can be applied in a post-drying step on the freestanding film after detaching from the carrier material (steel strip or roller). Roller-based coating processes are particularly suitable for this subsequent coating.
In a further embodiment, it is also possible to combine a plurality of steel strip or roller-dryer installations in such a way that two separately produced single-layer or multilayer films are connected to one another directly in a lamination step. This step can also be carried out with a pre viously prepared or commercially available film. The laminating step of the films may be carried out before detaching a film, immediately after detaching the film and before drying of the freestanding film, during the drying of the freestanding film or after the drying, but before the wind ing. A separate lamination of two films is also possible. In all variants of the lamination, lamination is possible solely by means of a targeted adjustment of the residual moisture in the film and correspondingly selected line loads.
A specific embodiment is a process for producing a washing- and cleaning-active single layer or multilayer polymer film, which comprises at least one additive. Additives can be added before or during the film formation in step b). Whether the addition takes place before or during step b) depends on the type and effect of the particular additive. For the film formation in step b) additives can be added to the aqueous composition before and/or during the film production.
In the case of multilayer films, an individual layer or a plurality of but not all the layers or all the layers may each comprise one or more than one additive. Alternatively, or additionally, it is pos sible that at least one additive is present between at least two layers.
The additives may be auxiliaries for adjustment of the properties of the pourable compositions capable of film formation, typical additives of the washing and cleaning compositions or mixtures thereof.
A special embodiment is a single layer film that comprises at least one additive. A further special embodiment is a multilayer film in which at least one of the layers includes an additive. Particular preference is given to single layer and multilayer films in which at least one of the layers includes an additive which is a constituent customary for washing and cleaning compositions. In that case, the additive is preferably selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, bleach activators, bleach catalysts, enzymes, bases, corrosion inhibitors, foam inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, bitter agents such as Bitrex®, antiyellowing agents, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, bitter substances, fluorescers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, anti-yellowing agents, cor rosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and antislip agents, plasticizers, scavengers, polymers other than the polymers of the polymer composition P1 and other than the polymers P2, agents for modification of gas permeability and water vapor permeability, antistats, glidants, slip agents, UV absorbers and mixtures thereof.
In a preferred embodiment of the inventive process for the production of a multilayer film, two enzyme-containing layers are bound to each other in a lamination process at low temperature. The wash-active layer, comprising or consisting of P1 ) or P2), may serve not only the purpose of being wash-active, but also can be used as lamination adhesive, due to their special compo sitions and associated properties (tackiness).
The residual moisture of the wash-active layer, comprising or consisting of P1 ) or P2, is prefer ably lower than 15 % by weight, more preferably equal to or lower than 10 % by weight.
The temperature during the lamination process is preferably lower than 100 °C, more preferably lower than 80 °C, even more preferably lower than 50 °C and most preferably lower than 30 °C.
In an embodiment of the inventive process for producing a water-soluble multilayer film, at least one layer, preferably an enzyme-containing layer, is laminated at room temperature onto any of the other layers.
In order to make the polymer films more flexible, plasticizers can be added to them before or during production. For production of pourable compositions capable of film formation, preferably 0.5% to 30% by weight, more preferably 2% to 20% by weight and especially 3% to 15% by weight of plasticizer is used, based on the total weight of the composition.
Suitable plasticizers are alkyleneamines, alkanolamines, polyols, such as alkylene glycols and oligoalkylene glycols, e.g. 2-methyl-1 ,3-propanediol, 3-methyl-1 ,5-pentadiol, hydroxypropylglyc- erol, neopentyl glycol, alkoxylated glycerol (such as e.g. Voranol® from Dow Chemicals), water- soluble polyesterpolyols (such as e.g. TriRez from Geo Specialty Chemicals) and mixtures thereof. Suitable plasticizers are also polyetherpolyols, which are available under the name Lu- pranol® from BASF SE. The term“alkyleneamines” refers to condensation products of alka- nolamines with ammonia or primary amines, e.g. ethyleneamines are obtained by reaction of monoethanolamine with ammonia in the presence of a catalyst. Here, the following result as main components: ethylenediamine, piperazine, diethylenetriamine and aminoethylethanola- mine.
Preferably, the plasticizers are selected from glycerol, diglycerol, propylene glycols with a weight-average molecular weight of up to 400, e.g. dipropylene glycol, ethylene glycol, diethylene glycol, triethylene glycol, tetraethylene glycol, sorbitol, isopentyldiol, polyethylene glycol, trimethylolpropane, diethylenetriamine, triethylenepentamine, triethanolamine and mixtures thereof.
In order to make the polymer films according to the invention more resistant to aggressive ingredients (such as e.g. chlorine-releasing compounds, as are used in the area of disinfection of water, etc.), so-called“scavengers” (capture molecules) can be added to the film. Suitable scavengers are polyamines, polymeric polyamines, such as polyethyleneimines,
poly(amidoamines) and polyamides. Moreover, it is also possible to use ammonium sulfate, primary and secondary amines with a low vapor pressure, such as ethanolamines, amino acid and salts thereof, and also polyamino acid and salts thereof, fatty amines, glucosamines and other aminated sugars. Furthermore, reducing agents, such as sulfites, bisulfites, thiosulfites, thiosulfates, iodides, nitrites and antioxidants such as carbamates, ascorbates and mixtures thereof can be used.
It is additionally possible to subject at least one surface or both surfaces of the single and multilayer films of the invention to at least partial coating with at least one additive. Such a treatment may serve, for example, to provide the surface with particular properties, such as nonstick action, antistatic action, hydrophilic or hydrophobic properties, etc. It is thus possible to provide the single and multilayer films, for example, with better detachment properties from the carrier material used in the production, better roll-off properties, better glide properties, reduced tack, better compatibility with particular components ensheathed or coated therewith, etc. According to the
nature and formulation of the additive, the application can be effected by standard methods, for example by spraying, dipping, powder application, etc. Suitable additives for coating of the sur face of the multilayer films of the invention are, for example, talc, surfactants such as silicone- containing surfactants, waxes, etc.
A further subject of the present invention is a process for producing a water-soluble container comprising the steps of:
forming an open pouch from a first water-soluble film;
filling at least part of the pouch with a composition;
covering the filled pouch with a second water-soluble film
sealing the first water-soluble film of the filled pouch with the second water-soluble film, wherein
at least one of the first or second water-soluble films is a multi-layered film as above, and wherein before the sealing step the second water-soluble film covering the filled pouch is contacted with water.
Also the use of an inventive multilayer film, or obtainable by an inventive process, as a washing composition or as a cleaning composition is a subject of the present invention.
A further inventive subject is the use of a multilayer film as defined above or obtainable by a process as defined above, for at least partial ensheathing of a liquid and/or solid washing and cleaning composition.
Another inventive subject is a sheath or coating for a washing composition portion or cleaning composition portion, comprising or consisting of a multilayer film as defined above or obtainable by a process as defined above.
Furthermore, a subject of the invention is also a washing or cleaning composition comprising:
A) at least one sheath and/or coating comprising or consisting of a washing- and cleaning- active multilayer film as defined above or obtainable by a process as defined above,
B) at least one surfactant,
C) optionally at least one builder,
D) optionally at least one bleach system,
E) optionally at least one further additive, preferably selected from enzymes, bases, corro- sion inhibitors, defoamers, dyes, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluores- cers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antish- rink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, corrosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and antislip agents and UV absorbers, and
F) optionally water.
According to this invention, the enzyme EN) is preferably selected from an oxidoreductase (EC 1), a transferase (EC 2), a hydrolase (EC 3), a lyase (EC 4), a Isomerase (EC 5), or a Ligase (EC 6) (EC-numbering according to Enzyme Nomenclature, Recommendations (1992) of the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology in cluding its supplements published 1993-1999).
Most preferably, the enzyme is a hydrolase (EC 3), preferably, a glycosidase (EC 3.2) or a pep tidase (EC 3.4). Especially preferred enzymes are enzymes selected from the group consisting of an amylase (in particular an alpha-amylase (EC 3.2.1.1 )), a cellulase (EC 3.2.1.4), a lactase (EC 3.2.1 .108), a mannanase (EC 3.2.1.25), a lipase (EC 3.1.1.3), a phytase (EC 3.1.3.8), a nuclease (EC 3.1 .1 1 to EC 3.1.31 ), and a protease (EC 3.4).
According to this invention, the enzyme EN) is preferably selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
Unless otherwise noted, the terms used herein are to be understood according to conventional usage by those of ordinary skill in the relevant art. In addition to the definitions of terms provided herein, definitions of common terms in molecular biology may also be found in Rieger et al.,
1991 Glossary of genetics: classical and molecular, 5th Ed., Berlin: Springer-Verlag; and in Cur rent Protocols in Molecular Biology, F.M. Ausubel et al., Eds., Current Protocols, a joint venture between Greene Publishing Associates, Inc. and John Wiley & Sons, Inc., (1998 Supplement).
Production of enzymes
Enzymes are generally produced commercially by using recombinant cells which express the desired enzyme by cultivation of the same under conditions suitable for expression of the desired enzyme. The term“recombinant cell” (also called“genetically modified cell” herein) refers to a cell which has been genetically altered, modified or engineered such that it exhibits an altered, modified or different genotype as compared to the wild-type cell which it was derived from. The“recombinant cell” may comprise an exogenous polynucleotide. The recombinant cell may comprise exogenous polynucleotide encoding for a certain protein or enzyme and therefore may express said protein or enzyme.
The term "heterologous” (or exogenous or foreign or recombinant) polypeptide is defined herein as a polypeptide that is not native to the host cell, a polypeptide native to the host cell in which structural modifications, e.g., deletions, substitutions, and/or insertions, have been made to alter the native polypeptide, or a polypeptide native to the host cell whose expression is quantitatively altered or whose expression is directed from a genomic location different from the native host cell as a result of manipulation of the DNA of the host cell by recombinant DNA techniques, e.g.,
a stronger promoter. Similarly, the term“heterologous” (or exogenous or foreign or recombinant) polynucleotide refers to a polynucleotide that is not native to the host cell, a polynucleotide native to the host cell in which structural modifications, e.g., deletions, substitutions, and/or insertions, have been made to alter the native polynucleotide, or a polynucleotide native to the host cell whose expression is quantitatively altered as a result of manipulation of the regulatory elements of the polynucleotide by recombinant DNA techniques, e.g., a stronger promoter, or a polynucleotide native to the host cell, but integrated not within its natural genetic environment as a result of genetic manipulation by recombinant DNA techniques.
With respect to two or more polynucleotide sequences or two or more amino acid sequences, the term "heterologous” is used to characterized that the two or more polynucleotide sequences or two or more amino acid sequences are naturally not occurring in the specific combination with each other.
The term“native” (or wildtype or endogenous) cell or organism and“native” (or wildtype or endoge nous) polynucleotide or polypeptide refers to the cell or organism as found in nature and to the polynucleotide or polypeptide in question as found in a cell in its natural form and genetic environment, respectively (i.e., without there being any human intervention).
Cultivation normally takes place in a suitable nutrient medium allowing the recombinant host cells to grow (this process may be called fermentation) and express the desired protein. At the end of the fermentation, fermentation broth is collected and may be further processed, wherein the fermentation broth comprises a liquid fraction and a solid fraction.
The desired protein or enzyme may be secreted (into the liquid fraction of the fermentation broth) or may not be secreted from the host cells (and therefore is comprised in the solid frac tion of the fermentation broth). Depending on this, the desired protein or enzyme may be recovered from the liquid fraction of the fermentation broth or from cell lysates. Recovery of the de- sired enzyme uses methods known to those skilled in the art. Suitable methods for recovery of proteins or enzymes from fermentation broth include but are not limited to collection, centrifugation, filtration, extraction, and precipitation.
The isolated polypeptide may then be further purified by a variety of procedures known in the art including, but not limited to, chromatography (e.g., ion exchange, affinity, hydrophobic, chroma- tofocusing, and size exclusion), electrophoretic procedures (e.g., preparative isoelectric focus- ing (IEF), differential solubility (e.g., ammonium sulfate precipitation), or extraction (see, e.g., Protein Purification, J.-C. Janson and Lars Ryden, editors, VCH Publishers, New York, 1989). The purified polypeptide may then be concentrated by procedures known in the art including, but not limited to, ultrafiltration and evaporation, in particular, thin film evaporation.
The final enzyme-comprising product may be liquid or aqueous and may be called enzyme concentrate. Liquid enzyme-comprising products may be dried to stabilize enzyme(s). However, dried enzymes need to be re-solved in solvent such as water or water-containing buffer prior to
use. Hence, enzyme-comprising products are often aqueous before they are used in applications.
“Liquid enzyme concentrate” herein means any liquid enzyme-comprising product comprising at least one type of enzyme.“Liquid” in the context of enzyme concentrate is related to the physi cal appearance at 20°C and 101.3 kPa.
Liquid enzyme concentrates may comprise amounts of enzyme in the range of 0.1 % to 40% by weight, or 0.5% to 30% by weight, or 1 % to 25% by weight, all relative to the total weight of the enzyme concentrate.
The liquid enzyme concentrate may comprise more than one type of enzyme.
In one embodiment, liquid enzyme concentrate is an aqueous enzyme concentrate.
“Aqueous enzyme concentrate” herein means any aqueous enzyme-comprising product comprising at least one type of enzyme, which may result e.g. from fermentation. Aqueous enzyme concentrate may also mean that at least one type of enzyme in its solid state has been dissolved in aqueous solvent.
Aqueous enzyme concentrates of the invention may comprise water in amounts of more than about 50% by weight, more than about 60% by weight, more than about 70% by weight, or more than about 80% by weight, all relative to the total weight of the enzyme concentrate.
Liquid enzyme concentrate of the invention may comprise residual components such as salts originating from the fermentation medium, cell debris originating from the production host cells, metabolites produced by the production host cells during fermentation.
In one embodiment, residual components may be comprised in liquid enzyme concentrates in amounts less than 30% by weight, less than 20% by weight less, than 10% by weight, or less than 5% by weight, all relative to the total weight of the aqueous enzyme concentrate.
Lipases and cutinases
In one embodiment, the water-soluble multilayer film of the invention comprises at least one lipase.“Lipases”,“lipolytic enzyme”,“lipid esterase”, all refer to an enzyme of EC class 3.1.1 (“carboxylic ester hydrolase”). Such an enzyme may have lipase activity (or lipolytic activity; triacylglycerol lipase, EC 3.1.1.3), cutinase activity (EC 3.1.1.74; enzymes having cutinase ac- tivity may be called cutinase herein), sterol esterase activity (EC 3.1.1.13) and/or wax-ester hydrolase activity (EC 3.1.1.50). Lipases include those of bacterial or fungal origin.
Commercially available lipase enzymes include but are not limited to those sold under the trade names Lipolase™, Lipex™, Lipolex™ and Lipoclean™ (Novozymes A/S), Lumafast (originally from Genencor) and Lipomax (Gist-Brocades/ now DSM).
In one aspect of the invention, a suitable lipase is selected from the following:
lipases from Humicola (synonym Thermomyces), e.g. from H. lanuginosa ( T. lanuginosus) as described in EP 258068, EP 305216, WO 92/05249 and WO 2009/109500 or from H. inso/ens as described in WO 96/13580,
lipases derived from Rhizomucor miehei as described in WO 92/05249.
lipase from strains of Pseudomonas (some of these now renamed to Burkho!deria ), e.g. from P. a I cali genes or P. pseudoalcaligenes (EP 218272, WO 94/25578, WO 95/30744, WO 95/35381 , WO 96/00292), P. cepacia (EP 331376), P. stutzeri (G 1372034), P. fiuo- rescens, Pseudomonas sp. strain SD705 (WO 95/06720 and WO 96/27002), P. wiscon- sinensis (WO 96/12012), Pseudomonas mendocina (NO 95/14783), P. g!umae (WO 95/35381 , WO 96/00292)
lipase from Streptomyces griseus (WO 201 1/150157) and S. pristinaespiralis (WO 2012/137147), GDSL-type Streptomyces lipases (WO 2010/065455),
lipase from Thermobifida fusca as disclosed in WO 201 1/084412,
lipase from Geobacillus stearothermophilus as disclosed in WO 201 1/084417,
Bacillus lipases, e.g. as disclosed in WO 00/60063, lipases from B. subtilis es disclosed in Dartois et al. (1992), Biochemica et Biophysica Acta, 1 131 , 253-360 or WO 201 1/084599, B. stearothermophilus (JP S64-074992) or B. pumi/us (WO 91/16422).
Lipase from Candida antarctica as disclosed in WO 94/01541 .
cutinase from Pseudomonas mendocina (US 5389536, WO 88/09367)
cutinase from Magnaporthe grisea (WO 2010/107560),
cutinase from Fusarum soiani pisi as disclosed in WO 90/09446, WO 00/34450 and WO 01/92502
cutinase from Humicoia lanuginosa as disclosed in WO 00/34450 and WO 01/92502
Suitable lipases include also those referred to as acyltransferases or perhydrolases, e.g. acyl- transferases with homology to Candida antarctica lipase A (WO 2010/1 1 1 143), acyltransferase from Mycobacterium smegmatis (WO 2005/056782), perhydrolases from the CE7 family (WO 2009/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant (WO 2010/100028).
Suitable lipases include also those which are variants of the above described lipases and/or cutinases which have lipolytic activity. Such suitable lipase variants are e.g. those which are developed by methods as disclosed in WO 95/22615, WO 97/04079, WO 97/07202, WO 00/60063, WO 2007/087508, EP 407225 and EP 260105.
Suitable lipases/cutinases include also those, which are variants of the above described lipas- es/cutinases which have lipolytic activity. Suitable lipase/cutinase variants include variants with at least 40 to 100% identity when compared to the full length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment lipase/cutinase variants having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent en- zyme as disclosed above.
In another embodiment, the invention relates to lipase/cutinase variants comprising conservative mutations not pertaining the functional domain of the respective lipase/cutinase. Li pase/cutinase variants of this embodiment having lipolytic activity may be at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least
80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least
95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
Enzyme variants may be defined by their sequence identity when compared to a parent en- zyme. Sequence identity usually is provided as“% sequence identity” or“% identity”. To determine the percent-identity between two amino acid sequences in a first step a pairwise sequence alignment is generated between those two sequences, wherein the two sequences are aligned over their complete length (i.e., a pairwise global alignment). The alignment is generated with a program implementing the Needleman and Wunsch algorithm (J. Mol. Biol. (1979) 48, p. 443- 453), preferably by using the program“NEEDLE” (The European Molecular Biology Open Software Suite (EMBOSS)) with the programs default parameters (gapopen=10.0, gapextend=0.5 and matrix=EBLOSUM62). The preferred alignment for the purpose of this invention is that alignment, from which the highest sequence identity can be determined.
After aligning the two sequences, in a second step, an identity value shall be determined from the alignment. Therefore, according to the present invention the following calculation of percent- identity applies:
%-identity = (identical residues / length of the alignment region which is showing the respective sequence of this invention over its complete length) *100. Thus sequence identity in relation to comparison of two amino acid sequences according to this embodiment is calculated by dividing the number of identical residues by the length of the alignment region which is showing the re spective sequence of this invention over its complete length. This value is multiplied with 100 to give“%-identity”.
For calculating the percent identity of two DNA sequences the same applies as for the calculation of percent identity of two amino acid sequences with some specifications. For DNA sequences encoding for a protein the pairwise alignment shall be made over the complete length of the coding region from start to stop codon excluding introns. For non-protein-coding DNA sequences the pairwise alignment shall be made over the complete length of the sequence of this invention, so the complete sequence of this invention is compared to another sequence, or regions out of another sequence. Moreover, the preferred alignment program implementing the Needleman and Wunsch algorithm (J. Mol. Biol. (1979) 48, p. 443-453) is“NEEDLE” (The European Molecular Biology Open Software Suite (EMBOSS)) with the programs default parame ters (gapopen=10.0, gapextend=0.5 and matrix=EDNAFULL).
The following example is meant to illustrate the embodiments of the invention, which is on two nucleotide sequences, but same calculations apply to protein sequences:
Seq A: AAGATACTG length: 9 bases
Seq B: GATCTGA length: 7 bases
Hence, the shorter sequence is sequence B.
Producing a pairwise global alignment which is showing both sequences over their complete lengths results in
Seq A: AAGATACTG-
I I I I I I
Seq B: —GAT-CTGA
The Ί” symbol in the alignment indicates identical residues (which means bases for DNA or amino acids for proteins). The number of identical residues is 6.
The symbol in the alignment indicates gaps. The number of gaps introduced by alignment within the Seq B is 1. The number of gaps introduced by alignment at borders of Seq B is 2, and at borders of Seq A is 1.
The alignment length showing the aligned sequences over their complete length is 10.
Producing a pairwise alignment which is showing the shorter sequence over its complete length according to the invention consequently results in:
Seq A:
Producing a pairwise alignment which is showing sequence A over its complete length accord ing to the invention consequently results in:
Seq A:
Producing a pairwise alignment which is showing sequence B over its complete length accord ing to the invention consequently results in:
Seq A:
The alignment length showing the shorter sequence over its complete length is 8 (one gap is present which is factored in the alignment length of the shorter sequence).
Accordingly, the alignment length showing Seq A over its complete length would be 9 (meaning Seq A is the sequence of the invention).
Accordingly, the alignment length showing Seq B over its complete length would be 8 (meaning Seq B is the sequence of the invention).
According to the example provided above, %-identity is: for Seq A being the sequence of the invention (6 / 9) * 100 = 66.7 %; for Seq B being the sequence of the invention (6 / 8) * 100 = 75%.
Enzyme variants may be defined by their sequence similarity when compared to a parent en zyme. Sequence similarity usually is provided as“% sequence similarity” or“%-similarity”. For calculating sequence similarity in a first step a sequence alignment has to be generated as described above. In a second step, the percent-similarity has to be calculated, whereas percent sequence similarity takes into account that defined sets of amino acids share similar properties, e.g., by their size, by their hydrophobicity, by their charge, or by other characteristics. Herein, the exchange of one amino acid with a similar amino acid is referred to as‘‘conservative muta tion”. Enzyme variants comprising conservative mutations appear to have a minimal effect on protein folding resulting in certain enzyme properties being substantially maintained when compared to the enzyme properties of the parent enzyme.
For determination of %-similarity according to this invention the following applies, which is also in accordance with the BLOSUM62 matrix, which is one of the most used amino acids similarity matrix for database searching and sequence alignments
Amino acid A is similar to amino acids S
Amino acid D is similar to amino acids E; N
Amino acid E is similar to amino acids D; K; Q
Amino acid F is similar to amino acids W; Y
Amino acid H is similar to amino acids N; Y
Amino acid I is similar to amino acids L; M; V
Amino acid K is similar to amino acids E; Q; R
Amino acid L is similar to amino acids I; M; V
Amino acid M is similar to amino acids I; L; V
Amino acid N is similar to amino acids D; H; S
Amino acid Q is similar to amino acids E; K; R
Amino acid R is similar to amino acids K; Q
Amino acid S is similar to amino acids A; N; T
Amino acid T is similar to amino acids S
Amino acid V is similar to amino acids I; L; M
Amino acid W is similar to amino acids F; Y
Amino acid Y is similar to amino acids F; H; W.
Conservative amino acid substitutions may occur over the full length of the sequence of a poly peptide sequence of a functional protein such as an enzyme. In one embodiment, such mutations are not pertaining the functional domains of an enzyme. In another embodiment conservative mutations are not pertaining the catalytic centers of an enzyme.
Therefore, according to the present invention the following calculation of percent-similarity applies:
%-similarity = [ (identical residues + similar residues) / length of the alignment region which is showing the respective sequence of this invention over its complete length ] *100. Thus se quence similarity in relation to comparison of two amino acid sequences herein is calculated by dividing the number of identical residues plus the number of similar residues by the length of the alignment region which is showing the respective sequence of this invention over its complete length. This value is multiplied with 100 to give“%-similarity”.
Especially, variant enzymes comprising conservative mutations which are at least m percent similar to the respective parent sequences with m being an integer between 50 and 100, prefer ably 50, 55, 60, 65, 70, 75, 80, 85, 90, 91 , 92, 93, 94, 95, 96, 97, 98 or 99 compared to the full length polypeptide sequence, are expected to have essentially unchanged enzyme properties. Variant enzymes described herein with m percent-similarity when compared to a parent en- zyme, have enzymatic activity.
Lipases according to the invention have“lipolytic activity”. The methods for determining lipolytic activity are well-known in the literature (see e.g. Gupta et al. (2003), Biotechnol. Appl. Biochem. 37, p. 63-71). E.g. the lipase activity may be measured by ester bond hydrolysis in the substrate para-nitrophenyl palmitate (pNP-Palmitate, C:16) and releases pNP which is yellow and can be detected at 405 nm.
Lipase variants may have lipolytic activity according to the present invention when said lipase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the lipolytic activity of the re spective parent lipase.
Proteases
In one embodiment, the water-soluble multilayer film of the invention comprises at least one protease. Enzymes having proteolytic activity are called“proteases” or peptidases in the context of the invention and are members of class EC 3.4.
Preferred proteases are further classified as aminopeptidases (EC 3.4.11 ), dipeptidases (EC 3.4.13), dipeptidyl-peptidases and tripeptidyl-peptidases (EC 3.4.14), peptidyl-dipeptidases (EC 3.4.15), serine-type carboxypeptidases (EC 3.4.16), metallocarboxypeptidases (EC 3.4.17), cysteine-type carboxypeptidases (EC 3.4.18), omega peptidases (EC 3.4.19), serine endopep- tidases (EC 3.4.21 ), cysteine endopeptidases (EC 3.4.22), aspartic endopeptidases (EC 3.4.23), metallo-endopeptidases (EC 3.4.24), threonine endopeptidases (EC 3.4.25), endopep tidases of unknown catalytic mechanism (EC 3.4.99).
The protease in the context of the present invention may be an endopeptidase of any kind or a mixture of endopeptidases of any kind. In one embodiment, protease according to the invention is selected from serine protease (EC 3.4.21).
Serine proteases or serine peptidases are characterized by having a serine in the catalytically active site, which forms a covalent adduct with the substrate during the catalytic reaction. A ser ine protease according to the invention is selected from the group consisting of chymotrypsin (e.g., EC 3.4.21.1), elastase (e.g., EC 3.4.21.36), elastase (e.g., EC 3.4.21.37 or EC 3.4.21.71 ), granzyme (e.g., EC 3.4.21.78 or EC 3.4.21 .79), kallikrein (e.g., EC 3.4.21.34, EC 3.4.21.35, EC 3.4.21.118, or EC 3.4.21.119,) plasmin (e.g., EC 3.4.21.7), trypsin (e.g., EC 3.4.21.4), thrombin (e.g., EC 3.4.21.5,) and subtilisin (also known as subtilopeptidase, e.g., EC 3.4.21.62), the latter hereinafter also being referred to as“subtilisin”.
In general, the three main types of protease activity (proteolytic activity) are: trypsin-like, where there is cleavage of amide substrates following Arg (N) or Lys (K) at P1 , chymotrypsin-like where cleavage occurs following one of the hydrophobic amino acids at P1 , and elastase-like with cleavage following an Ala (A) at P1.
A sub-group of the serine proteases tentatively designated subtilases has been proposed by Siezen et al. (1991), Protein Eng. 4:719-737 and Siezen et al. (1997), Protein Science 6:501 - 523. They are defined by homology analysis of more than 170 amino acid sequences of serine proteases previously referred to as subtilisin-like proteases. A subtilisin was previously often defined as a serine protease produced by Gram-positive bacteria or fungi, and according to Siezen et al. now is a subgroup of the subtilases. A wide variety of subtilases have been identified, and the amino acid sequence of a number of subtilases has been determined. For a more detailed description of such subtilases and their amino acid sequences reference is made to Siezen et al. (1997), Protein Science 6:501 -523.
The subtilases may be divided into 6 sub-divisions, i.e. the subtilisin family, thermitase family, the proteinase K family, the lantibiotic peptidase family, the kexin family and the pyrolysin family.
A subgroup of the subtilases are the subtilisins which are serine proteases from the family S8 as defined by the MEROPS database (http://merops.sanger.ac.uk). Peptidase family S8 con tains the serine endopeptidase subtilisin and its homologues. In subfamily S8A, the active site residues frequently occurs in the motifs Asp-Thr/Ser-Gly (which is similar to the sequence motif in families of aspartic endopeptidases in clan AA), His-Gly-Thr-His and Gly-Thr-Ser-Met-Ala- Xaa-Pro. Most members of the family are active at neutral-mildly alkali pH. Many peptidases in the family are thermostable. Casein is often used as a protein substrate and a typical synthetic substrate is Suc-Ala-Ala-Pro-Phe-NHPhN02.
Prominent members of family S8, subfamily A are:
The subtilisin related class of serine proteases shares a common amino acid sequence defining a catalytic triad which distinguishes them from the chymotrypsin related class of serine proteases. Subtilisins and chymotrypsin related serine proteases both have a catalytic triad comprising aspartate, histidine and serine.
In the subtilisin related proteases the relative order of these amino acids, reading from the amino to carboxy-terminus is aspartate-histidine-serine. In the chymotrypsin related proteases the relative order, however is histidine-aspartate-serine. Thus, subtilisin herein refers to a serine protease having the catalytic triad of subtilisin related proteases. Examples include the subtilisins as described in WO 89/06276 and EP 0283075, WO 89/06279, WO 89/09830, WO 89/09819, WO 91/06637 and WO 91/02792.
Parent proteases of the subtilisin type (EC 3.4.21.62) and variants may be bacterial proteases. Said bacterial protease may be a Gram-positive bacterial polypeptide such as a Bacillus, Clostridium, Enterococcus, Geobacillus, Lactobacillus, Lactococcus, Oceanobacitius, Staphylococcus, Streptococcus, or Streptomyces protease, or a Gram-negative bacterial polypeptide such as a Campylobacter, E. co/i, Flavobacterium, Fusobacterium, Helicobacter, Hyobacter, Neisseria, Pseudomonas, Salmonella, or Ureaptasma protease. They act as unspecific endopepti- dases, i.e. they hydrolyze any peptide bonds. Their pH optimum is usually within the neutral to distinctly alkaline range. A review of this family is provided, for example, in "Subtilases: Subtil- isin-like Proteases" by R. Siezen, pages 75-95 in "Subtilisin enzymes", edited by R. Bott and C. Betzel, New York, 1996.
Commercially available protease enzymes include those sold under the trade names Alcalase®, Blaze®, Duralase™, Durazym™, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, Pri- mase®, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Co- ronase® Ultra, Neutrase®, Everlase® and Esperase® (Novozymes A/S), those sold under the tradename Maxatase®, Maxacal®, Maxapem®, Purafect®, Purafect® Prime, Purafect MA®, Purafect Ox®, Purafect OxP®, Puramax®, Properase®, FN2®, FN3®, FN4®, Excellase®, Eraser®, Ultimase®, Opticlean®, Effectenz®, Preferenz® and Optimase® (Danisco/DuPont), Axapem™ (Gist-Brocases N.V.), Lavergy™ pro (BASF), Bacillus ientus Alkaline Protease
(BLAP; sequence shown in Figure 29 of US 5,352,604) and variants thereof and KAP ( Bacillus alkalophilus subtilisin) from Kao.
In one aspect of the invention, the parent enzymes and variants may be a Bacillus alcalophilus, Bacillus amyloliquefaciens, Bacillus brevis, Bacillus circuians, Bacillus c/ausii, Bacillus coagu- lans, Bacillus firmus, Bacillus gibsonii, Bacillus lautus, Bacillus lentus, Bacillus Hcheniformis, Bacillus megaterium, Bacillus pumiius, Bacillus sphaericus , Bacillus stearothermophilus, Bacil lus subti!is, or Bacillus thuringiensis protease.
In one embodiment of the present invention, the subtilase is selected from the following:
subtilisin from Bacillus amyloliquefaciens BPN' (described by Vasantha et al. (1984) J. Bacteriol. Volume 159, p. 811-819 and JA Wells et al. (1983) in Nucleic Acids Research, Volume 1 1 , p. 791 1-7925),
subtilisin from Bacillus Hcheniformis (subtilisin Carlsberg; disclosed in EL Smith et al. (1968) in J. Biol Chem, Volume 243, pp. 2184-2191 , and Jacobs et al. (1985) in Nucl. Ac- ids Res, Vol 13, p. 8913-8926),
subtilisin PB92 (original sequence of the alkaline protease PB92 is described in EP 283075 A2),
subtilisin 147 and/or 309 (Esperase®, Savinase®) as disclosed in GB 1243784, subtilisin from Bacillus lentus as disclosed in WO 91/02792, such as from Bacillus lentus
DSM 5483 or the variants of Bacillus lentus DSM 5483 as described in WO 95/23221 , subtilisin from Bacillus alcalophilus (DSM 1 1233) disclosed in DE 10064983,
subtilisin from Bacillus gibsonii { DSM 14391 ) as disclosed in WO 2003/054184, subtilisin from Bacillus sp. (DSM 14390) disclosed in WO 2003/056017,
subtilisin from Bacillus sp. (DSM 14392) disclosed in WO 2003/055974,
subtilisin from Bacillus gibsonii {D M 14393) disclosed in WO 2003/054184,
subtilisin having SEQ ID NO: 4 as described in WO 2005/063974 or a subtilisin which is at least 40% identical thereto and having proteolytic activity,
subtilisin having SEQ ID NO: 4 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity,
subtilisin having SEQ ID NO: 7 as described in WO 2005/103244 or subtilisin which is at least 80% identical thereto and having proteolytic activity, and
subtilisin having SEQ ID NO: 2 as described in application DE 102005028295.4 or subtil isin which is this at least 66% identical thereto and having proteolytic activity.
Examples of useful proteases in accordance with the present invention comprise the variants described in: WO 92/19729, WO 95/23221 , WO 96/34946, WO 98/20115, WO 98/20116, WO 99/1 1768, WO 01/44452, WO 02/088340, WO 03/006602, WO 2004/03186, WO 2004/041979, WO 2007/006305, WO 201 1/036263, WO 2011/036264, and WO 201 1/072099. Suitable exam ples comprise especially protease variants of subtilisin protease derived from SEQ ID NO:22 as described in EP 1921 147 (which is the sequence of mature alkaline protease from Bacillus len tus DSM 5483) with amino acid substitutions in one or more of the following positions: 3, 4, 9,
15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103, 104, 106, 118,
120, 123, 128, 129, 130, 131 , 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and 274 (according to the BPN' numbering), which have proteolyt ic activity. In one embodiment, such a subtilisin protease is not mutated at positions Asp32, His64 and Ser221 (according to BPN’ numbering).
In one embodiment, the subtilisin has SEQ ID NO:22 as described in EP 1921 147, or a subtilisin which is at least 80% identical thereto and has proteolytic activity. In one embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is charac terized by having amino acid glutamic acid (E), or aspartic acid (D), or asparagine (N), or glutamine (Q), or alanine (A), or glycine (G), or serine (S) at position 101 (according to BPN’ numbering) and has proteolytic activity. In one embodiment, subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by having amino acid glutamic acid (E), or aspartic acid (D), at position 101 (according to BPN’ numbering) and has proteolytic activity. Such a subtilisin variant may comprise an amino acid substitution at position 101 , such as R101 E or R101 D, alone or in combination with one or more substitutions at positions 3, 4, 9, 15, 24, 27, 33, 36, 57, 68, 76, 77, 87, 95, 96, 97, 98, 99, 100, 101 , 102, 103, 104, 106, 118, 120, 123, 128, 129, 130, 131 , 154, 160, 167, 170, 194, 195, 199, 205, 206, 217, 218, 222, 224, 232, 235, 236, 245, 248, 252 and/or 274 (according to BPN’ numbering) and has proteolytic activity.
In another embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising at least the following amino acids (according to BPN’ numbering) and has proteolytic activity:
(a) threonine at position 3 (3T)
(b) isoleucine at position 4 (4I)
(c) alanine, threonine or arginine at position 63 (63A, 63T, or 63R)
(d) aspartic acid or glutamic acid at position 156 (156D or 156E)
(e) proline at position 194 (194P)
(f) methionine at position 199 (199M)
(g) isoleucine at position 205 (205I)
(h) aspartic acid, glutamic acid or glycine at position 217 (217D, 217E or 217G),
(i) combinations of two or more amino acids according to (a) to (h).
In another embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921 147 and is characterized by comprising one amino acid (according to (a)-(h)) or combinations according to (i) together with the amino acid 101 E, 101 D, 101 N, 101 Q, 101 A, 101 G, or 101 S (according to BPN’ numbering) and has proteolytic activity.
In one embodiment, a subtilisin is at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and is characterized by comprising the mutation (according to BPN’ numbering) R101 E, or S3T + V4I + V205I, or S3T + V4I + V199M + V205I + L217D, and has proteolytic activity.
In another embodiment, the subtilisin comprises an amino acid sequence having at least 80% identity to SEQ ID NO:22 as described in EP 1921147 and being further characterized by com prising R101 E and S3T, V4I, and V205I (according to the BPN’ numbering) and has proteolytic activity.
In another embodiment, a subtilisin comprises an amino acid sequence having at least 80% identical to SEQ ID NO:22 as described in EP 1921147 and being further characterized by comprising R101 E, and one or more substitutions selected from the group consisting of S156D, L262E, Q137H, S3T, R45E,D,Q, P55N, T58W,Y,L, Q59D,M,N,T, G61 D,R, S87E, G97S, A98D,E,R, S106A,W, N1 17E, H120V,D,K,N, S125M, P129D, E136Q, S144W, S161 T,
S163A,G, Y171 L, A172S, N185Q, V199M, Y209W, M222Q, N238H, V244T, N261T,D and L262N,Q,D (as described in WO 2016/096711 and according to the BPN’ numbering), and has proteolytic activity.
%-identity for subtilisin variants is calculated as disclosed above. Subtilisin variant enzymes as disclosed above which are at least n% identical to the respective parent sequences include variants with n being at least 40 to 100. Depending on the %-identity values applicable as provided above, subtilisin variants in one embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme.
In another embodiment, the invention relates to subtilisin variants comprising conservative mu tations not pertaining the functional domain of the respective subtilisin protease. Depending on the %-identity values applicable as provided above, subtilisin variants of this embodiment have proteolytic activity and are at least 40%, at least 45%, at least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
Proteases, including serine proteases, according to the invention have“proteolytic activity” or “protease activity” or“proteolytic activity”. This property is related to hydrolytic activity of a pro- tease (proteolysis, which means hydrolysis of peptide bonds linking amino acids together in a polypeptide chain) on protein containing substrates, e.g. casein, haemoglobin and BSA. Quanti tatively, proteolytic activity is related to the rate of degradation of protein by a protease or proteolytic enzyme in a defined course of time. The methods for analyzing proteolytic activity are well-known in the literature (see e.g. Gupta et al. (2002), Appl. Microbiol. Biotechnol. 60: 381 - 395).
According to the invention, proteolytic activity as such can be determined by using Succinyl-Ala- Ala-Pro-Phe-p-nitroanilide (Suc-AAPF-pNA, short AAPF; see e.g. DelMar et al. (1979), Analytical Biochem 99, 316-320) as substrate. pNA is cleaved from the substrate molecule by proteo-
lytic cleavage, resulting in release of yellow color of free pNA which can be quantified by meas- uring OD405. Other methods are known to those skilled in the art.
Protease variants may have proteolytic activity according to the present invention when said protease variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the proteolytic activity of the respective parent protease.
Preferably, the pi value (isoelectric point) of the subtilisin protease is between pH 7.0 and pH 10.0, preferably between pH 8.0 and pH 9.5.
Amylases
In one embodiment, the water-soluble multilayer film of the invention comprises at least one amylase.“Amylases” according to the invention (alpha and/or beta) include those of bacterial or fungal origin (EC 3.2.1.1 and 3.2.1.2, respectively). Chemically modified or protein engineered mutants are included.
Commercially available amylase enzymes include but are not limited to those sold under the trade names Duramyl™, Termamyl™, Fungamyl™, Stainzyme™, Stainzyme Plus™, Natala- se™, Liquozyme X and BAN™ (from Novozymes A/S), and Rapidase™, Purastar™,
Powerase™, Effectenz™ (MIOO from DuPont), Preferenz™ (S1000, S1 10 and F1000; from DuPont), PrimaGreen™ (ALL; DuPont), Optisize™ (DuPont).
In one aspect of the present invention, the amylase is a parent or variant enzyme which is selected from the following:
- amylases from Bacillus Hcheniformis having SEQ ID NO:2 as described in WO 95/10603. Suitable variants are those which are at least 90% identical to SEQ ID NO: 2 as described in WO 95/10603 and/or comprising one or more substitutions in the following positions:
15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 21 1 , 243, 264, 304, 305, 391 , 408, and 444 which have amylolytic activity. Such variants are described in WO 94/02597, WO 94/018314, WO 97/043424 and SEQ ID NO:4 of WO 99/019467.
- amylases from B. stearothermophilus having SEQ ID NO:6 as disclosed in WO 02/10355 or an amylase which is at least 90% identical thereto having amylolytic activity. Suitable variants of SEQ ID NO:6 include those which is at least 90% identical thereto and/or further comprise a deletion in positions 181 and/or 182 and/or a substitution in position 193.
- amylases from Bacillus sp.707 having SEQ ID NO:6 as disclosed in WO 99/19467 or an amylase which is at least 90% identical thereto having amylolytic activity.
- amylases from Bacillus halmapalus having SEQ ID NO:2 or SEQ ID NO:7 as described in WO 96/23872, also described as SP-722, or an amylase which is at least 90% identical to one of the sequences which has amylolytic activity.
- amylases from Bacillus sp. DSM 12649 having SEQ ID NO:4 as disclosed in WO
00/22103 or an amylase which is at least 90% identical thereto having amylolytic activity.
- amylases from Bacillus strain TS-23 having SEQ ID NO:2 as disclosed in WO
2009/061380 or an amylase which is at least 90 % identical thereto having amylolytic ac tivity.
- amylases from Cytophaga sp. having SEQ ID NO:1 as disclosed in WO 2013/184577 or an amylase which is at least 90% identical thereto having amylolytic activity.
- amylases from Bacillus megaterium DSM 90 having SEQ ID NO:1 as disclosed in WO 2010/104675 or an amylase which is at least 90% identical thereto having amylolytic activ ity.
Suitable amylases are comprising amino acids 1 to 485 of SEQ ID NO:2 as described in WO 00/60060 or amylases comprising an amino acid sequence which is at least 96% identical with amino acids 1 to 485 of SEQ ID NO:2 which have amylolytic activity.
Other suitable amylases are those having SEQ ID NO: 12 as described in WO 2006/002643 or amylases having at least 80% identity thereto and have amylolytic activity. Suitable amylases include those having at least 80% identity compared to SEQ ID NO:12 and/or comprising the substitutions at positions Y295F and M202LITV and have amylolytic activity.
Suitable amylases include those having SEQ ID NO:6 as described in WO 2011/098531 or am ylases having at least 80% identity thereto having amylolytic activity. Suitable amylases include those having at least 80% identity compared to SEQ ID NO:6 and/or comprising a substitution at one or more positions selected from the group consisting of 193 [G,A,S,T or M], 195
[F,W,Y,L,I or V], 197 [F,W,Y,L,I or V], 198 [Q or N], 200 [F,W,Y,L,I or V], 203 [F,W,Y,L,I or V], 206 [F,W,Y,N,L,I,V,H,Q,D or E], 210 [F,W,Y,L,I or V], 212 [F,W,Y,L,I or V], 213 [G,A,S,T or M] and 243 [F,W,Y,L,I or V] and have amylolytic activity.
Suitable amylases are those having SEQ ID NO:1 as described in WO 2013/001078 or amylas es having at least 85% identity thereto having amylolytic activity. Suitable amylases include those having at least 85% identity compared to SEQ ID NO:1 and/or comprising an alteration at two or more (several) positions corresponding to positions G304, W140, W189, D134, E260, F262, W284, W347, W439, W469, G476, and G477 and having amylolytic activity.
Further suitable amylases are those having SEQ ID NO:2 as described in WO 2013/001087 or amylases having at least 85% identity thereto and having amylolytic activity. Suitable amylases include those having at least 85% identity compared to SEQ ID NO:2 and/or comprising a dele- tion of positions 181 +182, or 182+183, or 183+184, which have amylolytic activity. Suitable am ylases include those having at least 85% identity compared to SEQ ID NO:2 and/or comprising a deletion of positions 181 +182, or 182+183, or 183+184, which comprise one or two or more modifications in any of positions corresponding to W140, W159, W167, Q169, W189, E194, N260, F262, W284, F289, G304, G305, R320, W347, W439, W469, G476 and G477 and have amylolytic activity.
Amylases also include hybrid a-amylase from above mentioned amylases as for example as described in WO 2006/066594.
Suitable amylases include also those which are variants of the above described amylases which have amylolytic activity.
Depending on the %-identity values applicable as provided above, amylase variants in one embodiment may be those which are least 40 to 100% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above. In one embodiment amylase variants having amylolytic activity may be at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% identical when compared to the full length polypeptide sequence of the parent enzyme as disclosed above.
In another embodiment, the invention relates to amylase variants comprising conservative mutations not pertaining the functional domain of the respective amylase. Depending on the %- identity values applicable as provided above, amylase variants in this embodiment may be amylases have amylolytic activity which may be least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98% or at least 99% similar when compared to the full length polypeptide sequence of the parent enzyme.
Amylases according to the invention have“amylolytic activity” or“amylase activity” according to the invention involves (endo)hydrolysis of glucosidic linkages in polysaccharides a-amylase activity may be determined by assays for measurement of a-amylase activity which are known to those skilled in the art. Examples for assays measuring a-amylase activity are: a-amylase activity can be determined by a method employing Phadebas tablets as substrate (Phadebas Amylase Test, supplied by Magle Life Science). Starch is hydrolyzed by the a- amylase giving soluble blue fragments. The absorbance of the resulting blue solution, measured spectrophotometrically at 620 nm, is a function of the a-amylase activity. The measured absorbance is directly proportional to the specific activity (activity/mg of pure a-amylase protein) of the a-amylase in question under the given set of conditions. a-amylase activity can also be determined by a method employing the Ethyliden-4-nitrophenyl- a-D-maltoheptaosid (EPS). D-maltoheptaoside is a blocked oligosaccharide which can be cleaved by an endo-amylase. Following the cleavage, the a-glucosidase included in the kit to digest the substrate to liberate a free PNP molecule which has a yellow color and thus can be measured by visible spectophotometry at 405nm. Kits containing EPS substrate and a- glucosidase is manufactured by Roche Costum Biotech (cat. No. 10880078103). The slope of the time dependent absorption-curve is directly proportional to the specific activity (activity per mg enzyme) of the a-amylase in question under the given set of conditions.
Amylase variants have amylolytic activity according to the present invention when said amylase variants exhibit at least 20%, at least 25%, at least 30%, at least 35%, at least 40%, at least 45%, at 10 least 50%, at least 55%, at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, or 100% of the amylolytic activity of the respective parent amylase.
In one embodiment, the water-soluble multilayer film of the invention comprises at least one perhydrolase. Suitable“perhydrolases” are capable of catalyzing a perhydrolysis reaction that results in the production of a peracid from a carboxylic acid ester (acyl) substrate in the pres ence of a source of peroxygen (e.g., hydrogen peroxide). While many enzymes perform this reaction at low levels, perhydrolases exhibit a high perhydrolysis:hydrolysis ratio, often greater than 1. Suitable perhydrolases may be of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
Examples of useful perhydrolases include naturally occurring Mycobacterium perhydrolase enzymes, or variants thereof. An exemplary enzyme is derived from Mycobacterium smegmatis. Such enzyme, its enzymatic properties, its structure, and variants thereof, are described in WO 2005/056782, WO 2008/063400, US 2008145353, and US 2007167344.
In one embodiment, the water-soluble multilayer film of the invention comprises at least one mannanase.“Mannanase” may be an alkaline mannanase of Family 5 or 26. It may be a wild- type from Bacillus or Humicoia, particularly B. agaradhaerens, B. Hcheniformis, B. haiodurans,
B. ciausii, or H. inso/ens. Suitable mannanases are described in WO 99/064619.
A commercially available mannanase is Mannaway® (Novozymes AIS).
In one embodiment, the water-soluble multilayer film of the invention comprises at least one peroxidase and/or oxidase. Suitable peroxidases and oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
An oxidase according to the invention include, in particular, any laccase enzyme comprised by the enzyme classification EC 1.10.3.2, or any fragment derived therefrom exhibiting laccase activity, or a compound exhibiting a similar activity, such as a catechol oxidase (EC 1 .10.3.1 ), an o-aminophenol oxidase (EC 1 .10.3.4), or a bilirubin oxidase (EC 1.3.3.5).
Preferred laccase enzymes are enzymes of microbial origin. The enzymes may be derived from plants, bacteria or fungi (including filamentous fungi and yeasts). Suitable examples from fungi include a laccase derivable from a strain of Aspergillus, Neurospora, e.g. N. crassa, Podospora, Botrytis, Collybia, Fames , Lentinus, P/eurotus, Tra metes, e.g. T. villosa and T. versicolor, Rhi- zoctonia, e.g. R. so!ani, Coprinopsis, e.g. C. cinerea, C. comatus, C. friesii, and C. pHcatiiis, Psathyrella, e.g. P. condelleana, Panaeotus , e.g. P. papilionaceus, Myceliophthora, e.g. M. thermophila, Schytaiidium, e.g. S. thermophilum, Polyporus, e.g. P. pinsitus, Phlebia, e.g. P. radiata (WO 92/01046), or Corio!us, e.g. C. hirsutus (JP 2238885).
A laccase may be derived from Coprinopsis or Myceliophthora. In one embodiment, a laccase is derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora ther- mophiia, as disclosed in WO 95/33836.
The laccase may be a bacterial laccase, e.g. the laccase may be a Gram positive bacterial pol ypeptide such as a Bacillus, Streptococcus, Streptomyces, Staphylococcus, Enterococcus, Lactobacillus, Lactococcus, Clostridium, Geobacillus, or OceanobaciHus laccase, or a Gram negative bacterial polypeptide such as an E. coH, Pseudomonas, Salmonella, Campylobacter, Heli cobacter, Fiavobacterium, Fusobacterium, Hyobacter, Neisseria, or Ureap!asma laccase.
In one embodiment, laccase is selected from those as described in SEQ ID NO: 2, 4, 6, and 8 of WO 2009/127702 and variants thereof.
The term“laccase activity” is defined herein as covered by enzyme classification EC 1 .10.3.2, or a similar activity, such as a catechol oxidase activity (EC 1.10.3.1), o-aminophenol oxidase activity (EC 1.10.3.4), or bilirubin oxidase activity (EC 1.3.3.5), that catalyzes the oxidation of a substrate using molecular oxygen.
"Laccase activity” is determined by oxidation of syringaldazin under aerobic conditions. The violet colour produced is measured at 530 nm. The analytical conditions are 19 mM syringaldazin, 23 mM Tris/maleate buffer, pH 7.5, 30°C, and 1 min reaction time.
Examples of other oxidases include, but are not limited to, amino acid oxidase, glucose oxidase, lactate oxidase, galactose oxidase, polyol oxidase (e.g., WO 2008/051491 ), and aldose oxi dase. Oxidases and their corresponding substrates may be used as hydrogen peroxide generating enzyme systems, and thus a source of hydrogen peroxide. Several enzymes, such as pe- roxidases, haloperoxidases and perhydrolases, require a source of hydrogen peroxide. By stud ying EC 1.1.3._, EC 1.2.3._, EC 1.4.3._, and EC 1.5.3._ or similar classes (under the International Union of Biochemistry), other examples of such combinations of oxidases and substrates are easily recognized by one skilled in the art.
Peroxidases (EC 1.11.1.7) utilize hydrogen peroxide as substrate. Examples of useful peroxidases include peroxidases from Coprinus, e.g. from C. cinereus, and variants thereof as those described in WO 93/24618, WO 95/10602, WO 98/10060 and WO 98/15257.
Commercially available peroxidases include Guardzyme™ (Novozymes A/S), PrimaGreen™
Oxy (DuPont).
“Peroxidase activity” may be measured by the ABTS method as described in Childs et al. 1975 (Biochemical J, 145, p. 93-103) and commercial kits are available from different suppliers. Other measuring methods are known to those known in the art.
A peroxidase for use in the invention also include a haloperoxidase enzyme, such as chlo- roperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxi-
dase activity. Haloperoxidases are classified according to their specificity for halide ions. Chlo- roperoxidases (E.C. 1.1 1.1.10) catalyze formation of hypochlorite from chloride ions.
In an embodiment, the haloperoxidase is a chloroperoxidase. In one embodiment, the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate-containing haloperoxidase. In one embodiment of the present invention the vanadate-containing haloperoxidase is combined with a source of chloride ion.
Haloperoxidases have been isolated from many different fungi, in particular from the fungus group dematiaceous hyphomycetes, such as Caidariomyces, e.g., C. fumago, Aiternaria, Cur- vularia, e.g., C. verrucuiosa and C. inaequa/is, Drechslera, Ulocladium and Botrytis. Haloperox idases have also been isolated from bacteria such as Pseudomonas , e.g. P. pyrrocinia, and Streptomyces, e.g. S. aureofaciens.
In one embodiment, the haloperoxidase is from Curvularia sp., in particular Curvularia verrucu- losa or Curvularia inaequaiis, such as C. inaequa/is CBS 102.42 as described in WO 95/27046; or C. verrucuiosa CBS 147.63 or C. verrucuiosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartiebii as described in WO 2001/79459, Dendryphieiia saiina as described in WO 2001/79458, Phaeotrichoconis crotaiarie as described in WO 2001/79461 , or Genicuio- sporium sp. as described in WO 2001/79460.
In one embodiment, the water-soluble multilayer film of the invention comprises at least one lyase.“Lyase” may be a pectate lyase derived from Bacillus, particularly B. iicheniformis or B. agaradhaerens, or a variant derived of any of these, e.g. as described in US 6,124,127, WO 99/027083, WO 99/027084, WO 2002/006442, WO 2002/092741 , WO 2003/095638.
Commercially available pectate lyases are Xpect™, Pectawash™ and Pectaway™ (Novozymes A/S); PrimaGreen™, EcoScour (DuPont).
In one embodiment, the water-soluble multilayer film of the invention comprises at least one enzyme selected from the group of pectinases, and/or arabinases, and/or galactanases, and/or xylanases. Suitable pectinases, and/or arabinases, and/or galactanases, and/or xylanases are known to those skilled in the art.
Nuclease
Nuclease (EC 3.1.21.1 ) also known as Deoxyribonuclease I, or DNase preforms endonucleolytic cleavage to 5'-phosphodinucleotide and 5'-phosphooligonucleotide end-products.
Nuclease enzymes have been described in patents and published patent applications including, but not limited to: US3451935, GB1300596, DE10304331 , WO2015155350, WO2015155351 , WO2015166075, WO2015181287, and WO2015181286.
Examples
In the following paragraphs, examples are given in order to illustrate some aspects of the pre sent invention.
Preparation of enzyme containing application solutions:
Preparation of lipase containing application solution A1 for films based on PVOH, propane-1 ,2- diol and glycerol:
4.66g of solid polyvinyl alcohol (Powal 26-88, Kuraray) is dissolved in 34.20g deionized water at 80°C under stirring. 0.48g of propane-1 ,2-diol and 0.52g of glycerol is added under stirring and subsequently the solution is cooled to room temperature. At room temperature 32.17mg (equiv alent to 0.7wt% related to PVOH) lyophilisate of lipase (from Thermomyces lanuginosus L-0777, Sigma Aldrich) is added under stirring.
Preparation of protease and amylase containing application solution A2 for films based on PVOH, glycerol and propane-1 ,2-diol:
5.09g of solid polyvinyl alcohol (Powal 26-88, Kuraray) is dissolved in 36.71 g deionized water at 80°C under stirring. 0.51 g of propane-1 , 2-diol and 0.57g of glycerol is added under stirring and subsequently the solution is cooled to room temperature. At room temperature 307.28mg
(equivalent to 6wt% related to PVOH) lyophilisate of protease Seq ID 1 ( A Q S
) and 61 56mg (equivalent to 1 2wt% related to PVOH) amylase lyophilis- ate are added under stirring.
Preparation of lipase and amylase containing application solution A3 for films based on PVOH, glycerol and propane-1 ,2-diol:
3.43g of solid polyvinyl alcohol (Powal 26-88, Kuraray) is dissolved in 24.89g deionized water at 80°C under stirring. 0.34g of propane-1 ,2-diol and 0.38g of glycerol is added under stirring and subsequently the solution is cooled to room temperature. At room temperature 24.03mg (equiv alent to 0.7wt% related to PVOH) lipase lyophilisate (from Thermomyces lanuginosus L-0777, Sigma Aldrich) and 40.85mg (equivalent to 1.2wt% related to PVOH) amylase lyophilisate (a- Amylase from Bacillus licheniformis A4551 , Sigma Aldrich) are added under stirring.
Preparation of protease and amylase containing application solution B for films based on a vi- nylimidazole-vinylpyrrolidone copolymer (Sokalan HP56) and propane-1 , 2-diol:
3.81 g of solid Sokalan HP56 (BASF SE) is dissolved in 15.23g deionized water at 80°C under stirring. 0.41 g of propane-1 ,2-diol is added under stirring and subsequently the solution is cooled to room temperature. At room temperature 229.13mg (equivalent to 6wt% related to Sokalan HP56) purified protease lyophilisate Seq ID 2 (see above) and 45.29mg (equivalent to 1.2wt% related to Sokalan HP56) amylase lyophilisate (a-Amylase from Bacillus licheniformis A4551 , Sigma Aldrich) are added under stirring.
Preparation of protease and lipase containing application solution A4 for films based on PVOH and glycerol:
2.44g of solid polyvinyl alcohol (Powal 26-88, Kuraray) is dissolved in 17.40g deionized water at 80°C under stirring. 0.27g of glycerol is added under stirring and subsequently the solution is cooled to room temperature. At room temperature 146.00mg (equivalent to 6wt% related to
added under stirring.
Preparation of application solution C:
Table 1 : Wash active polymer composition:
2,2’Azobis(2-methylproprionamidine)dihydrochloride (CAS-No 2997-92-4)
Oxo alcohol and water were initially charged and the initial charge was heated to 75 ° C with stirring at 100 rpm. The feeds 1 , 2 and 3 were then added in 4 hours and the reaction mixture was polymerized for an additional hour. Then the mixture was allowed to cool to room temperature. The polymer composition was obtained in the form of a transparent and viscous solution. 100 g of the polymer composition was heated to 80°C. After adding 4.2 g of glycerol, the concentration of the polymer composition was diluted to 65% wt% with deionized water. The appli-
cation solution was well mixed and tempered at 80°C until the stirred-in air had completely escaped.
Preparation of enzyme containing films and enzyme activity in films:
In the following, some experimental examples are given, in order to illustrate some aspects of the present invention.
Enzyme activity assays have been conducted for enzyme containing water soluble films (Activi ty = mass detected enzyme after aging time / mass enzyme that should be in the film based on the composition of the coating solution). Time 0 of the shelf life aging tests is the instant when the enzyme containing polymer solution is prepared. Film sample preparation (coating and dry ing at room temperature and humidity) typically takes 1 -2 days with subsequent enzyme activity determination by protease or lipase assay.
Method:
Protease Assay
The protease acitivty was determined using Succinyl - Ala - Ala - Pro - Phe - p-Nitroanilide (Suc-AAPF-pNA, short : AAPF) as substrate.
pNA is cleaved from the substrate molecule at 30°C, pH 8.6 TRIS buffer. The rate of cleavage can be determined by the increase of the yellow color of free pNA in the solution by measuring OD405, the optical density at 405 nm.
Lipase Assay
Lipase activity is determined by a method employing para Nitrophenol-valerate (pNP-C5). Fol- lowing cleavage, a free pNP molecule is liberated with an absorption increase that can be moni tored at a wavelength of 405 nm. The sample to be analyzed is diluted in residual activity buffer (100 mM Tris pH 8.0, 2% w/w Arabic gum, 0.01 % Triton X100). The dilution is as such that the final dilution is in the linear range of the assay. The slope (absorbance increase at 405 nm per minute) of the time dependent absorption-curve is directly proportional to the activity of the lipase.
The enzyme activity in films has been determined by adding a solid piece of film into a microtiter plate. Activity evolution in aging tests at 37°C is measured during film dissolution over a period of time (typically 15min) until the activity value has reached a constant value. Activies might spread (100% plus, minus 10%) due to residual moisture in the films which impact the activity values of sample amounts determined gravimetrically .
Example 1 : Preparation of protease and amylase containing films based on the color transfer inhibitor polymer Sokalan HP56 (BASF SE) (application solution B):
To produce a single layer film, an automatic film applicator and a universal applicator from Zehntner were used. The application solution B was applied to a PET substrate (Hostaphan®,
Mitsubishi Polyester Film). The gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
Table 2: Change of normalized protease and amylase activity over time in single layer film based on color transfer inhibitor polymer stored at 37°C conditions:
Example 2: Preparation of protease and lipase containing single layer films based on PVOH and glycerol (application solution A4):
To produce a single layer film, an automatic film applicator and a universal applicator from Zehntner were used. The application solution A4 was applied to a PET substrate (Hostaphan®, Mitsubishi Polyester Film). The gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm.
Example 3: Preparation of 2-layer films containing a lipase top-layer on a layer comprising both protease and amylase based on PVOH, propane-1 ,2-diol and glycerol (application solution A1 & A2):
To produce the 2-layered film, an automatic film applicator and a universal applicator from Zehntner were used. The application solution A2 was applied to a PET substrate (Hostaphan®, Mitsubishi Polyester Film). The gap width of the doctor blade was chosen so that the layer after drying at room temperature has a thickness of 30 pm. After drying the application solution A2 layer, the application solution A1 was applied. The gap width of the doctor blade was adjusted so that after drying at room temperature, the total layer thickness of the film is 40 pm.
Example 4: Preparation of 3-layer films containing wash active polymer composition as adhesion layer in-between lipase top-layer and the combination of protease and amylase as bottom- layer based on PVOH, propane-1 ,2-diol and glycerol (application solution A1 & A3):
To produce the multi-layered film, an automatic film applicator and a universal applicator from Zehntner were used. The application solution A2 was applied to a first PET substrate (Hostaph an®, Mitsubishi Polyester Film). The gap width of the doctor blade was chosen so that the layer 1 after drying at room temperature has a thickness of 30 pm. After drying layer 1 , the application solution C of the wash active polymer composition heated to 80°C was applied. The gap width of the doctor blade was adjusted so that after drying at room temperature, the total layer thick ness of the first film comprising layer 1 and 2 is 110 pm. Subsequently, the application solution A1 was applied on a second PET substrate (Hostaphan®, Mitsubishi Polyester Film). The gap width of the doctor blade was adjusted so that after drying at room temperature, layer thickness of the second film consisting of layer 3 is 10 pm. After drying to a residual moisture of about 9wt% both films are laminated by manual force such that the 3-layer film of 120pm total thick ness is sandwiched between 2 PET sheets. Enzyme activity tests and wash performance tests have been determined with the individual layers to prevent interference between the multiple components in the analytics.
Table 3: Protease, amylase and lipase activity in fresh films of different film concepts:
Table 4: Change of normalized protease and amylase activity over time in layer 1 stored at 37°C conditions:
Wash performance of each layer:
To show that enzyme activity in water soluble films provides wash activity, wash performance tests have been conducted. The films were stored for 8 weeks at 37 °C in a heating cabinet. The wash performance of the films was determined directly and after 2, 6 and 8 weeks. The different enzymes had to be tested on varying stains.
Wash tests:
The washing effect of the enzyme-containing films were determined as follows:
Selected test fabric was washed at 25°C in the presence of cotton ballast fabric with addition of the film. After the wash cycle, the test fabric was rinsed, spun and dried. In order to determine the washing effect, the L*, a* and b* values of the test fabric were determined by photometry before and after the wash cycle. The values for the protease and amylase relevant stains were determined with a Datacolor (Elrepho 2000) photometer. The values for the lipase relevant stains were determind by MACH 5. The Delta E values were calculated from the L*, a* and b* values before and after wash. Delta E = ((L* before - L* after)2 + (a* before - a* after)2 + (b* before - b* after)2)0·5
Detergent formulations: all ingredients in % active
Wash conditions:
1) EMPA 1 17 polyester-cotton fabric, stained with blood, milk and indian ink
1> manufacturer/supplier: Swissatest Testmaterialien AG, Movenstrasse 12, CH-9015 St. Gallen 2> CFT CS 28 cotton fabric, stained withrice starch
2> manufacturer/supplier: Center for Testmaterials B.V., Vlaardingen, the Netherlands
3> CFT CS 62 cotton fabric, stained with lard/CFT CS 78, cotton fabric, stained with soybean oil/EMPA 1 12, cotton fabric, stained with cocoa/Wfk 20 D, polyester-cotton fabric, soiled with sebum/ CFT CS 70, cotton fabric, soiled with chocolate mousse (each stain 5 * 5 cm fixed on a PN 33 polyester sheet) The protease performance was tested on EMPA 117 (blood/milk/ink)
Table A: Wash result for wash active polymer composition layer 2 and layer 1 containing prote ase and amylase (stored at 37 °C), washed in detergent formulation 1 at 25“C on EMPA 1 17 blood/milk/ink (delta E values)
Table B: Wash result for wash active polymer composition layer 2 and layer 1 containing prote ase and amylase (stored at 37 °C), washed in detergent formulation 1 at 25 °C on CFT CS 28 (rice starch) (delta E values)
Protease and amylase embedded in the film are stable over 8 weeks stored at 37 °C
Table C: Wash result for wash active polymer composition layer 2 and layer 3 containing li pase, stored at 37°C and washed in formulation 2 at 25 °C on a multi stain set (sum of delta E values)
In summary, the examples show that in case of the combination of protease and lipase, it is not possible to embed both incompatible enzymes (example 2) in different layers of a 2-layer film, since during film manufacturing of subsequent coating and drying the bottom enzyme migrates into the top layer (example 3).
In a preferred scenario, both enzyme containing layers are laminated with each other. The properties of the wash active polymer composition layer matches exactly with requirements for an adhesive layer and makes a lamination process feasible. By this process, including the wash active polymer composition layer as an adhesive interlayer in-between both enzyme layers mi-
gration processes are prevented and enzyme activity of the individual layers is preserved (ex ample 4).
Additional wash performance tests show that the demonstrated wash active multilayer films not only exhibit enzyme activity but also provide additional wash performance if such films are used in addition to typical liquid detergent pouch formulation (example 4). The wash tests show the enzymes embedded in the film exhibit a very high storage stability.
Finally, the present invention may be illustrated by any of the following items.
1. A water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1 ) obtainable by physical blending of a at least one polymer PT) and at least one polyether component PE), or free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically un saturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic ac ids and mixtures thereof, in the presence of at least one polyether component PE), select ed from polyether alcohols with a number average molecular weight Mn of at least 200 g/mol, mono and di-(Ci to C6-alkyl)ethers of such polyether alcohols, polyether groups- containing surfactants or mixtures thereof, and/or at least one layer comprising or consist ing of a composition P2), wherein at least one of the layers comprises at least one en zyme EN).
2. A water-soluble multilayer film according to item 1 , wherein the film comprises at least one layer comprising or consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
3. A water-soluble multilayer film according to any one of items 1 to 2, wherein at least two of the layers, preferably two of the layers, comprise at least one type of enzyme EN) each.
4. A water-soluble multilayer film according to any one of items 1 to 3, wherein two of the layers comprise one enzyme EN) each, wherein the enzymes EN) comprised in the differ ent layers are different from each other, and preferably are incompatible with each other.
5. A water-soluble multilayer film according to any one of items 1 to 3, wherein at least two of the layers, preferably two of the layers, comprise one enzyme EN) each, and wherein the layers comprising one enzyme EN) each are spatially separated by at least one layer comprising or consisting of composition P1 ) or P2), and wherein the separating layer does not contain enzymes, and wherein the enzymes EN) comprised in the different layers are preferably different from each other, and further preferably are incompatible with each other.
6. A water-soluble multilayer film according to any one of items 1 to 5, wherein at least one enzyme EN) is incorporated in one of the layers comprising or consisting of a composition P2), wherein this layer comprising or consisting of a composition P2) preferably comprises polyvinyl alcohol.
7. A water-soluble multilayer film according to any one of items 1 to 6, wherein all of the enzymes EN) are incorporated in any one of the layers comprising or consisting of a composition P2).
8. A water-soluble multilayer film according to any one of items 1 to 7, wherein the enzyme EN) is selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
9. A water-soluble multilayer film according to any one of items 1 to 8, wherein at least one layer contains protease as enzyme EN1 ), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
10. A water-soluble multilayer film according to any one of items 1 to 9, wherein none of the layers contains a protease inhibitor.
11. Water soluble multilayer film according to any one of items 1 to 10, derived from a wash active layer based on a at least one polymer chosen from P2, preferred a polymer blend, more preferred chosen from polymer composition P 1 , which is used as adhesion layer in- between two enzyme containing layers, optionally in a lamination process.
12. The multilayer film according to according to any one of items 1 to 1 1 , comprising at least one further layer comprising or consisting of at least one polymer P2) selected from
natural and modified polysaccharides,
homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
homo- and copolymers comprising at least one copolymerized monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole,
2-vinylpyridine, 4-vinylpyridine, salts of the three latter monomers, vinylpyridine N- oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof,
homo- and copolymers of acrylic acid and/or methacrylic acid, especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least
one copolymerized hydrophobic monomer selected from Ci-Cs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C2-C8 olefin,
homo- and copolymers of acrylamide and/or methacrylamide,
polyamino acids,
water-soluble or water-dispersible polyamides,
polyalkylene glycols, mono- or diethers of polyalkylene glycols,
polyethylene imine alkoxylates,
multifunctional alkoxylated diamines, preferably alkoxylated diamines with 2 to 10 methylene groups,
cellulose derivatives, preferably cellulose ethers, cellulose esters, carboxyalkyl cellu- loses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
amphoteric modified starch, and
mixtures thereof.
13. The multilayer film according to any of the preceding items, wherein at least one of the layers comprises at least one additive and/or at least one additive is present between at least two layers, said additive preferably being selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, enzymes, bases, corrosion inhibitors, defoamers, wetting agents, dyes, pigments, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluorescers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxidants, corrosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and antislip agents, plasticizers, scavengers, polymers other than the polymer compositions P1 ) and the polymers P2), agents for modification of gas permeabil- ity and water vapor permeability, antistats, glidants, slip agents, bitter agent, anti-yellowing agents and UV absorbers and mixtures thereof.
14. A process for producing a multilayer film as defined in any of items 1 to 13, in which
11 ) a first free-flowing composition capable of film formation is applied to a carrier material to obtain a first layer,
12) the first layer applied to the carrier material is optionally subjected to an increase in viscosity,
13) a second free-flowing composition capable of film formation is applied to the first layer obtained in step i1 ) or in step i2) to obtain a second layer,
14) the second layer is optionally subjected to an increase in viscosity,
15) step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to re peat steps i3) and i4) once or more than once,
16) the layers applied to the carrier material are optionally subjected to a further in crease in viscosity,
17) the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing compositions each comprise a component which is ca pable of film formation and is independently selected from at least one polymer composition P1 ), at least one polymer P2) or a mixture thereof, and with the proviso that at least one of the free-flowing compositions and/or the carrier material comprises or consists of a polymer composition P 1 ) as defined in any of the preceding claims,
and wherein optionally at least two of the free-flowing compositions may be applied to the carrier material simultaneously, or at least two layers are optionally laminated.
15. The use of a multilayer film as defined in any of items 1 to 13 or obtainable by a process as defined in claim 14, as a washing composition or as a cleaning composition.
16. Washing composition, comprising a multilayer film according to any of items 1 to 13 or obtainable by a process as defined in item 14.
Enzyme sequences mentioned above in the examples section
Seq 1 (protease)
G A S
Seq 2 (protease)
Claims
1. A water-soluble multilayer film comprising at least one layer comprising or consisting of a polymer composition P1 ) obtainable by physical blending of a at least one polymer P1’) obtainable by by free-radical polymerization of a monomer composition M’) that comprises at least one monomer A ) which is selected from a,b-ethylenically unsaturated carboxylic acids, salts of a,b-ethylenically unsaturated carboxylic acids and mixtures thereof, and at least one polyether component PE), or free-radical polymerization of a monomer composition M1 ) comprising at least one monomer A) selected from a,b-ethylenically unsaturated mono- and dicarboxylic acids, salts of a,b-ethylenically unsaturated mono- and dicarboxylic acids, anhydrides of a,b-ethylenically unsaturated mono- and dicarboxylic acids and mixtures thereof, in the presence of at least one polyether component PE), selected from pol yether alcohols with a number average molecular weight Mn of at least 200 g/mol, mono and di-(Ci to C6-alkyl)ethers of such polyether alcohols, polyether groups-containing surfactants or mixtures thereof, and/or at least one layer comprising or consisting of a com position P2) selected from
natural and modified polysaccharides,
homo- and copolymers comprising repeat units which derive from vinyl alcohol, vinyl esters, alkoxylated vinyl alcohols or mixtures thereof,
homo- and copolymers comprising at least one copolymerized monomer selected from N-vinylpyrrolidone, N-vinylcaprolactam, N-vinylimidazole,
2-vinylpyridine, 4-vinylpyridine, salts of the three latter monomers, vinylpyridine N- oxide, N-carboxymethyl-4-vinylpyridium halides and mixtures thereof,
homo- and copolymers of acrylic acid and/or methacrylic acid, especially copolymers comprising at least one copolymerized acrylic monomer selected from acrylic acid, acrylic salts and mixtures thereof, and at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof,
copolymers comprising at least one copolymerized (meth)acrylic monomer selected from acrylic acid, methacrylic acid, salts thereof and mixtures thereof and at least one copolymerized hydrophobic monomer selected from CrCs-alkyl esters of (meth)acrylic acid, C2-C10 olefins, styrene and a-methylstyrene,
copolymers comprising at least one copolymerized maleic monomer selected from maleic acid, maleic anhydride, maleic salts and mixtures thereof and at least one copolymerized C2-C8 olefin,
homo- and copolymers of acrylamide and/or methacrylamide,
polyamino acids,
water-soluble or water-dispersible polyamides,
polyalkylene glycols, mono- or diethers of polyalkylene glycols,
polyethylene imine alkoxylates,
multifunctional alkoxylated diamines, preferably alkoxylated diamines with 2 to 10 methylene groups,
cellulose derivatives, preferably cellulose ethers, cellulose esters, carboxyalkyl cellu loses and salts thereof, sulfoalkyl celluloses and salts thereof, acidic sulfuric ester
salts of cellulose, alkyl celluloses, hydroxyalkyl celluloses, hydroxyalkyl alkyl celluloses and mixtures of two or more of these cellulose derivatives
amphoteric modified starch, and mixtures thereof,
wherein at least two of the layers, preferably two of the layers, comprise at least one type of enzyme EN) each.
2. A water-soluble multilayer film according to claim 1 , wherein the film comprises at least one layer consisting of at least one washing- and/or cleaning active polymer or polymer blend, wherein (i) the washing- and/or cleaning active polymer or polymer blend is selected from P1 ), and/or (ii) the washing- and/or cleaning active polymer or polymer blend is selected from P2).
3. A water-soluble multilayer film according to any one of claims 1 to 2, wherein two of the layers comprise one enzyme each, wherein the enzymes comprised in the different layers are different from each other, and preferably are incompatible with each other.
4. A water-soluble multilayer film according to any one of claims 1 to 2, wherein at least two of the layers, preferably only two of the layers, comprise one enzyme EN) each, and wherein the layers comprising one enzyme EN) each are spatially separated by at least one layer comprising or consisting of composition P1 ) or P2), and wherein the separating layer does not contain enzymes, and wherein the enzymes EN) comprised in the different layers are preferably different from each other, and further preferably are incompatible with each other.
5. A water-soluble multilayer film according to any one of claims 1 to 4, wherein at least one enzyme EN) is incorporated in one of the layers comprising or consisting of a composition P2), wherein this layer comprising or consisting of a composition P2) preferably comprises polyvinyl alcohol.
6. A water-soluble multilayer film according to any one of claims 1 to 5, wherein all of the enzymes EN) are incorporated in any one of the layers comprising or consisting of a composition P2).
7. A water-soluble multilayer film according to any one of claims 1 to 6, wherein the enzyme EN) is selected from the group consisting of proteases, amylases, lipases, cellulases, perhydrolases, mannanases, nucleases, peroxidases, oxidases, lyases, pectinases, arabinases, galactanases, xylanases, and mixtures thereof.
8. A water-soluble multilayer film according to any one of claims 1 to 7, wherein at least one layer contains protease as enzyme EN1 ), and at least one other layer contains at least one enzyme EN2) different from protease, preferably at least one enzyme EN2) that is incompatible with protease, more preferably lipase as enzyme EN2), and wherein, preferably, these two layers containing EN1 ) and EN2) are spatially separated by at least one further layer neither comprising EN1) nor EN2).
9. A water-soluble multilayer film according to any one of claims 1 to 8, wherein none of the layers contains a protease inhibitor.
10. Water soluble multilayer film according to any one of claims 1 to 9, derived from a wash active layer based on a at least one polymer chosen from P2, preferred a polymer blend, more preferred chosen from polymer composition P 1 , which is used as adhesion layer in- between two enzyme containing layers, optionally in a lamination process.
11 . The multilayer film according to any of the preceding claims, wherein at least one of the layers comprises at least one additive and/or at least one additive is present between at least two layers, said additive preferably being selected from nonionic, anionic, cationic and amphoteric surfactants, builders, complexing agents such as methylglycinediacetic acid, glutaminediacetic acid, glutamic acid diacetic acid and citric acid and the sodium and potassium salts thereof, bleaches, enzymes, bases, corrosion inhibitors, defoamers, wet ting agents, dyes, pigments, fragrances, fillers, tableting aids, disintegrants, thickeners, solubilizers, organic solvents, electrolytes, pH modifiers, perfume carriers, fluorescers, hydrotropes, antiredeposition agents, optical brighteners, graying inhibitors, antishrink agents, anticrease agents, dye transfer inhibitors, antimicrobial active ingredients, antioxi dants, corrosion inhibitors, antistats, ironing aids, hydrophobizing and impregnating agents, antiswell and antislip agents, plasticizers, scavengers, polymers other than the polymer compositions P1 ) and the polymers P2), agents for modification of gas permeabil ity and water vapor permeability, antistats, glidants, slip agents, bitter agent, anti-yellowing agents and UV absorbers and mixtures thereof.
12. A process for producing a multilayer film as defined in any of claims 1 to 1 1 , in which
11 ) a first free-flowing composition capable of film formation is applied to a carrier mate rial to obtain a first layer,
12) the first layer applied to the carrier material is optionally subjected to an increase in viscosity,
13) a second free-flowing composition capable of film formation is applied to the first layer obtained in step i1 ) or in step i2) to obtain a second layer,
14) the second layer is optionally subjected to an increase in viscosity,
15) step i3) is optionally repeated with a further composition capable of film formation to obtain a further layer and step i4) is optionally then repeated, it being possible to re peat steps i3) and i4) once or more than once,
16) the layers applied to the carrier material are optionally subjected to a further in
crease in viscosity,
i7) the multilayer film obtained is optionally detached from the carrier material, with the proviso that the free-flowing compositions each comprise a component which is ca pable of film formation and is independently selected from at least one polymer composition P1 ), at least one polymer P2) or a mixture thereof, and with the proviso that at least one of the free-flowing compositions and/or the carrier material comprises or consists of a polymer composition P1 ) as defined in any of the preceding claims,
and wherein optionally at least two of the free-flowing compositions may be applied to the carrier material simultaneously, or at least two layers are optionally laminated.
13. The use of a multilayer film as defined in any of claims 1 to 1 1 or obtainable by a process as defined in claim 12, as a washing composition or as a cleaning composition.
14. Washing composition, comprising a multilayer film according to any of claims 1 to 1 1 or obtainable by a process as defined in claim 12.
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CN114931934A (en) * | 2022-05-25 | 2022-08-23 | 安徽皖仪科技股份有限公司 | Grafting type cation exchange chromatographic column packing and preparation method thereof |
WO2023225459A2 (en) | 2022-05-14 | 2023-11-23 | Novozymes A/S | Compositions and methods for preventing, treating, supressing and/or eliminating phytopathogenic infestations and infections |
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