EP2727989A2 - Method for improving the cleaning performance of a washing and cleaning agent - Google Patents

Abstract

Washing- or cleaning agent comprises: (a) at least a hydrolytic enzyme, preferably a protease (preferred), amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, beta -glucosidase, carrageenase or a lipase; (b) at least a substance, which improves the synergistic cleaning performance in combination with the component (a). The substance (b) is (b1) amino acid or polyamino acid or its derivative, (b2) bio-surfactant, (b3) microbial metabolite and/or (b4) preparation of a microbial culture supernatant and contains at least 2.5 wt.% of one of the substances from b1 to b3.

Description

The present application is directed to methods for improving the cleaning performance of a detergent or cleaning agent containing a hydrolytic enzyme.

The use of enzymes in detergents and cleaners is well established in the art. They serve to extend the range of services of the funds concerned according to their specific activities. These include in particular hydrolytic enzymes such as proteases, amylases, lipases and cellulases. The first three hydrolyze proteins, starches and fats and thus contribute directly to soil removal. Cellulases are used in particular because of their tissue effect. Another group of detergents and cleaning agents are oxidative enzymes, in particular oxidases, which, if appropriate, in combination with other components, preferably serve to bleach soiling or to generate the bleaching agents in situ. In addition to these enzymes, which are subjected to constant optimization, further enzymes are constantly being made available for use in detergents and cleaners in order to be able to optimally address particular soiling, such as pectinases, β-glucanases, mannanases or other hemicellulases for hydrolysis, in particular more specific vegetable polymers.

The enzymes that have long been established and are contained in virtually all modern, high-performance detergents and cleaners are proteases, and in particular serine proteases, which include the subtilases. They cause the degradation of protein-containing stains on the items to be cleaned. Of these, in turn, proteases of the subtilisin type (subtilases, subtilopeptidases, EC 3.4.21.62) are particularly important, which are attributed to the serine proteases due to the catalytically active amino acids. They act as nonspecific endopeptidases, that is, they hydrolyze any acid amide linkages that are internal to peptides or proteins. Their pH optimum is usually in the clearly alkaline range. An overview of this family, for example, the article " Subtilases: Subtilisin-like Proteases "by R. Siezen, pages 75-95 in" Subtilisin enzymes ", edited by R. Bott and C. Betzel, New York, 1996 , Subtilases are naturally produced by microorganisms; Of these, in particular, the subtilisins formed and secreted by Bacillus species are to be mentioned as the most important group within the subtilases.

Examples of the subtilisin-type proteases preferably used in detergents and cleaners are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483, subtilisin DY and the subtilases, but not the subtilisins in the narrower sense attributable enzymes thermitase, proteinase K and the proteases TW3 and TW7. Further useful proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym, Natalase®, Kannase® and Ovozyme® from Novozymes, which are available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime and Properase ® from Genencor, sold under the trade name Protosol® by Advanced Biochemicals Ltd., Thane, India, under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and Protease P From Amano Pharmaceuticals Ltd., Nagoya, Japan, and that available under the name Proteinase K-16 from Kao Corp., Tokyo, Japan.

Favorably, there are synergy effects between the enzymes and the other constituents of the respective detergents or cleaners.

A disadvantage of these enzymes used in detergents and cleaning agents, in particular proteases, from the prior art is that they are especially at low temperatures, for example between 10 ° C and 40 ° C, in particular between 10 ° C and 30 ° C or even between 10 ° C and 25 ° C, have no satisfactory hydrolytic activity, in particular proteolytic activity, and therefore in particular in detergents and dishwashing detergents in this temperature range show no optimal cleaning performance.

Surprisingly, it has been found that the addition of certain substances considerably improves the cleaning performance of detergents and cleaners containing hydrolytic enzymes, in particular proteases, in particular at comparatively low temperatures, in particular between 10 ° C. and 50 ° C., between 10 ° C. and 40 ° C and preferably between 10 ° C and 30 ° C and 10 ° C and 25 ° C.

1. i. Aminosäure oder Polyaminosäure oder deren Derivat und/oder
2. ii. Biotensid und/oder
3. iii. mikrobieller Metabolit
4. iv. Präparat eines mikrobiellen Kulturüberstandes, das mindestens 2,5 Gew.-% einer der Substanzen i) bis iii) enthält.

The present invention is therefore based on the object to improve the cleaning performance (washing power) of detergents or cleaning agents, in particular with regard to soiling, which are sensitive to degradation by hydrolytic enzymes, in particular by proteases. A further object of the invention is to improve the cleaning performance of hydrolytic enzymes, in particular proteases, in detergents or cleaners or the wash liquor formed by the detergents or cleaners, in particular with regard to soiling, which are sensitive to degradation by hydrolytic enzymes , in particular by proteases, and in particular in a temperature range between 10 ° C and 50 ° C, between 10 ° C and 40 ° C and preferably between 10 ° C and 30 ° C and 10 ° C and 25 ° C. The invention thus provides a process for improving the cleaning performance of a washing or cleaning agent which comprises a hydrolytic enzyme, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase or a lipase preferably a protease, characterized in that a component is added to the washing or cleaning agent, which effects a synergistic cleaning performance in conjunction with the hydrolytic enzyme when using the agent and which is selected from

1. i. Amino acid or polyamino acid or its derivative and / or
2. ii. Biosurfactant and / or
3. iii. microbial metabolite
4. iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii).

According to the invention, it has been found that the cleaning performance of detergents or cleaners, in particular with regard to their enzymatic, in particular proteolytic cleaning performance is significantly improved if in these agents at least one hydrolytic enzyme (also referred to herein as component (a)) with one or more of the above i. to iv. cited substances or substance classes (also referred to herein as component (b)) is combined. In the context of the invention, cleaning performance is understood to mean the whitening performance of one or more soiling, in particular laundry soiling, which are sensitive to degradation by the particular hydrolytic enzyme, in particular for degradation by proteases. Examples of such stains are blood milk / ink on cotton, whole egg / pigment on cotton, chocolate milk / ink on cotton, peanut oil pigment / ink on polyester / cotton, grass on cotton or cocoa on cotton, especially such as indicated below. In the context of the invention, both the washing or cleaning agent, which comprises the hydrolytic enzyme, or the washing or cleaning liquor formed by this agent, and the hydrolytic enzyme itself have a respective cleaning performance. The cleaning performance of the hydrolytic enzyme thus contributes to the cleaning performance of the agent or the washing or cleaning liquor formed by the agent.

The cleaning performance of detergents and cleaners based on the enzymatic activity used, in particular on the proteolytic activity, is improved by the addition of component (b). With regard to the interaction of these components (a) and (b), a synergistic effect results, ie a better performance compared to the individual performances of the respective component in one-component systems (ie detergents or cleaners, each containing only the hydrolytic, in particular proteolytic enzyme, or the Component (b)) and also compared to the sum of the individual performances of components (a) and (b), ie the sum of two one-component systems, each having the component (a) and (b) alone. Thus, the selected combination of hydrolytic enzyme (a), in particular protease, with a component (b) according to the invention represents a further possibility for improving the performance of detergents in terms of their cleaning performance, in particular their enzyme-based cleaning performance, especially with regard to their cleaning performance, which is caused by a contained protease to improve.

The advantageousness of the combination of components (a) and (b) is present when the agent is used, i. in the washing or cleaning fleet. The washing or cleaning liquor is understood to be the use solution containing the washing or cleaning agent which acts on textiles or fabrics (wash liquor) or hard surfaces (cleaning liquor) and thus comes into contact with the soiling present on textiles or fabrics or hard surfaces , Usually, the washing or cleaning liquor arises when the washing or cleaning process begins and the detergent or cleaning agent, for example, in a washing machine or other suitable container dissolved in water or diluted with water.

Preferred hydrolytic enzymes in the sense of component (a) include in particular proteases, amylases, in particular α-amylases, cellulases, lipases, hemicellulases, in particular pectinases, mannanases, β-glucanases, and mixtures thereof. Proteases, amylases and / or lipases and mixtures thereof are particularly preferred, and proteases are particularly preferred. These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents or cleaning agents, which are preferably used accordingly.

Among the proteases, those of the subtilisin type are preferable. Examples thereof are the subtilisins BPN 'and Carlsberg, the protease PB92, the subtilisins 147 and 309, the alkaline protease from Bacillus lentus, subtilisin DY and the enzymes thermitase, proteinase K and the subtilases, but not the subtilisins in the narrower sense Proteases TW3 and TW7. Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase® from Novozymes A / S, Bagsværd, Denmark. The subtilisins 147 and 309 are sold under the trade names Esperase®, and Savinase® by the company Novozymes. From the protease from Bacillus lentus DSM 5483 derived under the name BLAP® protease variants derived. Further useful proteases are, for example, those under the trade names Durazym®, Relase®, Everlase®, Nafizym®, Natalase®, Kannase® and Ovozyme® from Novozymes, available under the trade names, Purafect®, Purafect® OxP, Purafect® Prime, Excellase® and Properase® from Genencor, sold under the trade name Protosol® by Advanced Biochemicals Ltd., Thane, India sold under the trade name Wuxi® by Wuxi Snyder Bioproducts Ltd., China, under the trade names Proleather® and Protease P® by Amano Pharmaceuticals Ltd., Nagoya, Japan, and the product called Proteinase K-16 of enzymes available from Kao Corp., Tokyo, Japan. Particular preference is also given to using the proteases from Bacillus gibsonii and Bacillus pumilus, which are disclosed in the international patent applications WO2008 / 086916 and W02007 / 131656 ,

Examples of amylases which can be used according to the invention are the α-amylases from Bacillus licheniformis, B. amyloliquefaciens or B. stearothermophilus and their further developments improved for use in detergents or cleaners. The B. licheniformis enzyme is available from Novozymes under the name Termamyl® and from Genencor under the name Purastar®ST. Further development products of this α-amylase are available from Novozymes under the trade name Duramyl® and Termamyl®ultra, from Genencor under the name Purastar®OxAm and from Daiwa Seiko Inc., Tokyo, Japan, as Keistase®. B. amyloliquefaciens α-amylase is sold by Novozymes under the name BAN®, and variants derived from the B. stearothermophilus α-amylase under the names BSG® and Novamyl®, also from Novozymes. Furthermore, for this purpose, the α-amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin glucanotransferase (CGTase) from B. agaradherens (DSM 9948). In addition, the amylolytic enzymes belonging to the sequence space of α-amylases which can be used in the international patent application WO 03/002711 A2 is defined, and the ones in the application WO 03/054177 A2 to be discribed. Likewise, fusion products of said molecules can be used. In addition, the further developments of the α-amylase from Aspergillus niger and A. oryzae available under the trade names Fungamyl® from Novozymes are suitable. Further usable commercial products are, for example, the Amylase-LT® and Stainzyme® or Stainzyme ultra® or Stainzyme plus®, the latter also from Novozymes. Also variants of these enzymes obtainable by point mutations can be used according to the invention.

Examples of lipases or cutinases which can be used according to the invention, which are contained in particular because of their triglyceride-cleaving activities, but also in order to generate in situ peracids from suitable precursors, are the lipases which are originally obtainable from Humicola lanuginosa (Thermomyces lanuginosus) or further developed, in particular those with the amino acid exchange D96L. They are, for example, from the company Novozymes under the Trade names Lipolase®, Lipolase® Ultra, LipoPrime®, Lipozyme® and Lipex®. Furthermore, for example, the cutinases can be used, which were originally isolated from Fusarium solani pisi and Humicola insolens. Lipases which are likewise useful are sold by Amano under the names Lipase CE®, Lipase P®, Lipase B® or Lipase CES®, Lipase AKG®, Bacillis sp. Lipase®, Lipase AP®, Lipase M-AP® and Lipase AML®. By Genencor, for example, the lipases or cutinases can be used, the initial enzymes were originally isolated from Pseudomonas mendocina and Fusarium solanii. Further important commercial products are the preparations M1 Lipase® and Lipomax®, which were originally sold by Gist-Brocades, and the enzymes marketed by Meito Sangyo KK, Japan, under the name Lipase MY-30®, Lipase OF® and Lipase PL® to mention also the product Lumafast® from the company Genencor.

Depending on the purpose, cellulases may be present as pure enzymes, as enzyme preparations or in the form of mixtures in which the individual components advantageously complement each other in terms of their various performance aspects. These performance aspects include, in particular, the contributions of the cellulase to the primary washing performance of the composition (cleaning performance), to the secondary washing performance of the composition (anti-redeposition effect or graying inhibition), to softening (fabric effect) or to the exercise of a "stone washed" effect. A useful fungal endoglucanase (EG) -rich cellulase preparation or its further developments is offered by Novozymes under the trade name Celluzyme®. The products Endolase® and Carezyme®, which are also available from Novozymes, are based on the 50 kD EG or the 43 kD EG from H. insolens DSM 1800. Further commercial products of this company are Cellusoft®, Renozyme® and Celluclean®. Also usable are, for example, the 20 kD-EG from Melanocarpus available from AB Enzymes, Finland, under the trade names Ecostone® and Biotouch®. Further commercial products of AB Enzymes are Econase® and Ecopulp®. Other suitable cellulases are from Bacillus sp. CBS 670.93 and CBS 669.93, those derived from Bacillus sp. CBS 670.93 from the company Genencor under the trade name Puradax® is available. Other commercial products of Genencor are "Genencor detergent cellulase L" and IndiAge®Neutra.

Furthermore, in particular for the removal of certain problem soiling, further enzymes can be used, which are summarized by the term hemicellulases. These include, for example, mannanases, xanthan lyases, pectin lyases (= pectinases), pectin esterases, pectate lyases, xyloglucanases (= xylanases), pullulanases and β-glucanases. Suitable enzymes for this purpose are, for example, available under the names Gamanase® and Pektinex AR® from Novozymes, under the name Rohapec® B1L from AB Enzymes and under the name Pyrolase® from Diversa Corp., San Diego, CA, USA , The from Bacillus subtilis-derived β-glucanase is available under the name Cereflo® from Novozymes. Hemicellulases which are particularly preferred according to the invention are mannanases which are sold, for example, under the trade names Mannaway® by the company Novozymes or Purabrite® by the company Genencor.

Furthermore, within the scope of the invention, the enzymes may be formulated together with accompanying substances, for example from the fermentation or with stabilizers.

Of all these enzymes, particular preference is given to those which have been stabilized per se with respect to oxidation in a comparatively stable manner or, for example, via point mutagenesis. These include, in particular, the already mentioned commercial products Everlase and Purafect® OxP as examples of such proteases and Duramyl as an example of such an α-amylase.

Agents used in a method according to the invention preferably contain enzymes in total amounts of 1 × 10 ^-8 to 5 percent by weight based on active protein. Preferably, the enzymes are from 0.001 to 5% by weight, more preferably from 0.01 to 5% by weight, even more preferably from 0.05 to 4% by weight and most preferably from 0.075 to 3.5% by weight. % contained in these agents, wherein each enzyme contained can be present in the stated amounts.

The protein concentration can be determined by known methods, for example the BCA method (bicinchoninic acid, 2,2'-biquinolyl-4,4'-dicarboxylic acid) or the biuret method ( Gornall AG, CS Bardawill and MM David, J. Biol. Chem., 177 (1948), pp. 751-766 ).

The hydrolytic enzyme, at least one of which is present in a detergent or cleaning agent used in the method according to the invention (namely as component (a)), supports the cleaning performance of the composition with respect to certain soils or stains. Particularly preferably, an agent used in a method according to the invention contains a plurality of enzymes, wherein the enzymes may belong to the same or different enzyme classes. Most preferably, the enzymes exhibit synergistic effects on their action against certain soils or stains, i. the enzymes contained in the middle composition mutually support each other in their cleaning performance.

1. i. Aminosäure oder Polyaminosäure oder deren Derivat und/oder
2. ii. Biotensid und/oder
3. iii. mikrobieller Metabolit und/oder
4. iv. Präparat eines mikrobiellen Kulturüberstandes, das mindestens 2,5 Gew.-% einer der Substanzen i) bis iii) enthält.

Synergistic effects can not only be present between different enzymes, but in particular also occur between one or more enzymes and other ingredients of the agent used in methods according to the invention. According to the invention, a hydrolytic enzyme (a) is combined therewith with a component (b), ie at least one A substance which, when used in conjunction with the hydrolytic enzyme (a), produces a synergistic cleaning performance and which is selected from

1. i. Amino acid or polyamino acid or its derivative and / or
2. ii. Biosurfactant and / or
3. iii. microbial metabolite and / or
4. iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii).

For the under i. The substances mentioned are preferably amino acids or polymers thereof or their salts or derivatives thereof, where both stereoisomers of the amino acids can be used, ie both D and L amino acids, also in combination, or corresponding polymers or derivatives. A polyamino acid in this regard comprises at least two amino acid residues. Particularly preferred are glutamate, polyglutamate, lysine, glutamine, histidine, phenylalanine, tyrosine, alanine, leucine, isoleucine, methionine, proline, valine, gluramine, cysteine, trypptophan, threonine, serine, glycine, aspartate and asparagine. Preference is given to using charged polyamino acids and, among these, more preferably negatively charged polyamino acids. Particularly preferred are poly-glutamic acid, including γ-D-polyglutamic acid, L-polyglutamic acid and DL-polyglutamic acid, poly-aspartic acid, including β-D-polyaspartic acid and L-polyaspartic acid, poly-glutamine, including γ-D-polyglutamine, L Polyglutamine and DL-polyglutamine, as well as poly-asparagine, including β-D-polyasparagine and L-polyasparagine. An example of a particularly preferred polyaspartic acid is the compound available under the trade name Baypure DS 100 solid G (Lanxess company).

• R ist-CH=CH-R2, -C=C-R2, -C(R2)=CH₂, -C(R2)=C(R3), -CH=NR2, -C(R2)=N-R3, ein 4-7 C-Ring System mit oder ohne Substitution, 4-7 Stickstoffheterozyklus mit oder ohne Substitution, oder eine 2 bis 8 Kohlenstoff Kette mit 1 bis 5 Doppel- oder Dreifachbindungen mit Substitutionen selektiert aus R1, R2, oder R3;
• -R1 ist H, -R, -NO₂, -CN, -halo, -N₃, -C1-8 alkyl, -(CH₂)nCO₂R2, -C2-8 alkenyl-CO₂R2,-O(CH₂)nCO₂R2, -C(O)NR2R3, -P(O)(OR2)₂, alkyl substitutiertes tetrazol-5-yl, -(CH₂)nO(CH₂)n aryl, -NR2R3, -(CH₂)nOR2, -(CH₂)nSR2, -N(R2)C(O)R3, -S(O₂)NR2R3, -N(R2)S(O₂)R3, -(CHR2)n NR2R3, -C(O)R3, (CH₂)nN(R3)C(O)R3, -N(R2)CR2R3 substitutiertes oder nicht substitutiertes (CH₂)n-cycloalkyl, substitutiertes oder nicht substitutiertes (CH₂)n-phenyl, oder zyklus;
• -R2 ist H, -halo, -alkyl, -haloalkyl, -(CH₂)n-phenyl, -(CH₂)1-3-biphenyl, -(CH₂)1-4-Ph-N(SO₂-C1-2-alkyl)₂, -CO(CHR1)n-OR1, -(CHR1)n-Heterozyklus, -(CHR1)n-NH-CO-R1,-(CHR1)n-NH-SO₂R1, -(CHR1)n-Ph-N(SO₂-C1-2-alkyl)₂, -(CHR1)n-C(O)(CHR1)-NHR1,-(CHR1)n-C(S)(CHR1)-NHR1, -(CH₂)nO(CH₂)nCH₃, -CF₃, -C2-5 acyl, -(CHR1)nOH,-(CHR1)nCO₂R1, -(CHR1)n-O-alkyl, -(CHR1)n-O-(CH₂)n-O-alkyl, -(CHR1)n-S-alkyl,-(CHR1)n-S(O)-alkyl, -(CHR1)n-S(O₂)-alkyl, -(CHR1)n-S(O₂)-NHR3, -(CHR3)n-N₃,-(CHR3)nNHR4, 2 bis 8 Kohlenstoffatom Alken-Kette mit 1 bis 5 Doppelbindungen, 2 bis 8 Kohlenstoff Alkyne-Kette mit 1 bis 5 Dreifachbindungen, substitutierter oder nicht substitutierter -(CHR3)n Heterocyclus, oder substitutiertes oder nicht substitutiertes gesättigtes oder nicht gesättigtes -(CHR3)n Cycloalkyl;
• -Wobei n größer als 1 ist und R1 und R3 gleich oder unterschiedlich sein kann;
• -R3 ist H, -OH, -CN, substitutiertes Alkyl, -C2-8 alkenyl, substitutiertes oder nicht substitutiertes Zykloalkyl, -N(R1)R2, oder 5-6 Kohlenstoff gesättigter oder nicht gesättigter Heterozyklus. -NR2R3 kann bestehen aus einem gesättigten oder nicht gesättigten Heterozyklus oder einem Heterobizyklus von 4 to 7 Atomen;
• -n ist 0-4 ;
• -R4 und R5 besteht jeweils aus: H, -(CH₂)nOH, -C(O)OR6, -C(O)SR6, -(CH₂)nC(O)NR7R8, -O-C(O)-O-R7, einer Aminosäure oder einem Peptid;
• -R6 ist H,
• -R7 ist, -C(R7)(R8)-(CH₂)n-O-C(O)-R9, -(CH₂)n-C(R7)(R8)-O-C(O)R9, -(CH₂)n-C(R7)(R8)-O-C(O)-O-R9, or -C(R7)(R8)-(CH₂)n-O-C(O)-O-R9; und
• -R7, R8 und R9 bestehen jeweils aus H, Alkyl, substitutiertes Alkyl, Aryl, substitutiertes Aryl, Alkenyl, substitutiertes Alkenyl, Alkynyl, substitutiertes Alkynyl, Heterozyklus, substitutiertes Heterozyklus, Alkylaryl, substitutiertes Alkylaryl, Zykloalkyl, substituiertes Zykloalkyl, oder CH₂CO₂alkyl.

For the purposes of the present application, derivatives are understood as meaning substances whose pure amino acid or amino acid chain has been modified. Such derivatizations can be carried out, for example, already biologically in connection with the biosynthesis by the host cell or else by molecular biological methods. However, they can also be carried out chemically, for example by the chemical transformation of a side chain of an amino acid or by covalent bonding of another compound to the amino acid or the amino acid chain. Such a compound may be, for example, low molecular weight compounds such as lipids or mono-, oligo- or polysaccharides or amines or amine compounds. Furthermore, the amino acids or amino acid chains may have further chemical modifications, in particular they may be glycosylated, hydrolyzed, oxidized, N-methylated, N-formylated, N-acetylated or methyl, formyl, ethyl, acetyl, t-butyl, anisyl, benzyl, Trifluoroacetyl, N-hydroxysuccinimides, t-butyloxycarbonyl, benzoyl, 4-methylbenzyl, thioanizyl, thiocresyl, benzyloxymethyl, 4-nitrophenyl, benzyloxycarbonyl, 2-nitrobenzoyl, 2-nitrophenylsulphenyl, 4-Toluenesulphonyl, pentafluorophenyl, diphenylmethyl, 2-chlorobenzyloxycarbonyl, 2,4,5-trichlorophenyl, 2-bromobenzyloxycarbonyl, 9-fluorenylmethyloxycarbonyl, tripheylmethyl, 2,2,5,7,8-pentamethylchroman-6-sulphonyl. Similarly, derivatization is understood to mean the covalent or noncovalent binding to a macromolecular carrier, as well as a noncovalent inclusion in suitable macromolecular cage structures. Also, couplings with other macromolecular compounds, such as polyethylene glycol, may be made. Amino acid chains may have further chemical modifications, wherein the amino acid groups: -COOH, -OH, = NH, -NH ₂ -SH preferably carry the following modifications: -COOR, -OR, -NHR, -NR 2, -NHR, -NR, -SR ; in which:

• R is -CH = CH-R2, -C = C-R2, -C (R ₂ ) = CH ₂ , -C (R ₂ ) = C (R 3), -CH = NR ₂ , -C (R ₂ ) = N-R 3 , a 4-7 C-ring system with or without substitution, 4-7 nitrogen heterocycle with or without substitution, or a 2 to 8 carbon chain with 1 to 5 double or triple bonds with substitutions selected from R1, R2, or R3;
• -R 1 is H, -R, -NO ₂ , -CN, -halo, -N ₃ , -C 1-8 alkyl, - (CH ₂ ) n CO ₂ R ₂ , -C ₂ -8 alkenyl-CO ₂ R ₂ , -O ( CH ₂ ) nCO ₂ R ₂ , -C (O) NR ₂ R 3, -P (O) (OR ₂ ) ₂ , alkyl substituted tetrazol-5-yl, - (CH ₂ ) n O (CH ₂ ) n aryl, -NR ₂ R 3, - ( _CH2) NOR 2, - (CH ₂₎ NSR2, -N (R2) C (O) R3, -S (O ₂₎ NR2R3, -N (R2) S (O ₂₎ R 3, - (CHR 2) n NR2R3, -C (O) R3, _(CH2) nN (R3) C (O) R3, -N (R2) CR2R3 substitutiertes substitutiertes or not _(CH2) n-cycloalkyl, substitutiertes substitutiertes or not _(CH2) n-phenyl , or cycle;
• -R2 is H, halo, alkyl, haloalkyl, - (CH ₂₎ n-phenyl, - _(CH2) 1-3-biphenyl, - (CH ₂₎ 1-4-Ph-N (SO ₂ - C1-2-alkyl) ₂ , -CO (CHR1) n-OR1, - (CHR1) n-heterocycle, - (CHR1) n -NH-CO-R1, - (CHR1) n -NH-SO ₂ R1, - (CHR1) n-Ph-N _(SO2 -C1-2 alkyl) _2, - (CHR1) n C (O) (CHR1) -NHR1, - (CHR1) n C (S) (CHR1) -NHR1, - ( CH ₂ ) nO (CH ₂ ) n CH ₃ , -CF ₃ , -C 2 5 acyl, - (CHR 1) n OH, - (CHR 1) n CO ₂ R ₁ , - (CHR 1) nO-alkyl, - (CHR 1) nO- ( CH ₂ ) nO-alkyl, - (CHR 1) nS-alkyl, - (CHR 1) nS (O) -alkyl, - (CHR 1) nS (O ₂ ) -alkyl, - (CHR 1) nS (O ₂ ) -NHR 3, - (CHR ₃ ) n N ₃ , - (CHR 3) n NHR 4, 2 to 8 carbon atom alkene chain having 1 to 5 double bonds, 2 to 8 carbon alkyne chain having 1 to 5 triple bonds, substituted or unsubstituted - (CHR 3) n heterocycle, or substituted or unsubstituted saturated or unsaturated - (CHR 3) n cycloalkyl;
• Where n is greater than 1 and R1 and R3 may be the same or different;
• -R3 is H, -OH, -CN, substituted alkyl, -C2-8 alkenyl, substituted or unsubstituted cycloalkyl, -N (R1) R2, or 5-6 carbon saturated or unsaturated heterocycle. -NR 2 R 3 may consist of a saturated or unsaturated heterocycle or a heterocycle of 4 to 7 atoms;
• -n is 0-4;
• Each of R 4 and R 5 is H, - (CH ₂ ) n OH, -C (O) OR 6, -C (O) SR 6, - (CH ₂ ) n C (O) NR 7 R 8, -OC (O) -O- R7, an amino acid or a peptide;
• -R6 is H,
• R 7 is -C (R 7) (R 8) - (CH ₂ ) n OC (O) -R 9, - (CH ₂ ) n C (R 7) (R 8) -OC (O) R 9, - (CH ₂ ) n C ( R7) (R8) -O-C (O) -O-R9, or -C (R7) (R8) - _(CH2) nOC (O) -O-R9; and
• -R7, R8 and R9 are each H, alkyl, substituted alkyl, aryl, substituted aryl, alkenyl, substituted alkenyl, alkynyl, substituted alkynyl, heterocycle, substituted heterocycle, alkylaryl, substituted alkylaryl, cycloalkyl, substituted cycloalkyl, or CH ₂ CO ₂ alkyl.

In the under ii. specified substances are biosurfactants. These are understood in the context of the invention substances that are formed by microorganisms and often also deposited. Like traditional surfactants, biosurfactants are surface-active substances that reduce the surface tension of liquids and thereby promote the mixing of aqueous (hydrophilic) and water-repellent (hydrophobic) phases. Preferred biosurfactants according to the invention belong, in particular, to the substance group of the lipids or lipid derivatives, in particular lipopeptides. They are therefore bioactive, peptidic substances that are formed by microorganisms. As a rule, they are synthesized nonribosomally by the respective microorganisms, for example Gram-positive bacteria, in particular the genera Bacillus and Streptomyces, Gram-negative bacteria, in particular the genera Pseudomonas and Myxobacteria, and filamentous fungi. The peptide chains preferably consist of two to forty amino acids and may be linear, cyclic or branched. In contrast to ribosomally synthesized peptide chains, they have as monomeric building blocks not only proteinogenic L-amino acids, but also D-amino acids as well as alpha-hydroxy and / or carboxylic acids of all kinds. The amino acids are L-α- or D-α Amino acids, but also β-, γ- or δ-amino acids can be present, both in the D and in the L configuration. The peptide chains may also have further chemical modifications, in particular they may be glycosylated, hydrolyzed, N-methylated or N-formylated. Frequently occurring structural elements are also thiazoline and / or oxazoline rings in different oxidation states. Particularly preferred biosurfactants according to the invention are anionic lipopeptides and more preferably surfactin-like or lichenigen-like substances or surfactin or lichenin itself. Surfactin-like or lichenigen-like substances are understood as meaning those which have either a similar chemical structure as surfactin or lichenyin and / or have a comparable with surfactin or Lichenysin effect. Surfactin can be described in particular by the following formula: fatty acid-cyclo- [Glu-Leu-Leu-Val-Asp-Leu-Leu]. The structure of surfactin is also in FIG. 1 specified. Lichenysine can be described in particular by the following formula: Fatty acid-cyclo [Gln-Leu-Leu-Val-Asp-Leu-Ile]. Since Lichenycin is often also referred to as Lichenisin, it is expressly pointed out at this point that according to the invention with the name Lichenysin both terms are included.

Other biosurfactants as well as these producing microorganisms are given in Table 1 below. Table 1: Biosurfactant type microorganism Trehalose lipids Arthrobacter paraffineus Corynebacterium sp. Mycobacterium sp. Rhodococcus erythropolis, Norcardia sp. rhamnolipids Pseudomonas aeruginosa Pseudomonas sp., Serratia rubidea sophorolipids Candida apicola, Candida bombicola Candida lipolytica Candida bogoriensis glycolipids Alcanivorax borkumensis Arthrobacter sp., Corynebacterium sp. R. erythropolis, Serratia marcescens Tsukamurella sp. Cellobiose lipids Ustilago maydis Polyol lipids Rhodotorula glutinus Rhodotorula graminus Diglycosyl diglycerides Lactobacillus fermentii lipopolysaccharide Acinetocbacter calcoacetius (RAG1) Pseudomonas sp., Candida lipolytica Arthrofactin Arthrobacter sp. Lichenysin A. Lichenysin B. Bacillus licheniformis surfactin Bacillus subtilis, Bacillus pumilus Visconsin Pseudomonas fluorescens Ornithine, lysine peptides Thiobacillus thiooxidans Streptomyces sioyaensis Gluconobacter cerinus phospholipids Acinetobacter sp. Sulfonylipide T.thioosidans Corynebacterium alkanolyticum fatty acids Capnocytophaga sp. ("Corynomic colic adics, spiculisporic acids", etc.) Penicillium spiculisporum Corynebacterium lepus Arthrobacter paraffineus Talaramy trachysperm Norcadia erythropolis Alasan Acinetrobacter radioesistens Streptofactin Streptomyces tendae "Particulate surfactant" (PM) Pseudomonas marginalis Biosur PM Pseudomonas maltophila

In the under iii. specified substances are microbial metabolites. These are understood to mean substances which arise as intermediates or as degradation products of metabolic processes of the microorganism or as degradation products of nutrient medium through the microorganism. Microbial metabolites preferred according to the invention are present in the culture medium of a culture of the microorganism forming them. Therefore, they are particularly preferably secreted by the microorganism which forms them. Examples of microbial metabolites which are particularly preferred according to the invention are diols, in particular 2,3-butanediol, acids, in particular acetate, lactate, pyruvate, 2-methylpropionate, 3-methylbutyrate, α-ketogluterate, propionate, butyrate, butyate, sugar, in particular levan, and as another particularly preferred microbial metabolite acetoin.

Furthermore, microbial metabolites may also be propanediol, glycol, glycerol, citrate, formate, ethanol, methanol or butanol.

In a separate embodiment of the invention, component (b) is a preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii). Preferably, the culture medium of a microbial culture contains one of the substances i described above. and / or ii. and / or iii. The culture supernatant obtained after the greatest possible separation of the cells or cell fragments containing at least one of these substances can therefore be used to enrich a washing or cleaning agent with the component (b). For this purpose, however, it is necessary that the detergent or cleaning agent, a preparation of such a microbial culture supernatant is added, the at least 2.5 wt .-% of one of the substances i. to iii. contains. Alternatively, the preparation contains at least 3, 3.5, 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9, 9.5, 10, 12 , 14, 16, 18, 20, 22, 24, 26, 28, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 85 and 90 wt .-% of one of the substances i. to iii. The required amount is necessary for the provision of a sufficient minimum amount of the respective substance, without affecting the washing or cleaning agent in its washing performance due to the presence of too many other components of the microbial culture supernatant, in particular adversely affect. In the worst case, the washing performance of the washing or cleaning agent would be reduced by the addition of too large a volume of the microbial culture supernatant, which is due to the above minimum amounts of the substances i. to iii. is avoided. Accordingly, component (b) is contained in the supernatant of a microbial culture. It may either have been actively produced or secreted by the microorganisms in the supernatant or have entered the supernatant due to cell lytic events in the culture. By customary routine measures, for example by fractionation, it is then possible to produce preparations of these culture supernatants which contain component (b) in sufficient quantity to allow use according to the invention. A suitable preparation can therefore also be, for example, one or more fractions of a culture supernatant. If the culture supernatant already contains component (b) in sufficient quantity, the culture supernatant can also be added directly to the washing or cleaning agent. In this case, the preparation is the culture supernatant itself.

According to the invention, it is further possible to use all possible combinations of the substances i described above. to iv. to use in the process according to the invention. For example, the natto or its non-bean content obtained with the aid of cultures of Bacillus subtilis natto can also be used according to the invention as component (b).

Preferably component (b) is added to the detergent or cleaning agent as a separate single substance, i. not as a component of another ingredient of the washing or cleaning agent. Preferably, component (b) is therefore free in the detergent, i. it is distributed in this and distributed as homogeneously as possible. In the case of liquid or gel detergents or cleaners, component (b) is preferably dissolved or dispersed in them. The washing or cleaning agent particularly preferably does not contain component (b) as part of the dosage form of the hydrolytic enzyme (a), in particular not as a constituent of an enzyme granulate.

According to the invention, liquid or gel-shaped, i. non-solid detergents or cleaners.

• Blut-Milch/Tusche auf Baumwolle: Produkt Nr. C5 von CFT B.V. Vlaardingen, Holland
• Voll-Ei/Pigment auf Baumwolle: Produkt Nr. 10N erhältlich von der Firma wfk Testgewebe GmbH; Brüggen-Bracht, Deutschland, in kleine Stücke geschnitten
• Schokolade-Milch/Tusche auf Baumwolle: Produkt Nr. C3 von CFT B.V. Vlaardingen, Holland
• Erdnuss Öl-Pigment/Tusche auf Polyester/Baumwolle: Produkt Nr. PC10 von CFT B.V. Vlaardingen, Holland
• Gras auf Baumwolle: Produkt Nr. 164 von erhältlich von der Firma Eidgenössische Material- und Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Schweiz
• Kakao auf Baumwolle: Produkt Nr. 112 von erhältlich von der Firma Eidgenössische Materialund Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Schweiz,

bestimmt wird durch Messung des Weißheitsgrades der gewaschenen Textilien, der Waschvorgang für mindestens 30 Minuten, optional 60 Minuten, bei einer Temperatur von 40°C erfolgt und das Wasser eine Wasserhärte zwischen 15,5 und 16,5° (deutsche Härte) aufweist.A synergistic cleaning performance of component (b) which, in conjunction with the hydrolytic enzyme (a), when used with the agent, provides a synergistic cleaning performance is determined in a washing system containing a detergent in a dosage between 4.5 and 7.0 grams per liter of wash liquor and the hydrolytic enzyme (a) and the component (b) each individually or in combination, wherein the enzyme respectively is used in the same activity, the component (b) is used in a concentration of 0.00025 to 0.6 wt .-%, in particular from 0.0003 to 0.5 wt .-% (use concentration in the wash liquor), and the washing performance against one or more of the stains blood milk / ink on cotton, full egg / pigment on cotton, chocolate milk / ink on cotton, peanut oil pigment / ink on polyester / cotton, grass on cotton and cocoa on cotton, in particular towards one or more of the stains

• Blood milk / ink on cotton: Product No. C5 from CFT BV Vlaardingen, Holland
• Full egg / pigment on cotton: Product No. 10N available from the company wfk Testgewebe GmbH; Brüggen-Bracht, Germany, cut into small pieces
• Chocolate milk / ink on cotton: Product No. C3 from CFT BV Vlaardingen, Holland
• Peanut oil pigment / ink on polyester / cotton: Product No. PC10 from CFT BV Vlaardingen, Holland
• Grass on cotton: Product No. 164 from available from the company Eidgenössische Material- und Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Switzerland
• Cocoa on cotton: Product No. 112 of available from the company Eidgenössische Materialund Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Switzerland,

is determined by measuring the whiteness of the washed textiles, the washing process for at least 30 minutes, optionally 60 minutes, at a temperature of 40 ° C and the water has a water hardness between 15.5 and 16.5 ° (German hardness).

A preferred liquid detergent for such a washing system is composed as follows (all figures in weight percent): 0.3- 0.5% xanthan gum, 0.2-0.4% anti-foaming agent, 6-7% glycerol, 0.3-0.5% ethanol, 4-7% FAEOS (fatty alcohol ether sulfate), 24-28% nonionic surfactants, 1% boric acid, 1-2% sodium citrate (dihydrate), 2-4% soda, 14-16% coconut Fatty acids, 0.5% HEDP (1-hydroxyethane- (1,1-di-phosphonic acid)), 0-0.4% PVP (polyvinylpyrrolidone), 0-0.05% optical brightener, 0-0.001% dye, Rest demineralized water. Preferably, the dosage of the liquid detergent is between 4.5 and 5.5 grams per liter of wash liquor, for example, 4.9 grams per liter of wash liquor. Preference is given to washing in a pH range between pH 8 and pH 10.5, preferably between pH 8 and pH 9.

A preferred powdered detergent for such a washing system is composed as follows (all figures in weight percent): 10% linear alkylbenzenesulfonate (sodium salt), 1.5% C12-C18 fatty alcohol sulfate (sodium salt), 2.0% C12-C18 fatty alcohol with 7 EO, 20% sodium carbonate, 6.5% sodium bicarbonate, 4.0% amorphous sodium disilicate, 17 % Sodium carbonate peroxohydrate, 4.0% TAED, 3.0% polyacrylate, 1.0% carboxymethylcellulose, 1.0% phosphonate, 25% sodium sulfate, balance: optional foam inhibitors, optical brightener, fragrances and, if necessary, water ad 100%. Preferably, the dosage of the liquid detergent is between 6.0 and 7.0 grams per liter of wash liquor, for example, 6.7 grams per liter of wash liquor. Preference is given to washing in a pH range between pH 9 and pH 11.

Preferably, a liquid detergent is used.

The degree of whiteness, i. the brightening of the stains, is preferably determined by optical measuring methods, preferably photometrically. A suitable device for this purpose is for example the spectrometer Minolta CM508d. Usually, the devices used for the measurement are previously calibrated with a white standard, preferably a supplied white standard.

The activity-like use ensures that, even if the ratio of active substance to total protein (the values of the specific activity) diverge, the respective enzymatic properties, for example the washing performance of certain soils, are compared. In general, a low specific activity can be compensated by adding a larger amount of protein. Methods for the determination of the enzyme activities are familiar to the expert in the field of enzyme technology and are routinely used by him. For example, methods for the determination of protease activity are disclosed in U.S. Patent Nos. 4,936,866 and 4,347,866 Surfactants, Vol. 7 (1970), pp. 125-132 , The protease activity is preferably indicated in PE (protease units). For example, suitable protease activities are 5 or 10 PE (protease units) per ml wash liquor. However, the enzymatic activity used is not equal to zero.

The synergistic cleaning performance is preferably based on a novel mechanism of action, ie there is no increase in enzyme activity per se in the classical sense, as would be measured in one of the following methods, based on proteases. Accordingly, a synergism according to the invention is also present in particular when an improved cleaning performance in the presence of components (a) and (b) is found compared to the sum of the cleaning powers of component (a) alone and component (b) alone, and the component ( b) in at least one of the subsequent test methods, preferably in both subsequent test methods, no effect with respect to increasing the hydrolytic activity of component (a), in particular with regard to increasing the hydrolytic activity of a protease, beyond the standard deviation due to measurement:

Method 1

The protease activity is determined quantitatively by the release of the chromophore para-nitroaniline (pNA) from the substrate. The substrate is: suc-L-Ala-L-Ala-L-Pro-L-Phe-p-Nitroanilide (substrate solution: 110 mM in DMSO). The protease cleaves the substrate and releases pNA. The release of pNA causes an increase in absorbance at 410 nm, the time course of which is a measure of enzymatic activity (see Del Mar et al., 1979).

The measurement is carried out at a temperature of 25 ° C, at pH 8.6 and a wavelength of 410 nm. The measurement time is 5 min and the measurement interval 20s to 60s.

The use buffer (Tris-HCl pH 8.6) is used as a blank sample, 10 μL of the substrate solution are added to each cuvette, 1000 μL of buffer are added to each cuvette, 1-300 μl of buffer (s) are added Add component (b) (0.1, 0.2, 0.5 or 1% by weight in working buffer) to the cuvette and place 1-300 μl of the protease or blank sample in the cuvette The measurement is started by mixing the sample After mixing, the cuvettes are immediately transferred to the photometer and the measurement is started.An activation or stabilization of the protease can be quantified by means of the measurement data.

Method 2

Protease activity is determined via the hydrolysis of casein and subsequent reaction of TCA-soluble peptides with Folin &Ciocalteu's phenol reagent. The absorbance of the resulting complex is measured at 660 nm and compared to a tyrosine standard. Reaction mixtures contain 3 ml of 0.8% (w / v) casein and 0.5 ml of a suitable enzyme dilution with or without the component (b) to be tested (concentration 0.1, 0.2, 0.5 or 1 wt. %), both in universal buffer 1 from Britton and Robinson, pH 9.5 (cf. J. Chem. Soc. 1931, p. 1451 ). The mixtures are incubated for 30 minutes at 25 ° C, then the reaction is stopped by adding Stop Reagent (TCA). In control reactions, the stop reagent is added before enzyme addition with or without the substance to be tested. After 20 minutes at 25 ° C, the reaction mixtures are filtered through Whatman # 42 filter paper or centrifuged.

To the filtrate is added water, sodium carbonate and Folin &Ciocalteu's phenol reagent. After 30 minutes of incubation, the absorbance at 660 nm is determined. Similarly, an aliquoted portion of 200 μl of a tyrosine standard is determined. The activity is expressed in protease units, with 1 PE defined as the amount of proteolytic enzyme resulting in the release of 1 mmol tyrosine released per minute under defined conditions (cf. Anson, ML, (1938) J. Gen. Physiol. 22, 79-89 such as Folin, O., and Ciocalteu, V., (1929) J. Biol. Chem. 73, 627 ).

In a further embodiment of the invention, the method is characterized in that component (b) is contained in a microbial culture supernatant, in particular in a bacterial or fungal culture supernatant, in particular in a culture supernatant of Bacillus sp. and in particular in a culture supernatant of Bacillus subtilis, Bacillus licheniformis, Bacillus pumilus, Bacillus aeolius or Bacillus subtilis natto. It has been found that culture supernatants of these microorganisms comprise at least one, preferably a plurality of substances of component (b) and thus can advantageously be used according to the invention. Other microorganisms whose culture supernatants contain a component (b) according to the invention in this regard are selected from the group of the genera of Escherichia, Klebsiella, Bacillus, Staphylococcus, Corynebacterium, Arthrobacter, Streptomyces, Stenotrophomonas and Pseudomonas and in particular selected from the group of Escherichia coli, Klebsiella planticola, Bacillus licheniformis, Bacillus lentus, Bacillus amyloliquefaciens, Bacillus subtilis, Bacillus alcalophilus, Bacillus globigu, Bacillus gibsonii, Bacillus pumilus, Staphylococcus carnosus, Corynebacterium glutamicum, Arthrobacter oxidans, Streptomyces lividans, Streptomyces coelicolor and Stenotrophomonas maltophilia.

1. i. ein Molekulargewicht (MW) aufweist von 150 bis 5x10⁶ Dalton, insbesondere von 200 bis 1x10⁶ Dalton, von 220 bis 0,75x10⁶ Dalton und insbesondere von 400 bis 0,5x10⁶ Dalton,
2. ii. ein Molekulargewicht (MW) aufweist von 500 bis 3000 Dalton, insbesondere von 600 bis 2500 Dalton, von 700 bis 2250 Dalton und insbesondere von 800 bis 2000 Dalton,
3. iii. ein Molekulargewicht (MW) aufweist von 150 bis 5x10⁶ Dalton, insbesondere von 200 bis 1x10⁶ Dalton, von 220 bis 0,75x10⁶ Dalton und insbesondere von 400 bis 0,5x10⁶ Dalton.

Advantageous synergistic cleaning performances also result from the fact that the substances used as component (b) have specific molecular weights. In a further embodiment of the invention, the method is characterized in that the component

1. i. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons,
2. ii. has a molecular weight (MW) of from 500 to 3000 daltons, in particular from 600 to 2500 daltons, from 700 to 2250 daltons and in particular from 800 to 2000 daltons,
3. iii. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons.

1. i. in dem Mittel vorliegt von 0,018 bis 0,2 Gew.-%, insbesondere von 0,04 bis 0,1 Gew.-%,
2. ii. in dem Mittel vorliegt von 0,001 % bis 25 Gew.-%, insbesondere von 0,005 bis 10 Gew.-%,
3. iii. in dem Mittel vorliegt von 0,018 bis 0,2 Gew.-%, insbesondere von 0,04 bis 0,1 Gew.-%.

Advantageous synergistic cleaning performance is further achieved by the fact that the substance used as component (b) is present in certain concentrations in the washing or cleaning agent. In a further embodiment of the invention, the method is characterized in that the component

1. i. in the composition is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%,
2. ii. in the composition is from 0.001% to 25% by weight, in particular from 0.005 to 10% by weight,
3. iii. in the agent is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%.

With regard to the use concentration, ie the concentration in the washing or cleaning liquor, a particularly advantageous synergistic cleaning performance also results from the fact that the substance used as component (b) is present in a certain concentration in the washing or cleaning liquor. In a further embodiment of the invention, the process is accordingly characterized in that this component is present in the washing or cleaning liquor in a concentration of from 0.00025 to 0.6% by weight, in particular from 0.0003 to 0.5% by weight .-%. This advantageous use concentration relates to the components i described above. and / or ii. and / or iii. and / or iv.

Detergents and cleaning agents which can be used in the process according to the invention include all conceivable types of detergents or cleaners, both concentrates and undiluted agents, for use on a commercial scale, in the washing machine or in hand washing or cleaning. These include detergents for textiles, carpets, or natural fibers, for which the term detergent is used. These include, for example, dishwashing detergents for dishwashers or manual dishwashing detergents or cleaners for hard surfaces such as metal, glass, porcelain, ceramics, tiles, stone, painted surfaces, plastics, wood or leather, for which the term detergent is used, ie in addition to manual and machine Dishwashing agents, for example, scouring agents, glass cleaners, toilet scenters, etc. The washing and cleaning agents in the invention also include washing aids which are added to the actual detergent in the manual or machine textile laundry to achieve a further effect. Furthermore, laundry detergents and cleaners in the context of the invention also include textile pre-treatment and post-treatment agents, ie those agents with which the laundry item is brought into contact before the actual laundry, for example to dissolve stubborn soiling, and also agents which are in one of the actual Textile laundry downstream step to give the laundry further desirable properties such as comfortable grip, crease resistance or low static charge. Among the latter, i.a. calculated the fabric softener.

The detergents or cleaning agents which can be used in the process according to the invention, which can be in the form of homogeneous solutions or suspensions, in particular in powdered solids, can in addition to the active compounds used according to the invention - the components (a) and (b) - in principle all known and contain usual ingredients in such agents, wherein preferably at least one further ingredient is present in the agent. The agents may in particular be builders, surface-active surfactants, bleaches based on organic and / or inorganic peroxygen compounds, bleach activators, water-miscible organic solvents, enzymes, sequestering agents, electrolytes, pH regulators and other auxiliaries such as optical brighteners, grayness inhibitors, foam regulators and colorants and fragrances, and combinations thereof. In particular, a further combination of the active compounds according to the invention with one or more further ingredient (s) of the agents proves advantageous, since then a further improved cleaning performance can be achieved by further resulting synergisms. In particular, the combination with a surfactant and / or a builder and / or a bleaching agent such a further synergism is achieved. Such preferred further ingredients of the washing or cleaning agent are disclosed in the international publication WO 2009/021867 , whose disclosure is therefore expressly referred to or the disclosure thereof is therefore expressly incorporated into the present application.

The ingredients to be selected as well as the conditions under which the agent is used, such as temperature, pH, ionic strength, redox ratios or mechanical influences, should be optimized for the respective cleaning problem. Thus, conventional temperatures for the use of detergents and cleaners in the ranges of 10 ° C over 40 ° C and 60 ° C up to 95 ° for mechanical means or in technical applications. Preferably, the ingredients of the respective agents are coordinated, in particular in such a way that synergies arise with regard to the cleaning performance. Particularly preferred are synergies which are present in a temperature range between 10 ° C and 60 ° C, in particular in a temperature range of 10 ° C to 50 ° C, from 10 ° C to 40 ° C, from 10 ° C to 30 ° C. , from 15 ° C to 30 ° C from 10 ° C to 25 ° C, from 15 ° C to 25 ° C, and most preferably at 20 ° C.

In another preferred embodiment, an agent useful in the method of the invention further contains the hydrolytic enzyme in an amount of from 2 μg to 20 mg, preferably from 5 μg to 17.5 mg, more preferably from 20 μg to 15 mg and most preferably from 50 μg to 10 mg per g of the agent. Further, the hydrolytic enzyme contained in the agent, in particular a protease, and / or other ingredients of the agent may be coated with a substance impermeable to the enzyme at room temperature or in the absence of water, which becomes permeable to the enzyme under conditions of use of the agent. Such an embodiment of the invention is thus characterized in that the hydrolytic enzyme is coated with a substance which is impermeable to the enzyme at room temperature or in the absence of water. Furthermore, the washing or cleaning agent itself may be packaged in a container, preferably an air-permeable container, from which it is released shortly before use or during the washing process.

1. (a) in fester Form vorliegt, insbesondere als rieselfähiges Pulver mit einem Schüttgewicht von 300 g/l bis 1200 g/l, insbesondere 500 g/l bis 900 g/l, oder
2. (b) in pastöser oder in flüssiger Form vorliegt, und/oder
3. (c) als Einkomponentensystem vorliegt, oder
4. (d) in mehrere Komponenten aufgeteilt ist.

In further embodiments of the invention, the method is characterized in that the washing or cleaning agent

1. (A) is in solid form, in particular as a free-flowing powder having a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l, or
2. (b) is in pasty or liquid form, and / or
3. (c) is present as a one-component system, or
4. (d) is divided into several components.

These embodiments of the present invention furthermore comprise all solid, powdery, liquid, gelatinous or paste-like administration forms of the agents which can be used in the method according to the invention, which if appropriate can also consist of several phases and can be present in compressed or uncompressed form. The agent can be present as a free-flowing powder, in particular with a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l or 600 g / l to 850 g / l. The solid dosage forms of the composition also include extrudates, granules, tablets or pouches. Alternatively, the agent can also be liquid, gelatinous or pasty, for example in the form of a non-aqueous liquid detergent or a non-aqueous paste or in the form of an aqueous liquid detergent or a water-containing paste. Furthermore, the agent may be present as a one-component system. Such means preferably consist of one phase. Alternatively, an agent can also consist of several phases. Such an agent is therefore divided into several components.

Detergents or cleaning agents which can be used in the process according to the invention may contain exclusively a hydrolytic enzyme, for example and in particular a protease. Alternatively, however, they may also contain further hydrolytic enzymes or other enzymes in a concentration which is expedient for the effectiveness of the agent, it being possible in principle to use all enzymes established for this purpose in the prior art. Preferred enzymes which can be used as enzymes are all enzymes which can display catalytic activity in the composition, in particular proteases, amylases, cellulases, hemicellulases, mannanases, tannases, xylanases, xanthanases, β-glucosidases, carrageenases, oxidases, perhydrolases, oxidoreductases or lipases, and preferably mixtures thereof. These enzymes are basically of natural origin; Starting from the natural molecules, improved variants are available for use in detergents and cleaners, which are preferably used accordingly.

1. (a) Bereitstellen einer Wasch- oder Reinigungslösung umfassend ein Wasch- oder Reinigungsmittel, das
   1. i. ein hydrolytisches Enzym enthält, insbesondere eine Protease, Amylase, Cellulase, Hemicellulase, Mannanase, Tannase, Xylanase, Xanthanase, ß-Glucosidase, Carrageenase oder eine Lipase, besonders bevorzugt eine Protease, und
   2. ii. eine Komponente enthält, die im Zusammenwirken mit dem hydrolytischen Enzym bei Anwendung des Mittels eine synergistische Reinigungsleistung bewirkt und die ausgewählt ist aus
      1. 1. Aminosäure oder Polyaminosäure oder deren Derivat und/oder
      2. 2. Biotensid und/oder
      3. 3. mikrobieller Metabolit
      4. 4. Präparat eines mikrobiellen Kulturüberstandes, das mindestens 2,5 Gew.-% einer der Substanzen 1) bis 3);
2. (b) In Kontakt bringen eines Textils oder einer harten Oberfläche mit der Wasch- oder Reinigungslösung gemäß (a).

Another object of the invention is a washing or cleaning process comprising the process steps

1. (A) providing a washing or cleaning solution comprising a washing or cleaning agent, the
   1. i. a hydrolytic enzyme, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase or a lipase, more preferably a protease, and
   2. ii. contains a component which, in cooperation with the hydrolytic enzyme when using the agent causes a synergistic cleaning performance and which is selected from
      1. 1. amino acid or polyamino acid or its derivative and / or
      2. 2. biosurfactant and / or
      3. 3. microbial metabolite
      4. 4. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of substances 1) to 3);
2. (b) contacting a textile or a hard surface with the washing or cleaning solution according to (a).

All facts, objects and embodiments described above for all methods according to the invention are also applicable to this subject of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to this subject of the invention.

Such a method is advantageous since, as described above, the cleaning performance of a washing or cleaning agent containing a corresponding hydrolytic enzyme is improved by the addition of a component as indicated. Thus, the method is advantageous to remove from textiles or hard surfaces corresponding contaminants, especially proteinaceous impurities. Embodiments of this subject invention include, for example, hand washing, manual removal of stains from textiles or from hard surfaces or machine processes.

Methods for cleaning textiles are generally distinguished by the fact that various cleaning-active substances are applied to the items to be cleaned in a plurality of process steps and washed off after the action time, or that the items to be cleaned are otherwise treated with a detergent or a solution of this agent. The same applies to methods for cleaning hard surfaces.

Since a hydrolytic enzyme, i. Component (a), which naturally already possesses a hydrolytic activity and also unfolds these in media which otherwise have no cleaning power, such as, for example, in mere buffer, such a method can also consist merely in that apart from the added component (b) the only other Component a hydrolytic enzyme, ie Component (a) is applied, preferably in a buffer solution or in water. This represents a further embodiment of this subject of the invention.

All processes of the invention are preferably in a temperature range of 10 ° C to 60 ° C, in particular from 10 ° C to 50 ° C, from 10 ° C to 40 ° C, from 10 ° C to 30 ° C, from 15 ° C to 30 ° C from 10 ° C to 25 ° C and from 15 ° C to 25 ° C performed. A synergistic interaction of the components (a) and (b) with regard to the cleaning performance is especially at these lower to middle washing temperatures or cleaning temperatures.

1. i. Aminosäure oder Polyaminosäure oder deren Derivat und/oder
2. ii. Biotensid und/oder
3. iii. mikrobieller Metabolit und/oder
4. iv. Präparat eines mikrobiellen Kulturüberstandes, das mindestens 2,5 Gew.-% einer der Substanzen i) bis iii) enthält

zum Erreichen einer synergistischen Reinigungsleistung im Zusammenwirken mit einem hydrolytischen Enzym in einem Wasch- oder Reinigungsmittel bei Anwendung des Wasch- oder Reinigungsmittels, insbesondere im Zusammenwirken mit einer Protease, Amylase, Cellulase, Hemicellulase, Mannanase, Tannase, Xylanase, Xanthanase, ß-Glucosidase, Carrageenase oder einer Lipase, besonders bevorzugt im Zusammenwirken mit einer Protease.Another object of the invention is the use of a component which is selected from

1. i. Amino acid or polyamino acid or its derivative and / or
2. ii. Biosurfactant and / or
3. iii. microbial metabolite and / or
4. iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii)

for achieving a synergistic cleaning performance in conjunction with a hydrolytic enzyme in a washing or cleaning agent when using the washing or cleaning agent, in particular in conjunction with a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, Carrageenase or a lipase, particularly preferably in conjunction with a protease.

The facts, objects and embodiments described for washing or cleaning processes according to the invention are also applicable to this subject of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive use.

1. i. in dem Mittel vorliegt von 0,018 bis 0,2 Gew.-%, insbesondere von 0,04 bis 0,1 Gew.-%,
2. ii. in dem Mittel vorliegt von 0,001 % bis 25 Gew.-%, insbesondere von 0,005 bis 10 Gew.-%,
3. iii. in dem Mittel vorliegt von 0,018 bis 0,2 Gew.-%, insbesondere von 0,04 bis 0,1 Gew.-%.

In a further embodiment, the use is accordingly characterized in that the component

1. i. in the composition is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%,
2. ii. in the composition is from 0.001% to 25% by weight, in particular from 0.005 to 10% by weight,
3. iii. in the agent is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%.

1. i. Aminosäure oder Polyaminosäure oder deren Derivat und/oder
2. ii. Biotensid und/oder
3. iii. mikrobieller Metabolit und/oder
4. iv. Präparat eines mikrobiellen Kulturüberstandes, das mindestens 2,5 Gew.-% einer der Substanzen i) bis iii) enthält

zur Steigerung der Reinigungsleistung eines hydrolytischen Enzyms in einem Wasch- oder Reinigungsprozess. Wie vorstehend beschrieben wirken diese Komponenten (Komponente (b)) vorteilhaft, insbesondere synergistisch, mit einem hydrolytischen Enzym (Komponente (a)) zusammen, so dass nicht nur die Reinigungsleistung eines Wasch- oder Reinigungsmittels (bzw. der von diesem Mittel gebildeten Waschflotte) verbessert wird, sondern auch die Reinigungsleistung des hydrolytischen Enyzms selbst. Die Sachverhalte, Gegenstände und Ausführungsformen, die für erfindungsgemäße Wasch- oder Reinigungsverfahren beschrieben sind, sind auch auf diesen Erfindungsgegenstand anwendbar. Daher wird an dieser Stelle ausdrücklich auf die Offenbarung an entsprechender Stelle verwiesen mit dem Hinweis, dass diese Offenbarung auch für die vorstehende erfindungsgemäße Verwendung gilt.Another object of the invention is the use of a component which is selected from

1. i. Amino acid or polyamino acid or its derivative and / or
2. ii. Biosurfactant and / or
3. iii. microbial metabolite and / or
4. iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii)

to increase the cleaning performance of a hydrolytic enzyme in a washing or cleaning process. As described above, these components (component (b)) interact advantageously, in particular synergistically, with a hydrolytic enzyme (component (a)), so that not only the cleaning performance of a washing or cleaning agent (or the wash liquor formed by this agent) but also the cleaning performance of the hydrolytic enzyme itself. The facts, objects and embodiments described for washing or cleaning processes according to the invention are also applicable to this subject of the invention. Therefore, reference is made at this point expressly to the disclosure in the appropriate place with the statement that this disclosure also applies to the above inventive use.

1. i. ein Molekulargewicht (MW) aufweist von 150 bis 5x10⁶ Dalton, insbesondere von 200 bis 1x10⁶ Dalton, von 220 bis 0,75x10⁶ Dalton und insbesondere von 400 bis 0,5x10⁶ Dalton,
2. ii. ein Molekulargewicht (MW) aufweist von 500 bis 3000 Dalton, insbesondere von 600 bis 2500 Dalton, von 700 bis 2250 Dalton und insbesondere von 800 bis 2000 Dalton,
3. iii. ein Molekulargewicht (MW) aufweist von 150 bis 5x10⁶ Dalton, insbesondere von 200 bis 1x10⁶ Dalton, von 220 bis 0,75x10⁶ Dalton und insbesondere von 400 bis 0,5x10⁶ Dalton.

Preferred embodiments of uses according to the invention are further characterized in that the component is contained in a microbial culture supernatant, in particular in a bacterial or fungal culture supernatant, in particular in a culture supernatant of Bacillus sp. and in particular in a culture supernatant of Bacillus subtilis, Bacillus licheniformis Bacillus pumilus, Bacillus aeolius or Bacillus subtilis natto. It has been found that culture supernatants of these microorganisms at least one, preferably several components i. to iv. include and thus can advantageously be applied according to the invention. Furthermore, advantageous cleaning results in particular in that the substances used as component (b) have certain molecular weights. Further preferred embodiments of uses according to the invention are accordingly characterized in that the component

1. i. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons,
2. ii. has a molecular weight (MW) of from 500 to 3000 daltons, in particular from 600 to 2500 daltons, from 700 to 2250 daltons and in particular from 800 to 2000 daltons,
3. iii. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons.

Examples: example 1

To determine the washing performance, the following formulation was used for a laundry detergent (see Table 2). Table 2: ingredient Wt .-% pure substance xanthan 0.3-0.5 Anti-foaming agents 0.2-0.4 glycerin 6-7 ethanol 0.3-0.5 FAEOS 4-7 Nonionic surfactants (FAEO, APG, etc.) 24 - 28 boric acid 1 Sodium citrate (dihydrate) 1-2 soda 2-4 Coconut fatty acids 14-16 HEDP 0.5 PVP 0-0.4 Optical brighteners 0-0.05 dye 0 to 0.001 Perfume 0-2 H ₂ O, demineralized rest

The assays were assembled into 48-well plates in 1 ml each of wash liquor as shown in Table 3 below. The incubation was carried out for 60 minutes at 40 ° C with shaking (about 600 revolutions per minute (rpm)). Table 3: volumes solution 420 μl 161-966 mg of laundry detergent in 42 ml of water or buffer 30-530 μl 1-100 PE / ml protease 30-530 μl Prepared substance solution rest H ₂ O Soiling Ø approx. 1cm

• Blut-Milch/Tusche auf Baumwolle: Produkt Nr. C5 von CFT B.V. Vlaardingen, Holland Voll-Ei/Pigment auf Baumwolle: Produkt Nr. 10N erhältlich von der Firma wfk Testgewebe GmbH; Brüggen-Bracht, Deutschland,
• Schokolade-Milch/Tusche auf Baumwolle: Produkt Nr. C3 von CFT B.V. Vlaardingen, Holland Erdnuss Öl-Pigment/Tusche auf Polyester/Baumwolle: Produkt Nr. PC10 von CFT B.V. Vlaardingen, Holland
• Gras auf Baumwolle: Produkt Nr. 164 von erhältlich von der Firma Eidgenössische Material- und Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Schweiz
• Kakao auf Baumwolle: Produkt Nr. 112 von erhältlich von der Firma Eidgenössische Material- und Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Schweiz.

Round pieces of stains (diameter approx. 10 mm) were used, which were selected from the following stains:

• Blood milk / ink on cotton: Product No. C5 from CFT BV Vlaardingen, Holland Whole egg / pigment on cotton: Product No. 10N available from the company wfk Testgewebe GmbH; Bruggen-Bracht, Germany,
• Chocolate milk / ink on cotton: Product No. C3 from CFT BV Vlaardingen, Holland Peanut oil pigment / ink on polyester / cotton: Product No. PC10 from CFT BV Vlaardingen, Holland
• Grass on cotton: Product No. 164 from available from the company Eidgenössische Material- und Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Switzerland
• Cocoa on cotton: Product No. 112 from available from the company Eidgenössische Material- und Prüfanstalt (EMPA) Testmaterialien AG, St. Gallen, Switzerland.

After incubation, the soils were rinsed, dried and fixed three times and the whiteness of the washed fabrics was measured as compared to a white standard (d / 8, 8mm, SCI / SCE) normalized to 100% (determination of L-value). , The measurement was carried out on a colorimeter (Minolta Cm508d) with an illumination setting of 10 ° / D65. The results obtained are given as percent power, the difference of the remission values from the base detergent without substance or enzymes to that with protease having been normalized to 100%.

Proteases used were the alkaline protease from Bacillus lentus DSM 5483 ( WO 92/21760 ), the protease from Bacillus pumilus according to WO2007 / 131656 and the protease shown in FIG. 2 or SEQ ID NO. 3 of the international publication WO 03/057713 is disclosed.

Example 2

The washing performance was tested with the following pure substances (component (b)): polyglutamate (poly-glutamic acid), lysine, phenylalanine, tyrosine, alanine, leucine, proline, cysteine, threonine, serine, glycine, aspartate, asparagine, 2,3- Butanediol, pyruvate, propionate, butyrate, levan and surfactin.

Stock solutions of these substances were prepared with 0.00001-1.5 M substance or 0.0001-55% (weight) in water or buffer (phosphate 0.00001-1.5 M pH 6.5-8.0 or Tris 0.00001-1.5 M pH 7.5-9.0 or Soerensen buffer pH 7.5-9.0 or citrate buffer 0.00001-1.5 M pH 4.5-7.0 or acetate buffer 0 , 00001-1.5 M pH 2.5-5.5).

The following Tables 4 to 9 show the washings obtained for each of the experimental approaches given (the abbreviation "nb" stands for "not determined"). The amino acids are listed in standard shorthand notation. It is clear that the components used (b) cause a synergistic increase in the washing performance of those detergents containing a hydrolytic enzyme, namely a protease, ie component (a). In controls in which no hydrolytic enzyme is present (referred to as "blank"), these components (b) do not increase the washing performance, so that the increased washing performance is based on a beneficial, synergistic interaction of components (a) and (b).

Example 3

The washing performance was increased with bacterial or fungal fermenter supernatants and nutrient media (culture supernatants) or fractions from the purification of these fluids, especially with Bacillus fermenter and Bacillus culture media and fractions containing such substances.

Fermenter cultures were centrifuged or not centrifuged to separate solids and boiled (15 min, 97.5-100 ° C) to inactivate the enzymes. After the slurry had boiled, the resulting solution was centrifuged again to separate precipitate formed (= boiled supernatant). The boiled supernatant was optionally further treated by filtering it using a 10 kDa cutoff membrane, then via a 1 kDa cutoff membrane. The filtrate of the 1 kDa cutoff membrane was further fractionated by means of a Bio-Gel P2 column (gel permeation chromatography / size exclusion chromatography).

Used as component (b) were therefore culture supernatants or dilutions of two different cultures of Bacillus sp. (Strain 1 or strain 2) as well as differently processed and / or fractionated preparations of the supernatants as indicated in each case.

The following Tables 10 to 15 show the washing performance obtained. It is clear that the components used (b) cause a synergistic increase in the washing performance of detergents containing a hydrolytic enzyme, namely a protease, ie component (a). Furthermore, it becomes clear on the basis of the different effectiveness of individual fractions that the effect is based on individual, distinct constituents of the supernatants which are contained in the respective fractions, for example due to their size.

Example 4

The washing performance was achieved with surfactin or lichenycin or fermented supernatants from microorganisms producing surfactin, lichenigen or similar lipopeptide-type molecules. In the fermented supernatants, surfactin-like or surfactin-like molecules were detected by mass spectroscopy.

Tables 16 to 19 below show the washings obtained. It is clear that the components used (b) cause a synergistic increase in the washing performance of those detergents containing a hydrolytic enzyme, namely a protease, ie component (a). In controls which do not contain a hydrolytic enzyme, these components (b) do not increase the washing performance, so that the increased washing performance is due to an advantageous synergistic interaction of components (a) and (b). An inactivated hydrolytic enzyme (see Table 19) also results in no longer a synergistic cleaning performance, which is further evidence of the specific advantageous interaction of components (a) and (b).

Description of the figure:

FIG. 1:

Structure of surfactin

Claims (14)

Process for improving the cleaning performance of a washing or cleaning agent which comprises a hydrolytic enzyme, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase or a lipase, particularly preferably a protease, characterized in that a component is added to the washing or cleaning agent, which causes a synergistic cleaning performance in conjunction with the hydrolytic enzyme when using the agent and which is selected from i. Amino acid or polyamino acid or its derivative and / or ii. Biosurfactant and / or iii. microbial metabolite iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii). A method according to claim 1, characterized in that the component is contained in a microbial culture supernatant, in particular in a bacterial or fungal culture supernatant, in particular in a culture supernatant of Bacillus sp. and especially in a culture supernatant of Bacillus subtilis, Bacillus licheniformis, Bacillus pumilus, Bacillus aeolius or Bacillus subtilis natto, and added to the washing or cleaning agent as a culture supernatant, preferably as a fraction of the culture supernatant. Method according to one of claims 1 or 2, characterized in that the component i. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons, ii. has a molecular weight (MW) of from 500 to 3000 daltons, in particular from 600 to 2500 daltons, from 700 to 2250 daltons and in particular from 800 to 2000 daltons, iii. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons. Method according to one of claims 1 to 3, characterized in that the component i. in the composition is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%, ii. in the composition is from 0.001% to 25% by weight, in particular from 0.005 to 10% by weight, iii. in the agent is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%. Method according to one of claims 1 to 4, characterized in that the component is present in the washing or cleaning liquor in a concentration of 0.00025 to 0.6 wt .-%, in particular from 0.0003 to 0.5 wt. -%. Method according to one of claims 1 to 5, characterized in that the washing or cleaning agent, the hydrolytic enzyme in an amount of 2 micrograms to 20 mg, preferably from 5 micrograms to 17.5 mg, more preferably from 20 micrograms to 15 mg and most preferably from 50 μg to 10 mg per g of the agent, and / or
the hydrolytic enzyme in the washing or cleaning agent is coated with a substance which is impermeable to the enzyme at room temperature or in the absence of water. Method according to one of claims 1 to 6, characterized in that the washing or cleaning agent (A) is in solid form, in particular as a free-flowing powder having a bulk density of 300 g / l to 1200 g / l, in particular 500 g / l to 900 g / l, or (b) is in pasty or liquid form, and / or (c) is present as a one-component system, or (d) is divided into several components. Washing or cleaning process comprising the process steps (A) providing a washing or cleaning solution comprising a washing or cleaning agent, the i. a hydrolytic enzyme, in particular a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, β-glucosidase, carrageenase or a lipase, more preferably a protease, and ii. contains a component which, in cooperation with the hydrolytic enzyme when using the agent causes a synergistic cleaning performance and which is selected from 1. amino acid or polyamino acid or its derivative and / or 2. biosurfactant and / or 3. microbial metabolite 4. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of substances 1) to 3); (b) contacting a textile or a hard surface with the washing or cleaning solution according to (a). Method according to one of claims 1 to 8, characterized in that it is in a temperature range of 10 ° C to 60 ° C, in particular from 10 ° C to 50 ° C, from 10 ° C to 40 ° C, from 10 ° C to 30 ° C, from 15 ° C to 30 ° C from 10 ° C to 25 ° C and from 15 ° C to 25 ° C, is performed. Using a component that is selected from i. Amino acid or polyamino acid or its derivative and / or ii. Biosurfactant and / or iii. microbial metabolite and / or iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii), for achieving a synergistic cleaning performance in cooperation with a hydrolytic enzyme in a washing or cleaning agent using the washing or cleaning agent, in particular in conjunction with a protease, amylase, cellulase, hemicellulase, mannanase, tannase, xylanase, xanthanase, ß-glucosidase, carrageenase or a lipase, more preferably in conjunction with a protease. Use according to claim 10, characterized in that the component i. in the composition is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%, ii. in the composition is from 0.001% to 25% by weight, in particular from 0.005 to 10% by weight, iii. in the agent is from 0.018 to 0.2 wt .-%, in particular from 0.04 to 0.1 wt .-%. Using a component that is selected from i. Amino acid or polyamino acid or its derivative and / or ii. Biosurfactant and / or iii. microbial metabolite and / or iv. Preparation of a microbial culture supernatant containing at least 2.5% by weight of one of the substances i) to iii), to increase the cleaning performance of a hydrolytic enzyme in a washing or cleaning process. Use according to one of claims 10 to 12, characterized in that the component is contained in a microbial culture supernatant, in particular in a bacterial or fungal culture supernatant, in particular in a culture supernatant of Bacillus sp. and in particular in a culture supernatant of Bacillus subtilis, Bacillus licheniformis, Bacillus pumilus, Bacillus aeolius or Bacillus subtilis natto. Use according to one of claims 9 to 13, characterized in that component i. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons, ii. has a molecular weight (MW) of from 500 to 3000 daltons, in particular from 600 to 2500 daltons, from 700 to 2250 daltons and in particular from 800 to 2000 daltons, iii. a molecular weight (MW) of from 150 to 5x10 ⁶ daltons, in particular from 200 to 1x10 ⁶ daltons, from 220 to 0,75x10 ⁶ Dalton and in particular from 400 to 0.5x10 ⁶ daltons.

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