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WO2025002934A1 - Composition détergente comprenant des lipases - Google Patents

Composition détergente comprenant des lipases Download PDF

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Publication number
WO2025002934A1
WO2025002934A1 PCT/EP2024/067046 EP2024067046W WO2025002934A1 WO 2025002934 A1 WO2025002934 A1 WO 2025002934A1 EP 2024067046 W EP2024067046 W EP 2024067046W WO 2025002934 A1 WO2025002934 A1 WO 2025002934A1
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WO
WIPO (PCT)
Prior art keywords
detergent composition
aep
lipase
seq
acid
Prior art date
Application number
PCT/EP2024/067046
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English (en)
Inventor
Iben DAMAGER
Original Assignee
Novozymes A/S
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Publication date
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Publication of WO2025002934A1 publication Critical patent/WO2025002934A1/fr

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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
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/04—Carboxylic acids or salts thereof
    • C11D1/06—Ether- or thioether carboxylic acids
    • 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
    • C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
    • 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
    • C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
    • C11D2111/10—Objects to be cleaned
    • C11D2111/12—Soft surfaces, e.g. textile

Definitions

  • the present invention concerns a detergent composition
  • a detergent composition comprising a first lipase and a second lipase, wherein the lipases have synergistic effect on the removal of fat.
  • the present invention concerns the use of the detergent composition of the invention for cleaning of a textile.
  • Lipases are included in some detergents to improve fat (triglyceride) removal. Most commercially available lipases for use in detergent release short-chain fatty acids (e.g., butyric acid and hexanoic acid) when degrading lipid stains, leading to malodor perception. The majority of these lipases have a high degree of identity to the lipase having SEQ ID NO: 3 from Thermomyces lanuginosus and for the ease of reference they will be referred to as TLL-like lipases.
  • TLL-like lipase is often limited in laundry detergents by the highest acceptable level of malodors, in particular under wash conditions with low detergent load since TLL-like lipase will be left on the stain after wash and the amount of ester-free perfume system in the detergent formulation is limited due to the lower detergent concentration.
  • WO 2016/050661 discloses TLL-like lipase variants which develop a low level or reduced level of malodor as compared to the parent enzyme.
  • WO 2017/001673 (Novozymes A/S) relates to methods of reducing malodor during lipid stain removal.
  • GCL 1 lipases A different group of lipases has been described by Bertolini et al (Eur. J. Biochem. 228, 863- 869 (1995)), namely the Geotrichum candidum lipase I (GCL 1).
  • the GCL 1 lipase is highly specific for long-chain length unsaturated fatty acids (such as linoleic acid and alpha-linoleic acid) and creates thus less odor compared to TLL-like lipase when used in laundry detergents. For the ease of reference, they will be referred to as GCL 1 -like lipases.
  • WO 2022/162043 discloses detergent composition comprising GCL 1 lipase.
  • SEQ ID NO: 2 is disclosed in Shimada et al: cDNA Molecular Cloning of Geotrichum candidum Liase, The Journal of Biochemistry, Volume 106, Issue 3, September 1989, Pages 383-388, (world wide web: doi.org/10.1093/oxfordjournals.jbchem.a122862) and Swisss-Prot: P17573.
  • SEQ ID NO: 1 is a variant of SEQ ID NO: 2 with two substitutions: S509A and K511 R
  • SEQ ID NO: 3 is a lipase from Thermomyces lanuginosus
  • GCL 1 -like lipases that are specific for long-chain length unsaturated fatty acids (e.g., SEQ ID NO: 1) and TLL-like lipase (e.g., a variant of SEQ ID NO: 3) has a strong synergistic effect on the degradation of lipid stains during wash. This is important as it allows for reduced detergent concentrations without reduction of lipid removal.
  • lipases In addition to being produced from a renewable agricultural source, and in contrast to many detergent ingredients, lipases are naturally found in the environment and readily biodegradable.
  • the replacement of detergent ingredients with GCL 1-like lipases and TLL-like lipases addresses the United Nations’ Sustainable Development Goals, in particular Goal 12 “Responsible consumption and production”: replacing detergent ingredients with GCL 1-like lipases and TLL-like lipases allows the detergent producer - and thus the end user - to move from a fossil feedstock to a renewable feedstock and reduce the volume of persistent chemicals emitted to the environment.
  • the present invention concerns a detergent composition
  • a detergent composition comprising a first lipase having at least 60% identity to SEQ ID NO:2 and a second lipase having at least 60% identity to SEQ ID NO: 3.
  • the present invention concerns the use of a first lipase having at least 60% identity to SEQ ID NO:2 and a second lipase having at least 60% identity to SEQ ID NO: 3. Further aspects of the present invention are disclosed in the following. Definitions
  • AEP active enzyme protein: Enzyme protein which has a catalytic activity. There is various way to determine AEP. For example, AEP can be calculated by dividing total activities by the enzyme’s specific activity. Active site titration may be used to determine the concentration of AEP (Example B). Unless specifically indicated reference to amount of enzyme used for wash is to be understood as AEP.
  • corresponding to refers to a way of determining the specific amino acid of a sequence wherein reference is made to a specific amino acid sequence.
  • references are made to specific amino acid positions, the skilled person would be able to align another amino acid sequence to said amino acid sequence that reference has been made to, in order to determine which specific amino acid may be of interest in said another amino acid sequence.
  • the mature polypeptide disclosed in SEQ ID NO: 2 is used to determine the corresponding amino acid residue in another GCL 1 -like lipase.
  • the amino acid sequence of another GCL 1 -like lipase is aligned with the mature polypeptide disclosed in SEQ ID NO: 2, and based on the alignment, the amino acid position number corresponding to any amino acid residue in the mature polypeptide disclosed in SEQ ID NO: 2 is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice etal., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the mature polypeptide disclosed in SEQ ID NO:3 is used to determine the corresponding amino acid residue in another TLL-like lipase.
  • the amino acid sequence of another TLL-like lipase is aligned with the mature polypeptide disclosed in SEQ ID NO: 3, and based on the alignment, the amino acid position number corresponding to any amino acid residue in the mature polypeptide disclosed in SEQ ID NO: 3 is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), preferably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • adjunct ingredients include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners, carriers, hydrotropes, builders and co-builders, fabric hueing agents, anti-foaming agents, dispersants, processing aids, solvents, and/or pigments.
  • Suitable adjunct materials include, but are not limited to the components described below such as surfactants, builders, flocculating aid, chelating agents, dye transfer inhibitors, enzymes, enzyme stabilizers, enzyme inhibitors, catalytic materials, bleach activators, hydrogen peroxide, sources of hydrogen peroxide, preformed peracids, brighteners, suds suppressors, dyes, perfumes, structure elasticizing agents, fabric softeners,
  • Detergent composition refers to compositions that find use in the removal of undesired compounds from items to be cleaned, such as textiles.
  • the detergent composition may be used to e.g., clean textiles for both household cleaning and industrial cleaning.
  • the terms encompass any materials/compounds selected for the particular type of cleaning composition desired and the form of the product (e.g., liquid, gel, powder, granulate, paste, bar, or spray compositions) and includes, but is not limited to, detergent compositions (e.g., liquid and/or solid laundry detergents and fine fabric detergents; fabric fresheners; fabric softeners; laundry boosters; and textile and laundry pre-spotters/pre-treatment).
  • the detergent formulation may contain one or more additional enzymes (such as proteases, amylases, lipases, cutinases, cellulases, endoglucanases, xyloglucanases, pectinases, pectin lyases, xanthan lyases, xanthan endoglucases, peroxidases, haloperoxygenases, catalases and mannanases, or any mixture thereof), and/or detergent adjunct ingredients such as surfactants, builders, chelators or chelating agents, bleach system or bleach components, polymers (as set forth herein), fabric conditioners, foam boosters, suds suppressors, dyes, perfume, tannish inhibitors, optical brighteners, bactericides, fungicides, soil suspending agents, anti-corrosion agents, enzyme inhibitors or stabilizers, enzyme activators, bluing agents and fluorescent dyes, antioxidants, and solubilizers.
  • additional enzymes such as proteases, amy
  • Detergent load is the amount of detergent used in a wash cycle, typically expressed as g detergent/L wash liquour.
  • Enzyme detergency benefit is defined herein as the advantageous effect an enzyme may add to a detergent compared to the same detergent without the enzyme.
  • Important detergency benefits which can be provided by enzymes are stain removal, such as removal of lipid stains, with no or very little visible soils after washing and/or cleaning.
  • Fatty acid is a carboxylic acid with an aliphatic tail (chain), which is either saturated or unsaturated. Most naturally occurring fatty acids have a chain of an even number of carbon atoms, from 4 to 28. Fatty acids are usually derived from triglycerides or phospholipids. When they are not attached to other molecules, they are known as "free" fatty acids.
  • fatty acids include, but are not limited to, butanoic acid (butyric acid), pentanoic acid (valeric acid), hexanoic acid (caproic acid), heptanoic acid (enanthic acid), octanoic acid (caprylic acid), nonanoic acid (pelargonic acid), decanoic acid (capric acid), dodecanoic acid (lauric acid), tetradecanoic acid (myristic acid), hexadecanoic acid (palmitic acid), octadecanoic acid (stearic acid), eicosanoic acid (arachidic acid) oleic acid, palmitoleic acid linoleic acid, linolenic acid, arachidonic acid, eicosapentaenoic acid, and docosahexaenoic acid.
  • butanoic acid butyric acid
  • pentanoic acid valeric acid
  • a fatty acid and an acyl group of a lipid are equivalents.
  • the fatty acid is an acyl group of a lipid
  • the lipid can be a monoglyceride, diglyceride, triglyceride, phospholipid, sphingolipid, galactolipid, sterolester or wax ester.
  • the acyl group may be saturated or unsaturated, and optionally functional groups (substituents) may be attached.
  • acyl groups include, but are not limited to, the acyl forms of butanoic acid (butyric acid), pentanoic acid (valeric acid), hexanoic acid (caproic acid), heptanoic acid (enanthic acid), octanoic acid (caprylic acid), nonanoic acid (pelargonic acid), decanoic acid (capric acid), dodecanoic acid (lauric acid), tetradecanoic acid (myristic acid), hexadecanoic acid (palmitic acid), octadecanoic acid (stearic acid), eicosanoic acid (arachidic acid), linoleic acid, linolenic acid, arachidonic acid, eicosapentaenoic acid, oleic acid, palmitoleic acid, and docosahexaenoic acid
  • fragment means a polypeptide having one or more (e.g., several) amino acids absent from the amino and/or carboxyl terminus of a mature polypeptide or domain; wherein the fragment has the same activity as the mature enzyme, e.g., lipase activity.
  • host cell means any cell type that is susceptible to transformation, transfection, transduction, or the like with a nucleic acid construct or expression vector comprising a polynucleotide of the present invention.
  • host cell encompasses any progeny of a parent cell that is not identical to the parent cell due to mutations that occur during replication.
  • Improved wash performance is defined herein as an enzyme displaying an increased wash performance in a detergent composition relative to the wash performance of same detergent composition without the enzyme e.g. by increased stain removal or improved bleaching.
  • improved wash performance includes wash performance in laundry.
  • Isolated means a substance in a form or environment that does not occur in nature.
  • isolated substances include (1) any non-naturally occurring substance, (2) any substance including, but not limited to, any enzyme, variant, nucleic acid, protein, peptide or cofactor, that is at least partially removed from one or more or all of the naturally occurring constituents with which it is associated in nature; (3) any substance modified by the hand of man relative to that substance found in nature; or (4) any substance modified by increasing the amount of the substance relative to other components with which it is naturally associated (e.g., recombinant production in a host cell; multiple copies of a gene encoding the substance; and use of a stronger promoter than the promoter naturally associated with the gene encoding the substance).
  • An isolated substance may be present in a fermentation broth sample; e.g. a host cell may be genetically modified to express the polypeptide of the invention. The fermentation broth from that host cell will comprise the isolated polypeptide.
  • Laundering relates to both household laundering and industrial laundering and means the process of treating textiles with a solution containing a detergent composition and optionally one or more enzymes.
  • the laundering process can for example be carried out using e.g., a household or an industrial washing machine or can be carried out by hand.
  • Lipase refers to an enzyme in class EC3.1.1 as defined by Enzyme Nomenclature. It may have lipase activity (triacylglycerol lipase, EC3.1.1.3), cutinase activity (EC3.1.1.74), sterol esterase activity (EC3.1.1.13) and/or wax-ester hydrolase activity (EC3.1.1.50).
  • a “lipase substrate” or a “lipid” is any substrate which can be hydrolyzed by a lipase.
  • a lipase substrate is fat (triglycerides).
  • lipase activity i.e. the hydrolytic activity of the lipase
  • Malodor means an odor which is not desired on clean items. Malodor can be quantified by SPME-GC as released butyric acid or assessed by sensory panel scoring. Unless otherwise specified the term malodour may be used interchangeably with the term odor.
  • Mature polypeptide means a polypeptide in its final form following translation and any post-translational modifications, such as N-terminal processing, C-terminal truncation, glycosylation, phosphorylation, etc. Specifically, the term “mature polypeptide” may refer to a mature lipase.
  • parent lipase means a lipase to which an alteration is made to produce the lipase variants.
  • the parent lipase may be a naturally occurring (wild-type) polypeptide but may also be a variant and/or fragment thereof.
  • the parent GCL 1 -like lipase and the parent TLL-like lipase may be the ones shown in SEQ ID NO: 2 and SEQ ID NO: 3, respectively.
  • Rhamnolipid is a glycolipid that may be used as a biodegradable surfactant. RL may be in the form of mono-rhamnolipid or di-rhamnolipid, which consist of one or two rhamnose groups respectively, wherein the length of the chain may vary: m,n being 4 to 8.
  • rhamnolipid includes mono-rhamnolipid or dirhamnolipid, mixtures thereof and varying chain length as well as salts of rhamnolipid.
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity”.
  • sequence identity is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, J. Mol. Biol. 48: 443-453) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, Trends Genet. 16: 276-277), pref-erably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the output of Needle labeled “longest identity” is used as the percent identity and is calculated as follows:
  • sequence identity between two deoxyribonucleotide sequences is determined using the Needleman-Wunsch algorithm (Needleman and Wunsch, 1970, supra) as implemented in the Needle program of the EMBOSS package (EMBOSS: The European Molecular Biology Open Software Suite, Rice et al., 2000, supra), prefer-ably version 5.0.0 or later.
  • the parameters used are gap open penalty of 10, gap extension penalty of 0.5, and the EDNAFULL (EMBOSS version of NCBI NUC4.4) substitution matrix.
  • the output of Needle labeled “longest identity” (obtained using the -nobrief option) is used as the percent identity and is calculated as follows: (Identical Deoxyribonucleotides x 1OO)/(Length of Alignment - Total Number of Gaps in Alignment).
  • Sophorolipid in the context of the present application the term “sophorolipid” include sophorolipid in the lactone form and the corresponding acidic form as well as mixtures thereof. Further “sophorolipid” also includes salts of sophorolipid.
  • substantially same in the present invention is within the reasonable understanding of those skilled in the art, and may mean that the level of lipid removal of different detergent compositions is similar or no obvious difference, for example, the difference in the level of lipid removal is within e.g. 1%, 2% or 3% depending on the experimental errors.
  • Sustainability means use of renewable resources that cause little or no damage to the environment and are biodegradable.
  • Sustainability profile In the context of the present invention the term sustainability profile is used for comparing the sustainability of ingredients (e.g. in a detergent composition) where one or more ingredients can replace other less sustainable ingredients while maintaining the performance of the system (e.g. the performance of a detergent composition during wash of an item).
  • TEP Total Enzyme Protein is measured by amino acid analyses.
  • Textile means any textile material including yarns, yarn intermediates, fibers, non-woven materials, natural materials, synthetic materials, and any other textile material, fabrics made of these materials and products made from fabrics (e.g., garments and other articles).
  • the textile or fabric may be in the form of knits, wovens, denims, non-wovens, felts, yarns, and toweling.
  • the textile may be cellulose based such as natural cellulosics, includ-ing cotton, flax/linen, jute, ramie, sisal or coir or manmade cellulosics (e.g.
  • the textile or fabric may also be non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers.
  • non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabbit and silk or synthetic polymers such as nylon, aramid, polyester, acrylic, polypropylene and spandex/elastane, or blends thereof as well as blends of cellulose based and non-cellulose based fibers.
  • blends are blends of cotton and/or rayon/viscose with one or more companion material such as wool, synthetic fiber (e.g.
  • Fabric may be conventional washable laundry, for example stained household laundry.
  • fabric or garment it is intended to include the broader term textiles as well.
  • textile also covers fabrics.
  • the term “textile” is used interchangeably with fabric and cloth.
  • variant means a polypeptide having same activity as the parent enzyme comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more (e.g., several) positions.
  • a substitution means replacement of the amino acid occupying a position with a different amino acid;
  • a deletion means removal of the amino acid occupying a position; and
  • an insertion means adding an amino acid adjacent to and immediately following the amino acid occupying a position.
  • variant and variant may be used interchangeably unless it is clear from the context that the variant refers to another enzyme class.
  • substitutions For an amino acid substitution, the following nomenclature is used: Original amino acid, position, substituted amino acid. Accordingly, the substitution of threonine at position 226 with alanine is designated as “Thr226Ala” or “T226A”. Multiple mutations are separated by addition marks (“+”) or comma (“,”), e.g., “Gly205Arg + Ser411 Phe” or “G205R + “S411 F”, Gly205Arg,Ser411 Phe” or “G205R,S411 F” representing substitutions at positions 205 and 411 of glycine (G) with arginine (R) and serine (S) with phenylalanine (F), respectively.
  • Insertions For an amino acid insertion, the following nomenclature is used: Original amino acid, position, original amino acid, inserted amino acid. Accordingly, the insertion of lysine after glycine at position 195 is designated “Gly195GlyLys” or “G195GK”. An insertion of multiple amino acids is designated [Original amino acid, position, original amino acid, inserted amino acid #1 , inserted amino acid #2; etc.]. For example, the insertion of lysine and alanine after glycine at position 195 is indicated as “Gly195GlyLysAla” or “G195GKA”. In such cases the inserted amino acid residue(s) are numbered by the addition of lower case letters to the position number of the amino acid residue preceding the inserted amino acid residue(s). In the above example, the sequence would thus be:
  • Variants comprising multiple alterations are separated by addition marks (“+”) or by commas (“,”), e.g., “Arg170Tyr+Gly195Glu”, “R170Y+G195E”, “Arg170Tyr,Gly195Glu” or “R170Y.G195E” representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively.
  • “Tyr167Gly,Ala + Arg170Gly,Ala” or “Tyr167Gly/Ala + Arg170Gly/Ala” designates the following variants: “Tyr167Gly+Arg170Gly”, “Tyr167Gly+Arg170Ala”, “Tyr167Ala+Arg170Gly”, and “Tyr167Ala+Arg170Ala”.
  • amino acid X (or Xaa) is used herein to represent any of the 20 natural amino acids.
  • An “X” preceding a position means that any original amino acid at that position may be substituted.
  • X93Q means that any amino acid residue at position 93 other than Q is substituted with Q. This allows for designation of substitution to a particular amino acid in different parent mannanases, where the original amino acid may vary among different parent polypeptides.
  • wash cycle is defined herein as a washing operation wherein textiles are immersed in the wash liquor, mechanical action of some kind is applied to the textile in order to release stains and to facilitate flow of wash liquor in and out of the textile and finally the superfluous wash liquor is removed. After one or more wash cycles, the textile is generally rinsed and dried.
  • Wash liquor is defined herein as the solution or mixture of water and detergent components optionally including one or more enzymes.
  • Wash performance is used as the detergent composition’s, enzyme’s or polymer’s capability to remove stains present on the object to be cleaned or maintain color and whiteness of textile during wash.
  • the improvement in the wash performance may be quantified by lipid removal or odor generation as described in the Experimental section.
  • Weight percentage is abbreviated w/w%, wt% or w%. The abbreviations are used interchangeably.
  • Wild-type lipase means a lipase expressed by a naturally occurring microorganism, such as a bacterium, yeast, or filamentous fungus found in nature.
  • the wild-type lipase is the one shown in SEQ ID NO: 3 herein, which is derived from Thermomyces lanuginosus DSM 4109 (synonym Humicola lanuginosa DSM 4109).
  • the lipase is the one shown as SEQ ID NO: 2 herein, which is derived from a strain of Geotrichum candidum disclosed by Bertolini et al (Eur. J. Biochem. 228, 863-869 (1995)).
  • Figure 1 shows an alignment of the GCL 1 -like lipase having SEQ ID NO: 2 and the TLL-like lipase having SEQ ID NO: 3.
  • SEQ ID NO: 1 is a lipase from Geotrichum candidum
  • SEQ ID NO: 2 is a lipase from Geotrichum candidum
  • SEQ ID NO: 3 is a lipase from Thermomyces lanuginosus
  • SEQ ID NO: 4 is a lipase from Thermomyces lanuginosus
  • SEQ ID NO: 5 is a lipase from Thermomyces lanuginosus
  • the inventors of the present invention have surprisingly found that GCL 1 -like lipases in combination with TLL-like lipases have a very good and synergistic performance on lipid removal from textile in wash with only low malodor generation. Further, the present invention shows that GCL 1 -like lipases in combination with TLL-like lipases have a good enzyme detergency benefit on lipid stain removal even when the detergent is dosed with reduced detergent load. Consequently, the invention makes it possible to use the GCL 1 -like lipases and the TLL-like lipases of the present invention in combination with good benefit in terms of lipid removal while at the same time allowing for significantly reduced detergent load.
  • the present invention concerns a detergent composition
  • a detergent composition comprising a first lipase having at least 60% identity to SEQ ID NO:2 and a second lipase having at least 60% identity to SEQ ID NO: 3.
  • the first lipase (a GCL 1 -like lipase) has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1 or the polypeptide of SEQ ID NO:2 .
  • the second lipase (a TLL-like lipase) is a varianat of SEQ ID NO: 3 that has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99%, or 100% sequence identity to any of the polypeptides of SEQ ID NO: 3, SEQ ID NO: 4 or SEQ ID NO: 5.
  • the invention concerns a detergent composition
  • a detergent composition comprising a first lipase selected from the group of lipases disclosed the section “GCL -l-like lipases” below and a second lipase selected from the group of lipases disclosed in the section “TLL-like lipases” below.
  • GCL 1 -like lipases and the TLL-like lipases are further specified in the paragraphs below (“GCL 1 -like lipases” and “TLL-like lipases”).
  • the present invention concerns the use of a first lipase having at least 60% e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1 or the polypeptide of SEQ ID NO:2, and a second lipase having at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, at least 90%, at least 91 %, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%
  • the wash liquor may have a temperature in the range of 5°C to 95°C, or in the range of 10°C to 80°C, in the range of 10°C to 70°C, in the range of 10°C to 60°C, in the range of 10°C to 50°C, in the range of 15°C to 40°C or in the range of 20°C to 40°C.
  • the above method for laundering an item further comprises draining of the wash liquor or part of the wash liquor after completion of a wash cycle.
  • the wash liquor can then be re-used in a subsequent wash cycle or in a subsequent rinse cycle.
  • the item may be exposed to the wash liquor during a first and optionally a second or a third wash cycle.
  • the item is rinsed after being exposed to the wash liquor.
  • the item can be rinsed with water or with water comprising a conditioner.
  • the GCL 1-like lipase has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 1 .
  • the GCL 1-like lipase comprises one or more, such as 2, 3, 4 or 5, variations selected from the group consisting of S509A, K511 R, S538T, T541 N and F543 when aligned with SEQ ID NO: 2 applying the settings outlined in the paragraph “Corresponding to”.
  • the GCL 1-like lipase comprises the variations S509A and K511 R when aligned with SEQ ID NO: 2 applying the settings outlined in the paragraph “Corresponding to”.
  • the GCL 1 -like lipase comprises the variations S538T, T541 N and F543Y when aligned with SEQ ID NO: 2 applying the settings outlined in the paragraph “Corresponding to”.
  • the GCL 1 -like lipase comprises the variations T541 N and F543Y when aligned with SEQ ID NO: 2 applying the settings outlined in the paragraph “Corresponding to”.
  • the GCL 1-like lipase comprises the variations I70F, I83L, A278T, G281S, E284D, E381Q, A402S, K501Q, S509A, wherein numbering is according to SEQ ID NO: 2 applying the settings outlined in the paragraph “Corresponding to”.
  • GCL 1 shows higher specific activity against unsaturated substrates with long fatty acyl chains (such as C18 cis-9, cis-12 and C22 cis-9, cis-12, cis-15).
  • the TLL-like lipase is a varianat of SEQ ID NO: 3 that has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99%, or 100% sequence identity to the polypeptide of SEQ ID NO: 3.
  • the TLL-like lipase is a lipase variant having lipase activity and comprises one or more of the following substitutions corresponding to E1C, T231 R, N233R, and N233C of SEQ ID NO: 3 and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3.
  • the TLL-like lipase is a lipase variant comprising substitutions corresponding to T231 R+N233R, and optionally at least one or more (e.g., several) of D96E, D111 A, D254S, G163K, P256T, G91T and G38A of SEQ ID NO: 3 and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3.
  • the TLL-like lipase is a lipase variant comprising substitutions corresponding to the substitutions selected from the following set of substitutions in SEQ ID NO: 3: R231 R+N233R; D96E+T231 R+N233R; N33Q+D96E+T231 R+N233R;
  • D96E+D111A+T231 R+N233R+D254S; D96E+D111 A+T231 R+N233R+D254S+P256T D96E+D111 A+T231 R+N233R+P256T; D96E+G163K+T231 R+N233R+D254S+P256T; D96E+T231 R+N233R+D254S+P256T; D96E+T231 R+N233R+P256T;
  • T231 R+N233R+D254S+P256T; T231 R+N233R+P256T and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3.
  • the TLL-like lipase is a lipase variant, wherein said variant
  • (a) comprises a modification in at least one position corresponding to positions E1 , V2, N33, F51 , E56, L69, K98, V176, H198, E210, Y220, L227, and K237 of SEQ ID NO: 3; and optionally further comprises a modification in at least one position corresponding to positions D27, G38, D96, D111 , G163, T231 , N233, D254, and P256 of SEQ ID NO: 3;
  • the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3.;
  • the TLL-like lipase is a variant comprising a modification corresponding to at least one of the following positions of SEQ ID NO: 3: E1 , V2, D27, N33, G38, F51 , E56, L69, D96, K98, D111 , G163, V176, H198, E210, Y220, L227, T231 , N233, K237, D254, and P256 and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3..
  • the TLL-like lipase is a lipase variant comprising at least one modification corresponding to the following modifications of SEQ ID NO: 3: E1C, V2Y, D27R, N33K, N33Q, G38A, F51V, E56K, L69R, D96E, D96L, K98I, K98Q, D111A, G163K, V176L, H198S, E210K, Y220F, L227G, T231 R, N233R, N233C, K237C, D254S, and P256T and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at
  • the TLL-like lipase is a lipase variant further comprises one of the substitutions corresponding to the substitutions in SEQ ID NO: 3 selected from the group of: S54T, S83T, G91A, A150G, I255A, and E239C and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3..
  • TLL-like lipase is a variant comprising substitutions E1C+N233C, and optionally one or more additional substitutions, wherein numbering is according to SEQ ID NO: 3 and the variant has at least 60%, e.g., at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 86%, at least 87%, at least 88%, at least 89%, 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%, at least 99% sequence identity to the polypeptide of SEQ ID NO: 3..
  • the TLL-like lipase is a variant comprising substitutions corresponding to the substitutions selected from the following set of substitutions of SEQ ID NO: 3: E1C+N233C; E1C+H198L+N233C; E1C+H198G+N233C; E1C+L69V+N233C; E1C+L69T+N233C;
  • E1C+T231 R+N233C; E1C+H198S+N233C; E1C+D111A+N233C; E1C+D96E+N233C;
  • E1C+K98V+N233C E1C+F51 L+N233C; E1C+F511+N233C; E1C+K237C; E1C+L227G+N233C;
  • the TLL-like lipase, or lipase variant may be derived from a strain of Thermomyces, in particular Thermomyces lanuginosus (TLL).
  • TLL Thermomyces lanuginosus
  • the number of amino acid substitutions, deletions and/or insertions introduced into the polypeptide SEQ ID NO: 1 , SEQ ID NO: 2, SEQ ID NO: 3, SEQ ID NO: 4 or SEQ ID NO: 5, is not more than 10, e.g., 1 , 2, 3, 4, 5, 6, 7, 8 or 9.
  • amino acid changes may be of a minor nature, that is conservative amino acid substitutions or insertions that do not significantly affect the folding and/or activity of the protein; small deletions, typically of 1-30 amino acids; small amino- or carboxyl-terminal extensions, such as an amino-terminal methionine residue; a small linker peptide of up to 20-25 residues; or a small extension that facilitates purification by changing net charge or another function, such as a poly-histidine tract, an antigenic epitope or a binding domain.
  • conservative substitutions are within the groups of basic amino acids (arginine, lysine and histidine), acidic amino acids (glutamic acid and aspartic acid), polar amino acids (glutamine and asparagine), hydrophobic amino acids (leucine, isoleucine and valine), aromatic amino acids (phenylalanine, tryptophan and tyrosine), and small amino acids (glycine, alanine, serine, threonine and methionine).
  • Amino acid substitutions that do not generally alter specific activity are known in the art and are described, for example, by H. Neurath and R.L. Hill, 1979, In, The Proteins, Academic Press, New York.
  • amino acid changes are of such a nature that the physico-chemical properties of the polypeptides are altered.
  • amino acid changes may improve the thermal stability of the polypeptide, alter the substrate specificity, change the pH optimum, and the like.
  • Essential amino acids in a polypeptide can be identified according to procedures known in the art, such as site-directed mutagenesis oralanine-scanning mutagenesis (Cunningham and Wells, 1989, Science 244: 1081-1085). In the latter technique, single alanine mutations are introduced at every residue in the molecule, and the resultant mutant molecules are tested for enzyme activity to identify amino acid residues that are critical to the activity of the molecule. See also, Hilton et al., 1996, J. Biol. Chem. 271 : 4699-4708.
  • the active site of the enzyme or other biological interaction can also be determined by physical analysis of structure, as determined by such techniques as nuclear magnetic resonance, crystallography, electron diffraction, or photoaffinity labelling, in conjunction with mutation of putative contact site amino acids. See, for example, de Vos et al., 1992, Science 255: 306-312; Smith et al., 1992, J. Mol. Biol. 224: 899-904; Wlodaver et al., 1992, FEBS Lett. 309: 59-64.
  • the identity of essential amino acids can also be inferred from an alignment with a related polypeptide.
  • Single or multiple amino acid substitutions, deletions, and/or insertions can be made and tested using known methods of mutagenesis, recombination, and/or shuffling, followed by a relevant screening procedure, such as those disclosed by Reidhaar-Olson and Sauer, 1988, Science 241 : 53- 57; Bowie and Sauer, 1989, Proc. Natl. Acad. Sci. USA 86: 2152-2156; WO 95/17413; or WO 95/22625.
  • Other methods that can be used include error-prone PCR, phage display (e.g., Lowman et al., 1991 , Biochemistry 30: 10832-10837; U.S. Patent No. 5,223,409; WO 92/06204), and region- directed mutagenesis (Derbyshire et al., 1986, Gene 46: 145; Ner ef al., 1988, DNA 7: 127).
  • Mutagenesis/shuffling methods can be combined with high-throughput, automated screening methods to detect activity of cloned, mutagenized polypeptides expressed by host cells (Ness et al., 1999, Nature Biotechnology 17: 893-896). Mutagenized DNA molecules that encode active polypeptides can be recovered from the host cells and rapidly sequenced using standard methods in the art. These methods allow the rapid determination of the importance of individual amino acid residues in a polypeptide.
  • the invention is directed to detergent compositions comprising a GCL 1- like lipase and a TLL-like lipase in combination with one or more additional cleaning composition components.
  • the detergent composition comprises a GCL 1 -like lipase having at least 60% identity, such as 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99% or even 100% identity to the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 2 or any GCL 1 -like lipase as described in the paragraph “GCL 1-like lipases”.
  • the detergent composition comprises a TLL-like lipase having at least 60% identity, such as 70%, 80%, 90%, 95% identity to the amino acid sequence set forth in SEQ ID NO: 3, SEQ ID NO: 4 or SEQ ID NO: 5 or any TLL-like lipase as described in the paragraph “TLL-like lipases”.
  • the detergent composition is in solid form.
  • the detergent composition is in a liquid or gel form.
  • a bar form In a further form the detergent composition is in liquid form.
  • the detergent may be wrapped in water soluble PVOH film.
  • the concentration of the GCL1-like lipase (AEP) in the detergent having at least 60% identity, such as 70%, 80%, 90%, 95%, 96%, 97%, 98%, 99% or even 100% identity to the amino acid sequence set forth in SEQ ID NO: 1 or SEQ ID NO: 2 is preferably in the range from 0.3 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as 0.4 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as 0.5 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as 0.6 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as 0.7 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as 0.8 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as from 0.3 mg AEP/g detergent composition to 8 mg AEP/g detergent composition, such as 0.4 mg AEP/g detergent composition to 8 mg AEP/g detergent composition, such as 0.5 mg A
  • the concentration of the GCL 1-like lipase (AEP) in the wash liquor is typically in the range of 0.05-20 ppm (mg/L) enzyme protein, such as in the range of 0.05-15 ppm, in the range of 0.1-15 ppm, in the range of 0.2-15 ppm, in the range of 0.3-10 ppm, in the range of 0.4-8 ppm, such as 0.4- 7 ppm, 0.4-6 ppm, 0.4-5 ppm, 0.4-4 ppm, 0.4-3 ppm, 0.4-2 ppm, in the range of 0.1-15 ppm 0.5-15 ppm, in the range of 1-15 ppm, in the range of 1-10 ppm, in the range of 1-8 ppm, such as 1-7 ppm, 1-6 ppm, 1-5 ppm, 1-4 ppm, 1-3 ppm, 1-2 ppm.
  • the GCL 1-like lipase (as formulated product) may be present in the detergent in a concentration from 0.2-10 wt%, such as in the range of 0.5-5 wt%, such as in the range of 0.5-3 wt%, such as in the range of 0.5-2.5 wt%, or in the range of 0.5-2 wt%, or even in the range of 0.5-1 wt%.
  • the concentration of the TLL-like lipase (AEP) in the wash liquor is typically in the range of 0.01-10 ppm (mg/L) enzyme protein, such as in the range of 0.05-10 ppm, in the range of 0.1-5 ppm, 0.1-4 ppm, 0.1-3 ppm, 0.1-2 ppm, 0.1-1 ppm, 0.1-0.5 ppm.
  • the GCL 1-like lipase as well as the TLL-like lipase as formulated products may be present in the detergent in a concentration from 0.2-10 wt%, such as in the range of 0.5-5 wt%, such as in the range of 0.5-3 wt%, such as in the range of 0.5-2.5 wt%, or in the range of 0.5-2 wt%, or even in the range of 0.5-1 wt%.
  • the GCL 1-like lipase as well as the TLL-like lipase of the detergent composition of the invention may be stabilized using conventional stabilizing agents, e.g. a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g. an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid, and the composition may be formulated as described in, for example, WO92/19709 and WO92/19708.
  • a polyol such as propylene glycol or glycerol
  • a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g. an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid
  • a polypeptide of the present invention may also be incorporated in the detergent formulations disclosed in W097/07202, which is hereby incorporated by reference.
  • the detergent composition comprising a GCL 1-like lipase and a TLL-like lipase may be a liquid detergent.
  • the liquid detergent composition may comprise a microcapsule, and thus form part of any detergent composition in any form, such as liquid and powder detergents, and soap and detergent bars.
  • the invention is directed to liquid detergent compositions comprising a microcapsule, as described above, in combination with one or more additional cleaning composition components.
  • the microcapsule may be added to the liquid detergent composition in an amount corresponding to from 0.0001% to 5% (w/w) active enzyme protein (AEP); preferably from 0.001% to 5%, more preferably from 0.005% to 5%, more preferably from 0.005% to 4%, more preferably from 0.005% to 3%, more preferably from 0.005% to 2%, even more preferably from 0.01% to 2%, and most preferably from 0.01% to 1 % (w/w) active enzyme protein.
  • AEP active enzyme protein
  • the liquid detergent composition has a physical form, which is not solid (or gas). It may be a pourable liquid, a paste, a pourable gel or a non-pourable gel. It may be either isotropic or structured, preferably isotropic. It may be a formulation useful for washing in automatic washing machines or for hand washing. It may also be a personal care product, such as a shampoo, toothpaste, or a hand soap.
  • the liquid detergent composition may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to 70% water, up to 50% water, up to 40% water, up to 30% water, or up to 20% water.
  • Other types of liquids including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid detergent.
  • An aqueous liquid detergent may contain from 0-30% organic solvent.
  • a liquid detergent may even be non-aqueous, wherein the water content is below 10%, preferably below 5%.
  • Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.
  • the detergent composition may take the form of a unit dose product.
  • a unit dose product is the packaging of a single dose in a non-reusable container. It is increasingly used in detergents for laundry.
  • a detergent unit dose product is the packaging (e.g., in a pouch made from a water-soluble film) of the amount of detergent used for a single wash.
  • Pouches can be of any form, shape and material which is suitable for holding the composition, e.g., without allowing the release of the composition from the pouch prior to water contact.
  • the pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch.
  • Preferred films are polymeric materials preferably polymers which are formed into a film or sheet.
  • Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water-soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, maltodextrin, polymethacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC).
  • the level of polymer in the film for example PVA is at least about 60%.
  • Preferred average molecular weight will typically be about 20,000 to about 150,000.
  • Films can also be a blend composition comprising hydrolytically degradable and water-soluble polymer blends such as polyactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by Chris Craft In. Prod. Of Gary, Ind., US) plus plasticizers like glycerol, ethylene glycerol, Propylene glycol, sorbitol and mixtures thereof.
  • the pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water-soluble film.
  • the compartment for liquid components can be different in composition than compartments containing solids (see e.g., US 2009/0011970).
  • Detergent ingredients such as polyactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by Chris Craft In. Prod. Of Gary, Ind., US) plus plasticizers like glycerol, ethylene glycerol, Propylene glycol, sorbitol and mixtures thereof.
  • detergent components may include, for textile care, the consideration of the type of textile to be cleaned, the type and/or degree of soiling, the temperature at which cleaning is to take place, and the formulation of the detergent product.
  • components mentioned below are categorized by general header according to a particular functionality, this is not to be construed as a limitation, as a component may comprise additional functionalities as will be appreciated by the skilled artisan.
  • any detergent components known in the art for use in detergents may also be utilized.
  • Other optional detergent components include anti-corrosion agents, anti-shrink agents, anti-soil redeposition agents, anti-wrinkling agents, bactericides, binders, corrosion inhibitors, disintegrants/disintegration agents, dyes, enzyme stabilizers (including boric acid, borates, and/or polyols such as propylene glycol), fabric conditioners including clays, fillers/processing aids, fluorescent whitening agents/optical brighteners, foam boosters, foam (suds) regulators, perfumes, soil-suspending agents, softeners, suds suppressors, tarnish inhibitors, and wicking agents, either alone or in combination.
  • Any ingredient known in the art for use in detergents may be utilized. The choice of such ingredients is well within the skill of the artisan and includes conventional ingredients, including the exemplary non-limiting components set forth below.
  • the cleaning composition may comprise one or more surfactants, which may be anionic and/or cationic and/or non-ionic and/or semi-polar and/or zwitterionic, or a mixture thereof.
  • the detergent composition includes a surfactant system (comprising more than one surfactant) e.g. a mixture of one or more nonionic surfactants and one or more anionic surfactants.
  • the detergent comprises at least one anionic surfactant and at least one non-ionic surfactant, the weight ratio of anionic to nonionic surfactant may be from 20:1 to 1 :20.
  • the amount of anionic surfactant is higher than the amount of non-ionic surfactant e.g.
  • the weight ratio of anionic to non-ionic surfactant may be from 10:1 to 1.1 :1 or from 5:1 to 1.5:1.
  • the amount of anionic to non-ionic surfactant may also be equal and the weight ratios 1 :1.
  • the amount of non-ionic surfactant is higher than the amount of anionic surfactant and the weight ratio may be 1 : 10 to 1 :1.1.
  • the weight ratio of anionic to non-ionic surfactant is from 10:1 to 1 :10, such as from 5:1 to 1 :5, or from 5:1 to 1 :1.2.
  • the weight fraction of non-ionic surfactant to anionic surfactant is from 0 to 0.5 or 0 to 0.2 thus non-ionic surfactant can be present or absent if the weight fraction is 0, but if non-ionic surfactant is present, then the weight fraction of the nonionic surfactant is preferably at most 50% or at most 20% of the total weight of anionic surfactant and non-ionic surfactant.
  • Light duty detergent usually comprises more nonionic than anionic surfactant and there the fraction of non-ionic surfactant to anionic surfactant is preferably from 0.5 to 0.9.
  • the total weight of surfactant(s) is typically present at a level of from about 0.1% to about 60% by weight, such as about 1% to about 40%, or about 3% to about 20%, or about 3% to about 10%.
  • the surfactant(s) is chosen based on the desired cleaning application, and may include any conventional surfactant(s) known in the art.
  • the detergent When included therein the detergent will usually contain from about 1% to about 40% by weight of an anionic surfactant, such as from about 5% to about 30%, including from about 5% to about 15%, or from about 15% to about 20%, or from about 20% to about 25% of an anionic surfactant.
  • anionic surfactants include sulfates and sulfonates, typically available as sodium or potassium salts or salts of monoethanolamine (MEA, 2-aminoethan-1-ol) or triethanolamine (TEA, 2,2',2"-nitrilotriethan-1-ol); in particular, linear alkylbenzenesulfonates (l-AS), isomers of l_AS such as branched alkylbenzenesulfonates (BABS) and phenylalkanesulfonates; olefin sulfonates, in particular alphaolefinsulfonates (AOS); alkyl sulfates (AS), in particular fatty alcohol sulfates (FAS), i.e., primary alcohol sulfates (PAS) such as dodecyl sulfate (SLS); alcohol ethersulfates (AES or AEOS or FES, also known as alcohol ethoxysul
  • MEA
  • the detergent When included therein the detergent will usually contain from about 0,1% to about 40% by weight of a cationic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • a cationic surfactant for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12% or from about 10% to about 12%.
  • Non-limiting examples of cationic surfactants include alkyldimethylethanolamine quat (ADMEAQ), cetyltrimethylammonium bromide (CTAB), dimethyldistearylammonium chloride (DSDMAC), and alkylbenzyldimethylammonium, alkyl quaternary ammonium compounds, alkoxylated quaternary ammonium (AQA) compounds, ester quats, and combinations thereof.
  • ADMEAQ alkyldimethylethanolamine quat
  • CAB cetyltrimethylammonium bromide
  • DMDMAC dimethyldistearylammonium chloride
  • AQA alkoxylated quaternary ammonium
  • the detergent When included therein the detergent will usually contain from about 0.2% to about 40% by weight of a nonionic surfactant, for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%.
  • a nonionic surfactant for example from about 0.5% to about 30%, in particular from about 1 % to about 20%, from about 3% to about 10%, such as from about 3% to about 5%, from about 8% to about 12%, or from about 10% to about 12%.
  • nonionic surfactants include alcohol ethoxylates (AE or AEO) e.g.
  • AEO-7 alcohol propoxylates, in particular propoxylated fatty alcohols (PFA), ethoxylated and propoxylated alcohols, alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters (in particular methyl ester ethoxylates, MEE), alkylpolyglycosides (APG), alkoxylated amines, fatty acid monoethanolamides (FAM), fatty acid diethanolamides (FADA), ethoxylated fatty acid monoethanolamides (EFAM), propoxylated fatty acid monoethanolamides (PFAM), polyhydroxyalkyl fatty acid amides, or N-acyl N- alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamides, FAGA), as well as products available under the trade names SPAN and TWEEN, and combinations thereof.
  • PFA propoxylated fatty alcohols
  • the detergent When included therein the detergent will usually contain from about 0.01 to about 10 % by weight of a semipolar surfactant.
  • semipolar surfactants include amine oxides (AO) such as alkyldimethylamine oxides, in particular N-(coco alkyl)-N,N-dimethylamine oxide and N- (tallow-alkyl)-N,N-bis(2-hydroxyethyl)amine oxide, and combinations thereof.
  • AO amine oxides
  • the detergent When included therein the detergent will usually contain from about 0.01 % to about 10 % by weight of a zwitterionic surfactant.
  • zwitterionic surfactants include betaines such as alkyldimethylbetaines, sulfobetaines, and combinations thereof.
  • bio-based surfactants may be used e.g. wherein the surfactant is a sugar-based non-ionic surfactant which may be a hexyl-p-D-maltopyranoside, thiomaltopyranoside or a cyclic- maltopyranoside, such as described in EP2516606 B1.
  • Other biosurfactants may include rhamnolipids and sophorolipids.
  • a hydrotrope is a compound that solubilises hydrophobic compounds in aqueous solutions (or oppositely, polar substances in a non-polar environment).
  • hydrotropes typically have both hydrophilic and a hydrophobic character (so-called amphiphilic properties as known from surfactants); however, the molecular structure of hydrotropes generally do not favor spontaneous self-aggregation, see e.g. review by Hodgdon and Kaier (2007), Current Opinion in Colloid & Interface Science 12: 121-128. Hydrotropes do not display a critical concentration above which selfaggregation occurs as found for surfactants and lipids forming miceller, lamellar or other well defined meso-phases.
  • hydrotropes show a continuous-type aggregation process where the sizes of aggregates grow as concentration increases.
  • many hydrotropes alter the phase behavior, stability, and colloidal properties of systems containing substances of polar and non-polar character, including mixtures of water, oil, surfactants, and polymers.
  • Hydrotropes are classically used across industries from pharma, personal care, food, to technical applications.
  • Use of hydrotropes in detergent compositions allow for example more concentrated formulations of surfactants (as in the process of compacting liquid detergents by removing water) without inducing undesired phenomena such as phase separation or high viscosity.
  • the detergent may contain 0-10% by weight, for example 0-5% by weight, such as about 0.5 to about 5%, or about 3% to about 5%, of a hydrotrope.
  • Any hydrotrope known in the art for use in detergents may be utilized.
  • Non-limiting examples of hydrotropes include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xylene sulfonate (SXS), sodium cumene sulfonate (SCS), sodium cymene sulfonate, amine oxides, alcohols and polyglycolethers, sodium hydroxynaphthoate, sodium hydroxynaphthalene sulfonate, sodium ethylhexyl sulfate, and combinations thereof.
  • Builders and Co-Builders include sodium benzenesulfonate, sodium p-toluene sulfonate (STS), sodium xy
  • the detergent composition may contain about 0-65% by weight, such as about 5% to about 50% of a detergent builder or co-builder, or a mixture thereof.
  • the builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca and Mg. Any builder and/or co-builder known in the art for use in cleaning detergents may be utilized.
  • Non-limiting examples of builders include zeolites, diphosphates (pyrophosphates), triphosphates such as sodium triphosphate (STP or STPP), carbonates such as sodium carbonate, soluble silicates such as sodium metasilicate, layered silicates (e.g., SKS-6 from Clariant), ethanolamines such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'- iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2',2"-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CMI), and combinations thereof.
  • zeolites such as 2-aminoethan-1-ol (MEA), diethanolamine (DEA, also known as 2,2'- iminodiethan-1-ol), triethanolamine (TEA, also known as 2,2',2"-nitrilotriethan-1-ol), and (carboxymethyl)inulin (CM
  • the detergent composition may also contain from about 0-50% by weight, such as about 5% to about 30%, of a detergent co-builder.
  • the detergent composition may include a co-builder alone, or in combination with a builder, for example a zeolite builder.
  • co-builders include or copolymers thereof, such as poly(acrylic acid) (PAA) or copoly(acrylic acid/maleic acid) (PAA/PMA). According to the present invention, these components can be included in lower levels than in currently available detergent compositions.
  • Further non-limiting examples include citrate, chelators such as aminocarboxylates, aminopolycarboxylates and phosphonates, and alkyl- or alkenylsuccinic acid.
  • NTA 2,2’,2”-nitrilotriacetic acid
  • EDTA ethylenediaminetetraacetic acid
  • DTPA diethylenetriaminepentaacetic acid
  • IDS iminodisuccinic acid
  • EDDS ethylenediamine-N,N’- disuccinic acid
  • MGDA methylglycinediacetic acid
  • GLDA glutamic acid-N,N-diacetic acid
  • EDTMPA diethylenetriaminepentamethylenepentakis(phosphonic acid)
  • DTMPA or DTPMPA diethylenetriaminepentamethylenepentakis(phosphonic acid)
  • EDG N-(2- hydroxyethyl)iminodiacetic acid
  • ASMA aspartic acid-N-monoacetic acid
  • ASDA aspartic acid-N,N- diacetic acid
  • ASMP aspartic acid-N-monopropionic acid
  • IDA iminodisuccinic acid
  • SMAS N-(2- sulfomethyl)aspartic acid (SMAS), N-(2-sulfoethyl)aspartic acid (SEAS)
  • SMGL N-(2-sulfoethyl)glutamic acid
  • SEGL N-methyliminodiacetic acid
  • MIDA N-alanine-N,N- diacetic acid
  • SEDA serine-N,N-diacetic acid
  • MIDA isos
  • detergent compositions may contain 0-10% by weight, such as 0.5-5%, 2-5%, 0.5-2% or 0.2-1 % of a polymer. Any polymer known in the art for use in detergents may be utilized.
  • the polymer may function as a co-builder as mentioned above, or may provide anti-redeposition, fiber protection, soil release, dye transfer inhibition, grease cleaning and/or anti-foaming properties.
  • Some polymers may have more than one of the above-mentioned properties and/or more than one of the below-mentioned motifs.
  • Exemplary polymers include poly(vinyl alcohol) (PVA), poly(vinylpyrrolidone) (PVP), poly(ethyleneglycol) or polyethylene oxide) (PEG), ethoxylated poly(ethyleneimine), carboxymethyl inulin (CMI), and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of polyethylene terephthalate) and poly(oxyethene terephthalate) (PETPOET), PVP, poly(vinylimidazole) (PVI), poly(vinylpyridine-A/-oxide) (PVPO or PVPNO) and polyvinylpyrrolidone-vinylimidazole (PVPVI).
  • PVA poly(vinyl alcohol)
  • PVP poly(vinylpyrrolidone)
  • PEG polyethylene oxide
  • CMI carboxymethyl inulin
  • silicones copolymers of terephthalic acid and oligomeric glycol
  • polymers include polyethylene oxide and polypropylene oxide (PEO-PPO), diquaternium ethoxy sulfate, styrene/acrylic copolymer and perfume capsules
  • PEO-PPO polypropylene oxide
  • diquaternium ethoxy sulfate diquaternium ethoxy sulfate
  • styrene/acrylic copolymer and perfume capsules
  • Other exemplary polymers are disclosed in, e.g., WO 2006/130575. Salts of the above-mentioned polymers are also contemplated.
  • the detergent compositions of the present invention can also contain dispersants.
  • powdered detergents may comprise dispersants.
  • Suitable water-soluble organic materials include the homo- or co-polymeric acids or their salts, in which the polycarboxylic acid comprises at least two carboxyl radicals separated from each other by not more than two carbon atoms.
  • Suitable dispersants are for example described in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.
  • the detergent compositions of the present invention may also include fabric hueing agents such as dyes or pigments, which when formulated in detergent compositions can deposit onto a fabric when said fabric is contacted with a wash liquor comprising said detergent compositions and thus altering the tint of said fabric through absorption/reflection of visible light.
  • fabric hueing agents alter the tint of a surface as they absorb at least a portion of the visible light spectrum.
  • Suitable fabric hueing agents include dyes and dye-clay conjugates and may also include pigments.
  • Suitable dyes include small molecule dyes and polymeric dyes.
  • Suitable small molecule dyes include small molecule dyes selected from the group consisting of dyes falling into the Colour Index (C.l.) classifications of Direct Blue, Direct Red, Direct Violet, Acid Blue, Acid Red, Acid Violet, Basic Blue, Basic Violet and Basic Red, or mixtures thereof, for example as described in WG2005/03274, WG2005/03275, WG2005/03276 and EP1876226 (hereby incorporated by reference).
  • the detergent composition preferably comprises from about 0.00003 wt% to about 0.2 wt%, from about 0.00008 wt% to about 0.05 wt%, or even from about 0.0001 wt% to about 0.04 wt% fabric hueing agent.
  • the composition may comprise from 0.0001 wt% to 0.2 wt% fabric hueing agent, this may be especially preferred when the composition is in the form of a unit dose pouch.
  • Suitable hueing agents are also disclosed in, e.g. WO 2007/087257 and W02007/087243.
  • the detergent compositions of the present invention may also include one or more dye transfer inhibiting agents.
  • Suitable polymeric dye transfer inhibiting agents include, but are not limited to, polyvinylpyrrolidone polymers, polyamine A/-oxide polymers, copolymers of A/-vinylpyrrolidone and A/-vinylimidazole, polyvinyloxazolidones and polyvinylimidazoles or mixtures thereof.
  • the dye transfer inhibiting agents may be present at levels from about 0.0001 % to about 10%, from about 0.01% to about 5% or even from about 0.1% to about 3% by weight of the composition.
  • the detergent compositions of the present invention will preferably also contain additional components that may tint articles being cleaned, such as fluorescent whitening agent or optical brighteners. Where present the brightener is preferably at a level of about 0.01 % to about 0.5%.
  • fluorescent whitening agent suitable for use in a laundry detergent composition may be used in the composition of the present invention.
  • the most commonly used fluorescent whitening agents are those belonging to the classes of diaminostilbene-sulfonic acid derivatives, diarylpyrazoline derivatives and bisphenyl-distyryl derivatives.
  • diaminostilbene-sulfonic acid derivative type of fluorescent whitening agents include the sodium salts of: 4,4'-bis-(2- diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(2,4-dianilino-s- triazin-6-ylamino) stilbene-2.2'-disulfonate, 4,4'-bis-(2-anilino-4-(A/-methyl-A/-2-hydroxy-ethylamino)- s-triazin-6-ylamino) stilbene-2,2'-disulfonate, 4,4'-bis-(4-phenyl-1 ,2,3-triazol-2-yl)stilbene-2,2'- disulfonate and sodium 5-(2/7-naphtho[1 ,2-c/][1 ,2,3]triazol-2-yl)-2-[(E)
  • Preferred fluorescent whitening agents are Tinopal DMS and Tinopal CBS available from Ciba-Geigy AG, Basel, Switzerland.
  • Tinopal DMS is the disodium salt of 4,4'-bis- (2-morpholino-4-anilino-s-triazin-6-ylamino) stilbene-2,2'-disulfonate.
  • Tinopal CBS is the disodium salt of 2,2'-bis-(phenyl-styryl)-disulfonate.
  • fluorescent whitening agents is the commercially available Parawhite KX, supplied by Paramount Minerals and Chemicals, Mumbai, India.
  • Tinopal CBS-X is a 4.4'-bis-(sulfostyryl)-biphenyl disodium salt also known as Disodium Distyrylbiphenyl Disulfonate.
  • fluorescers suitable for use in the invention include the 1 -3-diaryl pyrazolines and the 7-alkylaminocoumarins.
  • Suitable fluorescent brightener levels include lower levels of from about 0.01 , from 0.05, from about 0.1 or even from about 0.2 wt % to upper levels of 0.5 or even 0.75 wt%. Soil release polymers
  • the detergent compositions of the present invention may also include one or more soil release polymers which aid the removal of soils from fabrics such as cotton and polyester based fabrics, in particular the removal of hydrophobic soils from polyester based fabrics.
  • the soil release polymers may for example be nonionic or anionic terephthalte based polymers, polyvinyl caprolactam and related copolymers, vinyl graft copolymers, polyester polyamides see for example Chapter 7 in Powdered Detergents, Surfactant science series volume 71 , Marcel Dekker, Inc.
  • Another type of soil release polymers are amphiphilic alkoxylated grease cleaning polymers comprising a core structure and a plurality of alkoxylate groups attached to that core structure.
  • the core structure may comprise a polyalkylenimine structure or a polyalkanolamine structure as described in detail in WO 2009/087523 (hereby incorporated by reference).
  • random graft co-polymers are suitable soil release polymers. Suitable graft co-polymers are described in more detail in WO 2007/138054, WO 2006/108856 and WO 2006/113314 (hereby incorporated by reference).
  • the detergent compositions of the present invention may also include one or more antiredeposition agents such as carboxymethylcellulose (CMC), polyvinyl alcohol (PVA), polyoxyethylene and/or polyethyleneglycol (PEG), homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid.
  • CMC carboxymethylcellulose
  • PVA polyvinyl alcohol
  • PEG polyethyleneglycol
  • homopolymers of acrylic acid copolymers of acrylic acid and maleic acid.
  • the cellulose based polymers described under soil release polymers above may also function as anti-redeposition agents.
  • the detergent compositions of the present invention may also include one or more rheology modifiers, structurants or thickeners, as distinct from viscosity reducing agents.
  • the rheology modifiers are selected from the group consisting of non-polymeric crystalline, hydroxy-functional materials, polymeric rheology modifiers which impart shear thinning characteristics to the aqueous liquid matrix of a liquid detergent composition.
  • the rheology and viscosity of the detergent can be modified and adjusted by methods known in the art, for example as shown in EP 2169040.
  • adjunct materials include, but are not limited to, anti-shrink agents, anti-wrinkling agents, bactericides, binders, carriers, dyes, enzyme stabilizers, fabric softeners, fillers, foam regulators, hydrotropes, perfumes, pigments, sod suppressors, solvents, and structurants for liquid detergents and/or structure elasticizing agents.
  • the detergent additive as well as the detergent composition may comprise one or more [additional] enzymes such as a protease, a lipase, a cutinase, a cellulase, an amylase, carbohydrase, DNase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • additional enzymes such as a protease, a lipase, a cutinase, a cellulase, an amylase, carbohydrase, DNase, pectinase, mannanase, arabinase, galactanase, xylanase, oxidase, e.g., a laccase, and/or peroxidase.
  • the properties of the selected enzyme(s) should be compatible with the selected detergent, (/.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc.), and the enzyme(s) should be present in effective amounts.
  • cellulase means one or more (e.g., several) enzymes that hydrolyze a cellulosic material.
  • polypeptide having cellulase activity and cellulase are used interchangeably.
  • Cellulases may be selected from the group consisting of cellulases belonging to GH5, GH44, GH45, EC 3.2.1.4, EC 3.2.1.21 , EC 3.2.1.91 and EC 3.2.1.172.
  • Such enzymes include endoglucanase(s) (e.g. EC 3.2.1.4), cellobiohydrolase(s), beta-glucosidase(s), or combinations thereof.
  • Suitable cellulases include mono-component and mixtures of enzymes of bacterial or fungal origin. Chemically modified or protein engineered mutants are also contemplated.
  • the cellulase may for example be a mono-component or a mixture of mono-component endo-1 ,4-beta-glucanase also referred to as endoglucanase.
  • DNase means a polypeptide with DNase activity that catalyzes the hydrolytic cleavage of phosphodiester linkages in the DNA backbone, thus degrading DNA.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mutants are included.
  • the mannanase may be an alkaline mannanase of Family 5 or 26. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B. halodurans, B. clausii, or H. insolens.
  • Suitable mannanases are described in WO 1999/064619. A commercially available mannanase is Mannaway (Novozymes A/S).
  • Suitable proteases may be of any origin, but are preferably of bacterial or fungal origin, optionally in the form of protein engineered or chemically modified mutants.
  • the protease may be an alkaline protease, such as a serine protease ora metalloprotease.
  • a serine protease may for example be of the S1 family, such as trypsin, or the S8 family such as a subtilisin.
  • a metalloprotease may for example be a thermolysin, e.g. from the M4 family, or another metalloprotease such as those from the M5, M7 or M8 families.
  • subtilases refers to a sub-group of serine proteases according to Siezen et al., Protein Eng. 4 (1991) 719-737 and Siezen et al., Protein Sci. 6 (1997) 501-523.
  • Serine proteases are a subgroup of proteases characterized by having a serine in the active site, which forms a covalent adduct with the substrate.
  • the subtilases may be divided into six subdivisions, the Subtilisin family, the Thermitase family, the Proteinase K family, the Lantibiotic peptidase family, the Kexin family and the Pyrolysin family.
  • proteases suitable for detergent use may be obtained from a variety of organisms, including fungi such as Aspergillus
  • detergent proteases have generally been obtained from bacteria and in particular fromSac/7/t/s.
  • Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alkalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii.
  • Particular subtilisins include subtilisin lentus, subtilisin Novo, subtilisin Carlsberg, subtilisin BPN’, subtilisin 309, subtilisin 147 and subtilisin 168 and e.g. protease PD138 (described in WO 93/18140).
  • Other useful proteases are e.g. those described in WO 01/16285 and WO 02/16547.
  • trypsin-like proteases examples include the Fusarium protease described in WO 94/25583 and WO 2005/040372, and the chymotrypsin proteases derived from Cellumonas described in WO 2005/052161 and WO 2005/052146.
  • metalloproteases include the neutral metalloproteases described in WO 2007/044993 such as those derived from Bacillus amyloliquefaciens, as well as e.g. the metalloproteases described in WO 2015/158723 and WO 2016/075078.
  • proteases examples include the protease variants described in WO 89/06279 WO 92/19729, WO 96/34946, WO 98/20115, WO 98/20116, WO 99/11768, WO 01/44452, WO 03/006602, WO 2004/003186, WO 2004/041979, WO 2007/006305, WO 2011/036263, WO 2014/207227, WO 2016/087617 and WO 2016/174234.
  • Suitable commercially available protease enzymes include those sold under the trade names Alcalase®, DuralaseTM, DurazymTM, Relase®, Relase® Ultra, Savinase®, Savinase® Ultra, PrimaseTM, Polarzyme®, Kannase®, Liquanase®, Liquanase® Ultra, Ovozyme®, Coronase®, Coronase® Ultra, Blaze®, Blaze Evity® 100T, Blaze Evity® 125T, Blaze Evity® 150T, Blaze Evity® 200T, Neutrase®, Everlase®, Esperase®, Progress® Uno, Progress® In and Progress® Excel (Novozymes A/S), those sold under the tradename MaxataseTM, MaxacaiTM, Maxapem®, Purafect® Ox, Purafect® OxP, Puramax®, FN2TM, FN3TM, FN4 ex TM, Excellase®, ExcellenzTM P
  • Suitable lipases and cutinases include those of bacterial or fungal origin. Chemically modified or protein engineered mutant enzymes are included. Examples include lipase from Thermomyces, e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216, cutinase from Humicola, e.g. H. insolens (WO96/13580), lipase from strains of Pseudomonas (some of these now renamed to Burkholderia), e.g. P. alcaligenes or P. pseudoalcaligenes (EP218272), P. cepacia (EP331376), P. sp.
  • Thermomyces e.g. from T. lanuginosus (previously named Humicola lanuginosa) as described in EP258068 and EP305216
  • cutinase from Humicola e.g. H
  • strain SD705 (W095/06720 & W096/27002), P. wisconsinensis (WO96/12012), GDSL-type Streptomyces lipases (W010/065455), cutinase from Magnaporthe grisea (WO10/107560), cutinase from Pseudomonas mendocina (US5,389,536), lipase from Thermobifida fusca (W011/084412), Geobacillus stearothermophilus lipase (W011/084417), lipase from Bacillus subtilis (W011/084599), and lipase from Streptomyces griseus (WO11/150157) and S. pristinaespiralis (W012/137147).
  • lipase variants such as those described in EP407225, WO92/05249, WO94/01541 , WO94/25578, WO95/14783, WO95/30744, WO95/35381 , WO95/22615,
  • Preferred commercial lipase products include include Lipolase 100T/L, Lipex 100T/L, Lipex 105T, Lipex Evity 100L, Lipex Evity 200L (all Novozymes A/S), Preferenz® L 100 (DuPont).
  • lipases sometimes referred to as acyltransferases or perhydrolases, e.g. acyltransferases with homology to Candida antarctica lipase A (WO10/111143), acyltransferase from Mycobacterium smegmatis (WO05/56782), perhydrolases from the CE 7 family (WO09/67279), and variants of the M. smegmatis perhydrolase in particular the S54V variant used in the commercial product Gentle Power Bleach from Huntsman Textile Effects Pte Ltd (WO10/100028).
  • amylases include an alpha-amylase or a glucoamylase and may be of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g., a special strain of Bacillus licheniformis, described in more detail in GB 1 ,296,839.
  • Suitable amylases include amylases having SEQ ID NO: 2 in WO 95/10603 or variants having 90% sequence identity to SEQ ID NO: 3 thereof. Preferred variants are described in WO 94/02597, WO 94/18314, WO 97/43424 and SEQ ID NO: 4 of WO 99/019467, such as variants with substitutions in one or more of the following positions: 15, 23, 105, 106, 124, 128, 133, 154, 156, 178, 179, 181 , 188, 190, 197, 201 , 202, 207, 208, 209, 211 , 243, 264, 304, 305, 391 , 408, and 444.
  • amylases having SEQ ID NO: 6 in WO 02/010355 or variants thereof having 90% sequence identity to SEQ ID NO: 6.
  • Preferred variants of SEQ ID NO: 6 are those having a deletion in positions 181 and 182 and a substitution in position 193.
  • amylases which are suitable are hybrid alpha-amylase comprising residues 1-33 of the alpha-amylase derived from B. amyloliquefaciens shown in SEQ ID NO: 6 of WO 2006/066594 and residues 36-483 of the B. licheniformis alpha-amylase shown in SEQ ID NO: 4 of WO 2006/066594 or variants having 90% sequence identity thereof.
  • amylase variants such as those described in WO2011/098531 , WO2013/001078 and WO2013/001087.
  • amylases are DuramylTM, TermamylTM, FungamylTM, Stainzyme TM , Stainzyme PlusTM, NatalaseTM, Liquozyme X and BANTM Amplify; Amplify Prime; (from Novozymes A/S), and RapidaseTM , PurastarTM/EffectenzTM, Powerase, Preferenz S1000, Preferenz S100 and Preferenz S110 (from Genencor International Inc./DuPont).
  • Suitable peroxidases/oxidases include those of plant, bacterial or fungal origin. Chemically modified or protein engineered mutants are included. 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, and WO 98/15257. Commercially available peroxidases include GuardzymeTM (Novozymes A/S).
  • a suitable peroxidase is preferably a peroxidase enzyme comprised by the enzyme classification EC 1.11.1.7, as set out by the Nomenclature Committee of the International Union of Biochemistry and Molecular Biology (IUBMB), or any fragment derived therefrom, exhibiting peroxidase activity.
  • IUBMB Nomenclature Committee of the International Union of Biochemistry and Molecular Biology
  • Suitable peroxidases also include a haloperoxidase enzyme, such as chloroperoxidase, bromoperoxidase and compounds exhibiting chloroperoxidase or bromoperoxidase activity.
  • Haloperoxidases are classified according to their specificity for halide ions. Chloroperoxidases (E.C. 1.11.1.10) catalyze formation of hypochlorite from chloride ions.
  • the haloperoxidase may be a chloroperoxidase.
  • the haloperoxidase is a vanadium haloperoxidase, i.e., a vanadate- containing haloperoxidase. In a preferred method 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 Caldariomyces, e.g., C. fumago, Alternaria, Curvularia, e.g., C. verruculosa and C. inaequalis, Drechslera, Ulocladium and Botrytis.
  • Caldariomyces e.g., C. fumago
  • Alternaria Curvularia
  • Curvularia e.g., C. verruculosa and C. inaequalis
  • Drechslera Ulocladium and Botrytis.
  • Haloperoxidases have also been isolated from bacteria such as Pseudomonas, e.g., P. pyrrocinia and Streptomyces, e.g., S. aureofaciens.
  • the haloperoxidase may be derivable from Curvularia sp., in particular Curvularia verruculosa or Curvularia inaequalis, such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculosa CBS 444.70 as described in WO 97/04102; or from Drechslera hartlebii as described in WO 01/79459, Dendryphiella salina as described in WO 01/79458, Phaeotrichoconis crotalarie as described in WO 01/79461 , or Geniculosporium sp. as described in WO 01/79460.
  • Curvularia verruculosa or Curvularia inaequalis such as C. inaequalis CBS 102.42 as described in WO 95/27046; or C. verruculosa CBS 147.63 or C. verruculo
  • Suitable oxidases 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).
  • 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, Pomes, Lentinus, Pleurotus, Trametes, e.g., T. villosa and T. versicolor, Rhizoctonia, e.g., R. solani, Coprinopsis, e.g., C. cinerea, C. comatus, C. friesii, and C. plicatilis, Psathyrella, e.g., P. condelleana, Panaeolus, e.g., P.
  • papilionaceus Myceliophthora, e.g., M. thermophila, Schytalidium, e.g., S. thermophilum, Polyporus, e.g., P. pinsitus, Phlebia, e.g., P. radiata (WO 92/01046), or Coriolus, e.g., C. hirsutus (JP 2238885).
  • Suitable examples from bacteria include a laccase derivable from a strain of Bacillus.
  • a laccase derived from Coprinopsis or Myceliophthora is preferred; in particular a laccase derived from Coprinopsis cinerea, as disclosed in WO 97/08325; or from Myceliophthora thermophila, as disclosed in WO 95/33836.
  • Licheninases or lichenases (e.g. EC 3.2.1.73) hydrolyse (1 ,4)-beta-D-glucosidic linkages in beta-D-glucans containing (1 ,3)- and (1 ,4)-bonds and can act on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1 ,3- or 1 ,4-bonds.
  • Pectate lyases catalyze the cleavage of a-1 ,4-D-galacturonan (i.e., homogalacturonan or polygalacturonic acid) by an eliminative pathway leaving a double bond between C4 and C5 at the +1 subsite and a reducing sugar at the -1 subsite. Pectate lyases may also have pectin lyase activity.
  • the detergent composition of the invention may be in any convenient form, e.g., a bar, a homogenous tablet, a tablet having two or more layers, a pouch having one or more compartments, a regular or compact powder, a granule, a paste, a gel, or a regular, compact or concentrated liquid.
  • Pouches can be configured as single or multicompartments. It can be of any form, shape and material which is suitable for hold the composition, e.g. without allowing the release of the composition to release of the composition from the pouch prior to water contact.
  • the pouch is made from water soluble film which encloses an inner volume. Said inner volume can be divided into compartments of the pouch.
  • Preferred films are polymeric materials preferably polymers which are formed into a film or sheet.
  • Preferred polymers, copolymers or derivates thereof are selected polyacrylates, and water- soluble acrylate copolymers, methyl cellulose, carboxy methyl cellulose, sodium dextrin, ethyl cellulose, hydroxyethyl cellulose, hydroxypropyl methyl cellulose, malto dextrin, poly methacrylates, most preferably polyvinyl alcohol copolymers and, hydroxypropyl methyl cellulose (HPMC).
  • the level of polymer in the film for example PVA is at least about 60%.
  • Preferred average molecular weight will typically be about 20,000 to about 150,000.
  • Films can also be of blended compositions comprising hydrolytically degradable and water soluble polymer blends such as polylactide and polyvinyl alcohol (known under the Trade reference M8630 as sold by MonoSol LLC, Indiana, USA) plus plasticisers like glycerol, ethylene glycerol, propylene glycol, sorbitol and mixtures thereof.
  • the pouches can comprise a solid laundry cleaning composition or part components and/or a liquid cleaning composition or part components separated by the water-soluble film.
  • the compartment for liquid components can be different in composition than compartments containing solids: US2009/0011970 A1.
  • Detergent ingredients can be separated physically from each other by compartments in water dissolvable pouches or in different layers of tablets. Thereby negative storage interaction between components can be avoided. Different dissolution profiles of each of the compartments can also give rise to delayed dissolution of selected components in the wash solution.
  • a liquid or gel detergent which is not unit dosed, may be aqueous, typically containing at least 20% by weight and up to 95% water, such as up to about 70% water, up to about 65% water, up to about 55% water, up to about 45% water, up to about 35% water.
  • Other types of liquids including without limitation, alkanols, amines, diols, ethers and polyols may be included in an aqueous liquid or gel.
  • An aqueous liquid or gel detergent may contain from 0-30% organic solvent.
  • a liquid or gel detergent may be non-aqueous.
  • the GCL 1 of the invention may be added to laundry soap bars and used for hand washing laundry, fabrics and/or textiles.
  • laundry soap bar includes laundry bars, soap bars, combo bars, syndet bars and detergent bars.
  • the types of bar usually differ in the type of surfactant they contain, and the term laundry soap bar includes those containing soaps from fatty acids and/or synthetic soaps.
  • the laundry soap bar has a physical form which is solid and not a liquid, gel or a powder at room temperature.
  • the term solid is defined as a physical form which does not significantly change over time, i.e. if a solid object (e.g. laundry soap bar) is placed inside a container, the solid object does not change to fill the container it is placed in.
  • the bar is a solid typically in bar form but can be in other solid shapes such as round or oval.
  • the laundry soap bar may contain one or more additional enzymes, protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or hemiacetal adduct), boric acid, borate, borax and/or phenylboronic acid derivatives such as 4-formylphenylboronic acid, one or more soaps or synthetic surfactants, polyols such as glycerine, pH controlling compounds such as fatty acids, citric acid, acetic acid and/or formic acid, and/or a salt of a monovalent cation and an organic anion wherein the monovalent cation may be for example Na + , K + or NH 4 + and the organic anion may be for example formate, acetate, citrate or lactate such that the salt of a monovalent cation and an organic anion may be, for example, sodium formate.
  • protease inhibitors such as peptide aldehydes (or hydrosulfite adduct or hem
  • the laundry soap bar may also contain complexing agents like EDTA and HEDP, perfumes and/or different type of fillers, surfactants e.g. anionic synthetic surfactants, builders, polymeric soil release agents, detergent chelators, stabilizing agents, fillers, dyes, colorants, dye transfer inhibitors, alkoxylated polycarbonates, suds suppressers, structurants, binders, leaching agents, bleaching activators, clay soil removal agents, anti-redeposition agents, polymeric dispersing agents, brighteners, fabric softeners, perfumes and/or other compounds known in the art.
  • the laundry soap bar may be processed in conventional laundry soap bar making equipment such as, but not limited to, mixers, plodders, e.g. a two-stage vacuum plodder, extruders, cutters, logostampers, cooling tunnels and wrappers.
  • the invention is not limited to preparing the laundry soap bars by any single method.
  • the premix of the invention may be added to the soap at different stages of the process.
  • the premix containing a soap, GCL 1 , optionally one or more additional enzymes, a protease inhibitor, and a salt of a monovalent cation and an organic anion may be prepared, and the mixture is then plodded.
  • the GCL 1 and optional additional enzymes may be added at the same time as the protease inhibitor for example in liquid form.
  • the process may further comprise the steps of milling, extruding, cutting, stamping, cooling and/or wrapping.
  • a detergent composition comprising
  • E(2) The detergent composition according to E(1)1 , wherein the first lipase has at least 70% identity to SEQ ID NO: 1 , such as at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95%, 96%, 97%, 98% or 99% identity to SEQ ID NO: 1.
  • E(3) The detergent composition according to E(1)2, wherein the second lipase has at least 70% identity to SEQ ID NO: 3, such as at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95% identity to SEQ ID NO: 3.
  • E(4) The detergent composition according to E(1)2, wherein the second lipase has at least 80% identity such as at least 80%, 85%, 90%, 91 %, 92%, 93%, 94%, 95% identity to any of SEQ ID NO: 4 or SEQ ID NO: 5
  • E(6) A method for removal of lipid in a textile during a wash cycle comprising contacting the textile with the detergent composition of any of E(1) to E(5).
  • a washing method for textile comprising:
  • E(8) The washing method according to E(7), wherein the temperature of the wash liquor is in the range of 5°C to 90°C, or in the range of 10°C to 80°C, or in the range of 10°C to 70°C, or in the range of 10°C to 60°C, or in the range of 10°C to 50°C, or in the range of 15°C to 40°C, or in the range of 20°C to 30°C.
  • the detergent composition, method and washing method according to any of the previous embodiments further comprising one or more enzymes selected from the group consisting of proteases, amylases, deoxyribonucleases, xyloglucanases, pectinases, pectin lyases, xanthan lyases, xanthan endoglucanases, peroxidases, haloperoxygenases, cellulases, licheninase, lipases, cutinases, catalases, oxidase, arabinose, galactanase and mannanases.
  • one or more enzymes selected from the group consisting of proteases, amylases, deoxyribonucleases, xyloglucanases, pectinases, pectin lyases, xanthan lyases, xanthan endoglucanases, peroxidases, haloperoxygenases, cellulases,
  • E(12) The detergent composition according to any of E(1) to E(5), wherein the amount of first lipase having at least 60% sequence identity to SEQ ID NO: 1 in the detergent composition is from 0.1 mg AEP/g detergent composition to 50 mg AEP/g detergent composition, such as 0.1 mg AEP/g detergent composition to 40 mg AEP/g detergent composition, such as 0.1 mg AEP/g detergent composition to 30 mg AEP/g detergent composition, such as 0.1 mg AEP/g detergent composition to 20 mg AEP/g detergent composition, such as 0.1 mg AEP/g detergent composition to 10 mg AEP/g detergent composition, such as 0.2 mg AEP/g detergent composition to 50 mg AEP/g detergent composition, such as 0.2 mg AEP/g detergent composition to 40 mg AEP/g detergent composition, such as 0.2 mg AEP/g detergent composition to 30 mg AEP/g detergent composition, such as 0.2 mg AEP/g detergent composition to 20 mg AEP/g detergent composition, such as 0.2 mg AEP/g detergent composition to 10 mg AEP/g detergent composition.
  • E(13) The detergent composition according to any of E(1) to E(5) comprising 0.05-20 wt% rhamnolipid, such as 1-15 wt% rhamnolipid, such as 2-10 wt% rhamnolipid, such as 3-9 wt% rhamnolipid, such as 4-8 wt% rhamnolipid.
  • Example A pNP assay for determination of lipase activity
  • the substrate pNP-substrate is hydrolyzed by the lipolytic enzyme under standard conditions.
  • pNP- valerate is used as an example of a saturated short chain fatty acid.
  • Valeric acid as the acyl group may be replaced by a long chain fatty acid such as oleic acid.
  • the absorbance of the solution measured at 405 nm is a function of the activity of the lipolytic enzyme.
  • the ratio between lipase activity on unsaturated substrates having long fatty acyl chains (e.g. oleic acid) to short acyl chain (e.g. p-nitrophenyl butyrate and/or p- nitrophenyl valerate) can be determined.
  • Variation of substrate may call for adjustment of e.g. buffer system, adjustments that are easily within the purview of the skilled person.
  • Substrate The relevant pNP substrate (e.g. pNp-Valerate Sigma N-4377) 1 mM in Buffer prepared from stock-solution 100 mM in Methanol
  • Buffer 50 mM TRIS, 0,4% Triton X-100, is prepared to pH 7,7
  • Microtiter plates (Thermo Scientific 269620 96F without lid microwell plate) for plate reader spectrophotometers (Molecular Devices Spectramax 190) can conveniently be used for determination of lipase activity by standard methods based on use of paranitrophenol-esters.
  • Example B Active site titration of lipase variants
  • Active site titration can be used to determine the concentration of active enzyme protein (AEP) in a given sample. Active site titration for TLL-like lipases as well as for GCL 1 -like lipases is provided below.
  • AEP active enzyme protein
  • Concentrations of micropurified and conventionally purified lipase variants are determined by burst active site titration. 100 pl lipase (diluted in 0.01 % Triton X-100 if necessary to get concentration below 5 pM) is mixed with 100 pl approximately 40 pM ethyl resorufinyl heptylphosphonate inhibitor dissolved in 1 M Tris, 4 mM SDS, pH 9.0 in the well of a black microtiter plate.
  • F FO + Burst * (1-exp(-(t + dt) * ln(2) I T 1 / 2 ) + Slope * (t + dt)
  • F the measured fluorescence
  • FO the fluorescence background from inhibitor and lipase
  • t the time since first fluorescence measurement
  • dt the time from mixing of lipase with inhibitor to the first fluorescence measurement
  • Burst the fluorescence burst
  • T 1 Z> is the half-time for the exponential burst
  • Slope is the slope for the linear change in fluorescence e.g.
  • the active lipase concentration is determined by using a resorufin standard curve (0-4 pM) included on the microtiter plate.
  • Concentrations of micro-purified and conventionally purified lipase variants are determined by burst active site titration.
  • 100 pl lipase diluted in 0.01 % Triton X-100 to 0.1 mg/mL (or 50 pl lipase diluted in 0.01% Triton X-100 to 0.1 mg/mL + 0.05 mL 0.01 % Triton X-100) is mixed with 100 pl ethyl resorufinyl heptylphosphonate inhibitor dissolved in DSMA (3.8 mg/mL) further diluted with buffer (1 M Tris, 4 mM SDS, pH 7.0) to 0.016 mg/mL in the well of a black microtiter plate.
  • F F0 + Burst * (1-exp(-(t + dt) * ln(2) I T 1 / 2 ) + Slope * (t + dt)
  • F the measured fluorescence
  • F0 the fluorescence background from inhibitor and lipase
  • t the time since first fluorescence measurement
  • dt the time from mixing of lipase with inhibitor to the first fluorescence measurement
  • Burst is the fluorescence burst
  • T 1 Z> is the half-time for the exponential burst
  • Slope is the slope for the linear change in fluorescence e.g. due to hydrolysis of lipase-ethyl heptylphosphonate complex and/or bleaching of resorufin. From the calculated burst the active lipase concentration is determined using a resorufin standard curve (0-4 pM) included on the microtiter plate.
  • the Terg-O-tometer is a medium scale model wash system that can be applied to test 16 different wash conditions simultaneously.
  • a TOM is basically a large temperature-controlled water bath with up to 16 open metal beakers (1000 mL) submerged into it. Each beaker constitutes one small top loader style washing machine and during an experiment, each of them will contain a solution of a specific detergent/enzyme system and the soiled and unsoiled fabrics its performance is tested on. Mechanical stress is achieved by a rotating stirring arm, which stirs the liquid within each beaker.
  • the TOM model wash system is mainly used in medium scale testing of detergents and enzymes at US or Latin America/Asian Pacific (LA/AP) wash conditions.
  • the TOM provides the link between small scale experiments, such as AMSA and mini-wash, and the more time-consuming full-scale experiments in top loader washing machines.
  • Example 1 Terg-O-tometer (TOM) wash, 2.8 ppm SEQ ID NO: 1 and 0.1 ppm SEQ ID NO: 4
  • Water hardness was adjusted to the strength described below by addition of CaCI 2 , MgCI 2 and NAHCO 3 . Wash solutions were prepared with desired amount of detergent, temperature and water hardness in a bucket as described below. Detergent was dissolved during magnet stirring for 10 min. (Wash solution was used within 30 to 60 min after preparation).
  • Temperature and rotation (rpm) in the water bath in the Terg-O-Tometer were set according to the settings below.
  • temperature was adjusted according to settings (+/- 1 °C) wash solution was added to TOM beaker according to the amount described below.
  • Agitation in the beaker was at 120 rpm.
  • 2 homemade lard stains and 2 CS-10 butter fat stains from Equest (when odor was measured) were added to each of the beakers and wash carried out according to time stated below with 2 replicas of each stain type in each beaker.
  • the swatches were rinsed in cold tap water for 10 minutes and dried in the dark overnight.
  • Lard stains were weighted on an analytical scale (348-AV-50).
  • CS-10 butter fat stains were cut out in 2 cm in diameter and used for odor measurements.
  • Example 2 Terg-O-tometer (TOM) wash, 0.4 ppm SEQ ID NO: 1 and 0.1 ppm SEQ ID NO: 4
  • Example 3 Terg-O-tometer (TOM) wash, 2.8 ppm SEQ ID NO: 1 and SEQ ID NO: 5
  • the butyric acid release (odor) from the lipase washed swatches can measured by Solid Phase Micro Extraction Gas Chromatography (SPME-GC) using the following method.
  • the cotton textile is washed as specified above and after wash, excess water is removed from the textile using filter paper and the textile is thereafter dried at 25°C for 2 h.
  • Each SPME-GC measurement is performed with four pieces of the washed and dried textile (5 mm in diameter), which are transferred to a Gas Chromatograph (GC) vial and the vial is closed.
  • GC Gas Chromatograph
  • the samples are incubated at 30°C for 24 hours and subsequently heated to 140°C for 30 minutes and stored at 20°C-25°C for at least 4 hours before analysis.
  • FID Flame Ionization Detector
  • culture supernatants were purified by gel filtration Sephadex G-25 and anion exchange Q-sepharose Fast Flow. Purification of culture supernatants was performed as follows: The culture broth is filtered through a Nalgene 0.2 pm filtration unit to remove the host cells. The filtrated supernatant is applied to a 1000mL Sephadex G-25 column (Cytiva) equilibrated in 50mM Hepes, pH 7.6. The enzyme was eluted from the column using 50mM Hepes, pH 7.6, fractions are collected.
  • the pool of the fractions was applied to a 50mL Q-sepharose Fast Flow column (Cytiva) equilibrated in 50mM Hepes, pH 7.6. After washing the column with the equilibration buffer, the GCL-1 was eluted with a linear NaCI gradient (0-1 M NaCI) using a 50mM Hepes, 1 M NaCI, pH 7.6 buffer over five column volumes. Fractions were analyzed by SDS-PAGE and fractions in which only one band is observed on the Coomassie stained SDS-PAGE gel are pooled as the purified enzyme preparation and used for further experiments.
  • GCL1 samples having SEQ ID NO:4 and SEQ ID NO:5 were purified with an additional step using Size exclusion as they had been kept cold (refrigerator). From earlier studies some aggregation of GCL 1 after cold storage has been observed, thus it was decided to use size exclusion to remove/avoid aggregation for GCL1 samples.
  • the size exclusion was done by use of Sephadex G25 PD-10 column and the following gravity protocol:

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Abstract

La présente invention concerne une composition détergente comprenant une première lipase et une seconde lipase, les lipases ayant un effet synergique sur l'élimination de graisse. Dans un autre aspect, la présente invention concerne l'utilisation de la composition détergente de l'invention pour le nettoyage d'un textile.
PCT/EP2024/067046 2023-06-28 2024-06-19 Composition détergente comprenant des lipases WO2025002934A1 (fr)

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