WO2024061317A1 - Utilisation d'une enzyme pour remplacer un agent de maintien de la blancheur dans une composition de nettoyage - Google Patents

Utilisation d'une enzyme pour remplacer un agent de maintien de la blancheur dans une composition de nettoyage Download PDF

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Publication number
WO2024061317A1
WO2024061317A1 PCT/CN2023/120395 CN2023120395W WO2024061317A1 WO 2024061317 A1 WO2024061317 A1 WO 2024061317A1 CN 2023120395 W CN2023120395 W CN 2023120395W WO 2024061317 A1 WO2024061317 A1 WO 2024061317A1
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seq
protease
variant
enzyme
polypeptide
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PCT/CN2023/120395
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English (en)
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Chaoyang YU
Iasminy Da Silva BRASIL
Mirko IUBATTI
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Novozymes A/S
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Publication of WO2024061317A1 publication Critical patent/WO2024061317A1/fr

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    • 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
    • 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

Definitions

  • This invention relates to use of an enzyme for replacement of a whiteness/color maintaining component (e.g., an optical brightener) in a cleaning composition, wherein the enzyme is selected from the group consisting of a protease, a mannanase, a cellulase and combinations thereof.
  • a whiteness/color maintaining component e.g., an optical brightener
  • the present inventor has surprisingly found that some enzymes can substitute significant amounts of the whiteness/color maintaining agent (e.g., optical brighteners and/or anti-redeposition polymers) of a detergent composition without impairing the overall whiteness/color maintenance performance.
  • the whiteness/color maintaining agent e.g., optical brighteners and/or anti-redeposition polymers
  • the inventor has found that the whiteness/color of the treated textiles may even be improved by this substitution.
  • the invention concerns use of an enzyme for replacement of a whiteness-maintaining agent in a cleaning composition, wherein the enzyme is selected from the group consisting of a protease, a mannanase, a cellulase and combinations thereof, preferably the enzyme is a combination of two or three enzymes selected from a protease, a mannanase and a cellulase.
  • the present invention relates to a cleaning composition free of at least one whiteness-maintaining agent, wherein the composition comprises an enzyme selected from the group consisting of a protease, a mannanase, a cellulase and combinations thereof, wherein the whiteness-maintaining agent is selected from the group consisting of an optical brightener, an anti-redeposition polymer and mixture thereof.
  • the cleaning composition provided by the present invention has improved sustainability profile because at least one whiteness-maintaining agent can be replaced by eco-friendly enzymes while keeping or even improving the key performance (e.g., whiteness/color-maintaining effect) of the composition.
  • the invention relates to a method for maintaining or improving the whiteness and/or color of a textile, comprising: (a) exposing said textile to a wash liquor comprising the detergent composition of the invention; and optionally (b) rinsing the textile.
  • cleaning components is defined herein to mean the types of chemicals which can be used in cleaning compositions.
  • cleaning components are alkalis, surfactants, solvents, hydrotropes, builders, co-builders, chelators or chelating agents, bleaching system or bleach components, polymers, foam boosters, suds suppressors, dispersants, dye transfer inhibitors, perfume, bactericides, fungicides, corrosion inhibitors, soil suspending agents, soil release polymers, whiteness/color-maintaining agents such as optical brighteners and anti-redeposition agents, enzyme inhibitors or stabilizers, enzyme activators, antioxidants, preservatives, solvents and solubilizers.
  • Whiteness/color-maintaining agents refers to additives used in a detergent that can help maintain the original whiteness/color of the fabric or prevent/delay the loss of whiteness/color, via e.g., preventing soil (e.g., soluble soil, and insoluble soil such as clay particles and tiny fibers) from resettling on a fabric after it has been removed during washing, or by disguising/masking the loss of whiteness/color so as to make a textile appear whiter and brighter. These agents typically include but not limited to optical brighteners and anti-redeposition agents as set forth below.
  • the term “whiteness/color-maintaining agents” may be used interchangeably with the term “whiteness-maintaining agents” .
  • optical brighteners as used herein is used interchangeably with the terms optical brightening agents, fluorescent brightening agents or fluorescent whitening agents. These additives are often used to enhance the appearance of color and/or brightness of a material such as a textile and paper, making materials look less yellow/less dingy, and thus to maintain the original whiteness and color of a material for a longer period of time.
  • Anti-redeposition agents refers to additives used in a detergent to help prevent soil from resettling on a fabric after it has been removed during washing.
  • Suitable anti-redeposition agents may include but are not limited to anti-redeposition polymers such as polyacrylic acid, a modified polyacrylic acid polymer, a modified polyacrylic acid copolymer, a maleic acid-acrylic acid copolymer, carboxymethylcellulose (CMC) , cellulose gum, methyl cellulose, polyvinyl alcohol (PVA) , polyvinylpyrrolidone (PVP) , polyoxyethylene and/or polyethyleneglycol (PEG) , homopolymers of acrylic acid, copolymers of acrylic acid and maleic acid, ethoxylated polyethyleneimines, and/or combinations thereof.
  • the cellulose-based polymers described under soil release polymers below may also function as anti-redeposition agents.
  • Cleaning composition refers to compositions that find use in the removal of undesired compounds from items to be cleaned.
  • the cleaning composition may be used to e.g., for 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, or spray compositions) .
  • the cleaning composition of the present invention may contain one or more additional enzymes (such as lipases, amylases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, malanases, ⁇ -glucanases, arabinosidases, hyaluronidase, laccase, deoxyribonucleases (DNases) , hexosaminidases, and any mixture thereof) , and/or one or more cleaning components as described above.
  • additional enzymes such as lipases, amylases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxida
  • 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.
  • a host cell may produce a mixture of two of more different mature polypeptides (i.e., with a different C-terminal and/or N-terminal amino acid) expressed by the same polynucleotide. It is also known in the art that different host cells process polypeptides differently, and thus, one host cell expressing a polynucleotide may produce a different mature polypeptide (e.g., having a different C-terminal and/or N-terminal amino acid) as compared to another host cell expressing the same polynucleotide.
  • Sequence identity The relatedness between two amino acid sequences or between two nucleotide sequences is described by the parameter “sequence identity” .
  • the sequence identity between two amino acid sequences is determined as the output of “longest identity” 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 6.6.0 or later.
  • the parameters used are a gap open penalty of 10, a gap extension penalty of 0.5, and the EBLOSUM62 (EMBOSS version of BLOSUM62) substitution matrix.
  • the nobrief option must be specified in the command line.
  • the output of Needle labeled “longest identity” is calculated as follows:
  • variant means a polypeptide/enzyme having the same type of activity as the parent enzyme and comprising an alteration, i.e., a substitution, insertion, and/or deletion, at one or more positions compared to the amino acid sequence of the parent.
  • 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.
  • a variant may e.g. be a variant of an identified protease that has the enzymatic activity of the parent.
  • 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 “T226A” .
  • Multiple mutations may be separated by addition marks ( “+” ) , e.g., “G205R + S411 F” , or by a comma, e.g., “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 “G195GK” .
  • An indication of an insertion at a particular position is understood as being an insertion after the original amino acid residue.
  • an “insertion at position 195” is understood to be an insertion after the original residue in position 195.
  • Variants comprising multiple alterations are separated by addition marks ( “+” ) or commas, e.g., “R170Y+G195E” or “R170Y, G195E” representing a substitution of arginine and glycine at positions 170 and 195 with tyrosine and glutamic acid, respectively.
  • R170Y, E represents a substitution of arginine at position 170 with tyrosine or glutamic acid.
  • Y167G, A+ R170G, A designates the following variants: “Y167G+R170G” , “Y167G+R170A” , “Y167A+R170G” , and “Y167A+R170A” .
  • 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 towelling.
  • the textile may be cellulose based such as natural cellulosics, including 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, rabit and silk or synthetic polymer such as nylon, aramid, polyester, acrylic, polypropylen and spandex/elastane, or blends thereof as well as blend of cellulose based and non-cellulose based fibers.
  • non-cellulose based such as natural polyamides including wool, camel, cashmere, mohair, rabit and silk or synthetic polymer such as nylon, aramid, polyester, acrylic, polypropylen and spandex/elastane, or blends thereof as well as blend 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 fibers (e.g.
  • Fabric may be conventional washable laundry, for example, stained household laundry. When the term fabric or garment is used it is intended to include the broader term textiles as well.
  • Whiteness/color-maintaining performance The term is defined herein as a broad term with different meanings in different regions and for different consumers. Loss of whiteness/color of a fabric can e.g., be due to greying, yellowing, or removal of optical brighteners/hueing agents. Greying and yellowing can be due to soil redeposition, body soils, colouring or dye transfer.
  • the term “whiteness/color-maintaining performance” may be used interchangeably with the term “Whiteness-maintaining effect” or “whiteness performance” .
  • the whiteness/color maintaining performance can be measured as ⁇ R460 value as described in the Example section.
  • Figure 1 shows the pictures of the washed CN-42 cotton textile by detergent (with or without whiteness-maintaining agent) in the presence or absence of the enzymes of the present invention, wherein,
  • the inventor has found that the reduction in the obtained R460-value of textiles treated with a detergent composition free of whiteness/color-maintaining agents (e.g., optical brighter/anti-redeposition polymers) may be fully compensated by addition of enzyme (s) of the invention.
  • a detergent composition free of whiteness/color-maintaining agents e.g., optical brighter/anti-redeposition polymers
  • one aspect of the present invention concerns use of an enzyme for replacement of a whiteness/color-maintaining agent in a cleaning composition, wherein the enzyme is selected from the group consisting of a protease, a mannanase, a cellulase and combinations thereof.
  • the amount of a whiteness/color-maintaining agent can be reduced by at least 20%, e.g., by at least 30%, by at least 40%, by at least 50%or even 100%.
  • the amount of optical brightener is reduced by at least 30%, by at least 40%, by at least 50%, by at least 60%, by at least 70%, by at least 75%, by at least 80%or by at least 90%.
  • the amount of anti-redeposition polymer is reduced by at least 30%, by at least 40%, by at least 50%, by at least 60%, by at least 70%, by at least 75%, by at least 80%or by at least 90%.
  • both the optical brightener and the anti-redeposition polymer in a detergent composition are fully replaced by said enzyme (s) .
  • Another aspect of the invention concerns a method for maintaining and/or improving the whiteness/color of a textile, wherein the textile is exposed to a wash liquid with a detergent comprising an enzyme selected from the group consisting of a protease, a mannanase, a cellulase and combinations thereof.
  • said enzyme is a combination of a protease and a mannanase.
  • said enzyme is a combination of a protease and a cellulase.
  • said enzyme is a combination of a protease, a mannanase and a cellulase.
  • Suitable amount of the enzyme (s) of the present invention may be present in the range of 0.0001 wt%to 3 wt%based on the total weight of the cleaning composition, such as in the range of 0.0003 wt%to 2 wt%, 0.005 wt%to 1 wt%, 0.05 wt%to 1.5 wt%or 0.1 wt%to 0.5 wt%, based on the total weight of the cleaning composition.
  • the amount of the enzyme (s) of the invention is in the range of 0.0001 mg to 100 mg enzyme protein per liter of wash liquor, such as 0.01 mg to 50 mg enzyme protein, 0.1 mg to 30 mg enzyme protein, 0.2 mg to 10 mg enzyme protein or 1 mg to 5 mg enzyme protein, per liter of wash liquor.
  • the optical brightener is selected from the group comprising benzenesulfonic acid, 2, 2'- (1, 2-ethenediyl) bis [5- [4- (4-morpholinyl) -6- (phenylamino) -1, 3, 5-triazin-2-yl] amino] -, disodium salt; 2, 2'- ( [1, 1'-biphenyl] -4, 4'-diyldi-2, 1-ethenediyl) bis-, disodium salt; diaminostilbene-sulphonic acid derivative including sodium salts of: 4, 4'-bis- (2-diethanolamino-4-anilino-s-triazin-6-ylamino) stilbene-2, 2'-disulphonate; 4, 4'-bis- (2, 4-dianilino-s-triazin-6-ylamino) stilbene-2.2'-disulphonate; 4, 4'-bis- (2-anilino-4 (N-methyl-benzenesulf
  • the optical brightener is 4.4'-bis- (sulfostyryl) -biphenyl disodium salt or bistriazinyl stilbene derivative.
  • preferred optical brighteners are Tinopal DMS or Tinopal CBS or Tinopal CBS-X available from BASF.
  • Tinopal DMS is the disodium salt of 4, 4'-bis- ( (2-morpholino-4 anilino-s-triazin-6-yl) amino) stilbene disulphonate.
  • Tinopal CBS is the disodium salt of 2, 2'-bis- (phenyl-styryl) disulphonate.
  • Tinopal CBS-X is a 4.4'-bis- (sulfostyryl) -biphenyl disodium salt also known as Disodium Distyrylbiphenyl Disulfonate.
  • Parawhite KX supplied by Paramount Minerals and Chemicals, Mumbai, India.
  • fluorescers suitable for use in the invention include the 1-3-diaryl pyrazolines and the 7-alkylaminocoumarins.
  • the anti-redeposition polymer is selected from the group comprising (carboxymethyl) cellulose (CMC) , poly (vinyl alcohol) (PVA) , poly (vinylpyrrolidone) (PVP) , poly (ethyleneglycol) or poly (ethylene oxide) (PEG) , ethoxylated poly (ethyleneimine) , carboxymethyl inulin (CMI) , and polycarboxylates such as PAA, PAA/PMA, poly-aspartic acid, and lauryl methacrylate/acrylic acid copolymers, hydrophobically modified CMC (HM-CMC) and silicones, copolymers of terephthalic acid and oligomeric glycols, copolymers of poly (ethylene terephthalate) and poly (oxyethene terephthalate) (PET-POET) , PVP, poly (vinylimidazole) (PVI) , poly (vinylpyridine-N-oxid
  • Suitable examples include PVP-K15, PVP-K30, ChromaBond S-400, ChromaBond S-403E and Chromabond S-100 from Ashland Aqualon, and HP 165, HP 50 (Dispersing agent) , HP 53 (Dispersing agent) , HP 59 (Dispersing agent) , HP 56 (dye transfer inhibitor) , HP 66 K (dye transfer inhibitor) from BASF.
  • polymers include sulfonated polycarboxylates, polyethylene oxide and polypropylene oxide (PEO-PPO) and diquaternium ethoxy sulfate, ACUSOL TM 445N Detergent Polymer from DOW, and ethoxylated homopolymer HP 20 from BASF.
  • the detergent composition comprising the enzyme (s) of the invention improves the whiteness of the textile, i.e., the ⁇ R460 value is at least 1.0, e.g., at least 2.0, 5.0, 8.0, 10.0, or at least 15.0, as compared to the detergent with optical brightener and/or anti-redeposition polymer but without said enzyme (s) .
  • the detergent composition further comprises an enzyme selected from the group of amylases, lipases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, ⁇ -glucanases, arabinosidases, hyaluronidase, laccase, deoxyribonucleases (DNases) , hexosaminidases and, or any mixture thereof.
  • an enzyme selected from the group of amylases, lipases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases,
  • the enzyme suitable for replacing a whiteness-maintaining agent is an enzyme having cellulase activity.
  • Suitable cellulase may be selected from glycoside hydrolase family 5 (GH5) , glycoside hydrolase family 7 (GH7) , glycoside hydrolase family 12 (GH12) , glycoside hydrolase family 44 (GH44) and glycoside hydrolase family 45 (GH45) , preferably family GH45 cellulases.
  • Suitable family GH44 cellulases can be a family 44 xyloglucanase having a sequence of at least 60%identity to positions 40-559 of SEQ ID NO: 2 of WO 2001/062903.
  • the enzyme having cellulase activity is a polypeptide having at least 60%sequence identity to the polypeptide of SEQ ID NO: 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or 23.
  • the enzyme having cellulase activity is a polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%sequence identity to the polypeptide of SEQ ID NO: 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or 23, or a fragment thereof having cellulase activity.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 13, or a fragment thereof having cellulase activity.
  • said cellulase is from Thermothielavioides, preferably from Thermothielavioides terrestris.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 14, or a fragment thereof having cellulase activity.
  • the mature polypeptide is amino acids 22 to 294 of SEQ ID NO: 14.
  • said enzyme is from Paenibacillus, preferably from Paenibacillus polymyxa.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 15, or a fragment thereof having cellulase activity.
  • said enzyme is from Thermothielavioides, preferably from Thermothielavioides terrestris.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 16, or a fragment thereof having cellulase activity.
  • said enzyme is from Thermothielavioides, preferably from Thermothielavioides terrestris.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 17, or a fragment thereof having cellulase activity.
  • said enzyme is from Acremonium, preferably from Acremonium thermophilum.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 18, or a fragment thereof having cellulase activity.
  • said enzyme is from Paenibacillus, preferably from Paenibacillus polymyxa.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 19, or a fragment thereof having cellulase activity.
  • said enzyme is from Neurospora, preferably from Neurospora tetrasperma.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 20, or a fragment thereof having cellulase activity.
  • said enzyme is from Staphylotrichum, preferably from Staphylotrichum coccosporum.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 21, or a fragment thereof having cellulase activity.
  • said enzyme is from Humicola, preferably from Humicola insolens.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 22, or a fragment thereof having cellulase activity.
  • said enzyme is from Paenibacillus, preferably from Paenibacillus polymyxa.
  • the enzyme having cellulase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 23, or a fragment thereof having cellulase activity.
  • said enzyme is from Chaetomium, preferably from Chaetomium thermophilum.
  • Additional suitable cellulases are the alkaline or neutral cellulases having colour care benefits.
  • Examples of such cellulases are cellulases described in EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, WO 98/08940.
  • Other examples are cellulase variants such as those described in WO 94/07998, EP 0 531 315, US 5, 457, 046, US 5, 686, 593, US 5, 763, 254, WO 95/24471, WO 98/12307 and WO99/001544.
  • cellulases include Celluzyme, Carezyme, Carezyme Elite, Carezyme Premium, Luminous, Celluclean, Celluclean Classic, Cellusoft, Whitezyme, Celluclean 4500T and Celluclean 5000L (all registered trademarks of Novozymes A/S) , Clazinase and Puradax HA (registered trademarks of Genencor International Inc.
  • the preparation of the enzyme having cellulase activity as described herein can e.g., be performed as described in WO 2015/036579 (incorporated herein by reference) .
  • the enzyme of the present invention may also be prepared by any method known in the art.
  • the polypeptide having mannanase activity or the mannanase suitable for replacing a whiteness/color-maintaining agent is an enzyme that hydrolyses compounds known as mannans.
  • Mannanases are enzymes catalyzing hydrolyses of 1, 4-beta-D- mannosidic linkages in mannans, galactomannans, glucomannans, and galactoglucomannans.
  • Mannans are polysaccharides with a backbone of b-1, 4-linked D-mannopyranosyl residues, which can contain galactose or acetyl substitutions and may have glucose residues in the backbone.
  • the main enzyme type participating in the degradation of mannans are endo-1, 4-p-mannanases (EC 3.2.1.78) , which hydrolyze the internal glycoside bonds in the mannan backbone.
  • mannanase activity is determined according to the procedure described in the Assay II. According to CAZy (www. Bacillus. org) , endo-1, 4-p-mannanases can be found in glycoside hydrolase families 5, 26 and 113.
  • Suitable mannanases include those of bacterial or fungal origin. Chemically or genetically modified mannanases are included. It may be a wild-type from Bacillus or Humicola, particularly B. agaradhaerens, B. licheniformis, B.
  • Suitable mannanases are described in WO 1999/064619. Commercially available mannanases are Mannaway (Novozymes A/S) , EFFECTENZ TM M1000 and Preferenz M 100 from Dupont, (Danisco/DuPont) , and Biotouch M9 from AB Enzyme.
  • mannanases include any of the GH26 Mannanases, mannanase from Preussia aemulans mature sequence of SEQ ID NO: 2 of W02017/021515, mannanase from Yunnania penicillata mature sequence of SEQ ID NO: 2 of W02017/021516, mannanase from Myrothecium roridum mature sequence of SEQ ID NO: 2 of W02017/021517, mannanase from Chaetomium brasiliense mature sequence of SEQ ID NO: 2 of W02017/021518, mannanases from Ascobolus stictoideus or mannanase from Chaetomium virescens SEQ ID NO: 3 and 6 from WO2015/040159.
  • the enzyme having mannanase activity or the mannanase is a polypeptide having at least 60%sequence identity to the polypeptide of SEQ ID NO: 6, 7, 8, 9, 10, 11 or 12.
  • the enzyme having mannanase activity is a polypeptide having at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%, or 100%sequence identity to the polypeptide of SEQ ID NO: 6, 7, 8, 9, 10, 11 or 12, or a fragment thereof having mannanase activity.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 6, or a fragment thereof having mannanase activity.
  • said mannanase is from Alkalihalobacillus, preferably from Alkalihalobacillus bogoriensis.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 7, or a fragment thereof having mannanase activity.
  • said mannanase is from Alkalihalobacillus, preferably from Alkalihalobacillus bogoriensis.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 8, or a fragment thereof having mannanase activity.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 9, or a fragment thereof having mannanase activity.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 10, or a fragment thereof having mannanase activity.
  • said mannanase is from Bacillus, preferably from Bacillus clausii.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 11, or a fragment thereof having mannanase activity.
  • said mannanase is from Bacillus sp.
  • the enzyme having mannanase activity is a polypeptide having at least 80%, at least 85%, at least 90%, at least 95%, at least 98%, at least 99%or 100%sequence identity to the mature polypeptide of SEQ ID NO: 12, or a fragment thereof having mannanase activity.
  • said mannanase is from Paenibacillus sp.
  • protease suitable for replacing a whiteness/color-maintaining agent 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 or a 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 from Bacillus and related genera (cf. Patel and Gupta, supra) .
  • Bacillus species from which subtilases have been derived include Bacillus lentus, Bacillus alcalophilus, Bacillus subtilis, Bacillus amyloliquefaciens, Bacillus licheniformis, Bacillus pumilus and Bacillus gibsonii.
  • 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.
  • Preferred protease variants may, for example, comprise one or more of the mutations selected from the group consisting of: S3T, V4I, S9R, S9E, A15T, S24G, S24R, K27R, N42R, S55P, G59E, G59D, N60D, N60E, V66A, N74D, S85R, A96S, S97G, S97D, S97A, S97SD, S99E, S99D, S99G, S99M, S99N, S99R, S99H, S101A, V102I, V102Y, V102N, S104A, G116V, G116R, H118D, H118N, A120S, S126L, P127Q, S128A, S154D, A156E, G157D, G157P, S158E, Y161A, R164S, Q176E, N179E, S182E, Q185N, A188P, G189E, V
  • Protease variants having one or more of these mutations are preferably variants of the Bacillus lentus protease (also known as subtilisin 309) shown in SEQ ID NO: 1 of WO 2016/001449 or of the Bacillus amyloliquefaciens protease (BPN’ ) shown in SEQ ID NO: 2 of WO 2016/001449.
  • Bacillus lentus protease also known as subtilisin 309
  • BPN Bacillus amyloliquefaciens protease
  • Such protease variants preferably have at least 80%sequence identity to SEQ ID NO: 1 or to SEQ ID NO: 2 of WO 2016/001449.
  • protease of interest is the alkaline protease from Bacillus lentus DSM 5483, as described for example in WO 91/02792, and variants thereof which are described for example in WO 92/21760, WO 95/23221, EP 1921147, EP 1921148 and WO 2016/096711.
  • the protease may alternatively be a variant of the TY145 protease having SEQ ID NO: 1 of WO 2004/067737, for example a variant comprising a substitution at one or more positions corresponding to positions 27, 109, 111, 171, 173, 174, 175, 180, 182, 184, 198, 199 and 297 of SEQ ID NO: 1 of WO 2004/067737, wherein said protease variant has a sequence identity of at least 75%but less than 100%to SEQ ID NO: 1 of WO 2004/067737.
  • a preferred protease according to the present invention may be a protease having at least 60%, such as at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%or 100%sequence identity to the polypeptide of SEQ ID NO: 1, 2, 3, 4 or 5.
  • a preferred protease according to the present invention may be a variant of the polypeptide of SEQ ID NO: 2 comprising an alteration at one or more positions corresponding to positions 3, 4, 9, 15, 43, 68, 76, 99, 101, 103, 104, 160, 167, 170, 194, 199, 205, 206, 209, 217, 218, 222, 245, 261 and 262, wherein position numbers correspond to the positions of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to the polypeptide of SEQ ID NO: 2.
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 2, comprising one or more substitutions selected from the group consisting of: S3T, V4I, S9E, S9R, A15T, V68A, N76D, S99D, S99G, S99A, S99SE, S101E, S101N, S101R, S103A, V104I, G160S, Y167A, R170S, A194P, V199M, V205I, Q206L, Y209W, L217D, L217Q, N218D, M222S, Q245R, N261W and L262E, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%,
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 2, comprising one or more substitutions selected from the group consisting of: S3T, V4I, S9E, S9R, A15T, V68A, N76D, S99D, S99G, S99A, S99SE, S101E, S101N, S101R, S103A, V104I, G160S, Y167A, R170S, A194P, V199M, V205I, Q206L, Y209W, L217D, L217Q, N218D, M222S, Q245R, N261W and L262E, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%,
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 2, comprising the substitution S87N, wherein the variant has protease activity and wherein the position corresponds to the position of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2.
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 2, comprising the substitutions Y167A + R170S + A194P, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2.
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 2, comprising the substitutions S9E + N43R + N76D + V205I + Q206L + Y209W + S259D +N261W + L262E, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2.
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 2, comprising the substitutions S3T + N43R + N76D + S87N + G118M + S128Q + N184E +V205I + Q206L + Y209W + S259D + N261W + L262E, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2.
  • the protease of the invention is a variant of the polypeptide of SEQ ID NO: 4, comprising the substitutions A68S + T77N + T78I + G127S + A128P + G165Q + N184Q +A202V + N217S + S258P, wherein position numbers correspond to the positions of SEQ ID NO: 4, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 4.
  • the protease of the invention is a variant comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179 or 180 of SEQ ID NO: 1 of WO2004/067737, wherein the variant has protease activity and has a sequence identity of at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%to SEQ ID NO: 1 of WO2004/067737.
  • the protease of the invention is a variant comprising one or more substitutions compared to a parent protease, selected from the group consisting of X3V, X9 [E, R] , X22[R, A] , X43R, X61 [E, D] , X62 [E, D] , X76 [D] , X87N, X101 [E, G, D, N, M] , X103A, X104I, X118 [V, R] , X120V, X128 [A, L, S] , X129Q, X130A, X160D, X185 [E, D] , 188 [E, D] , X191N, X194P, X205I, X206L, X209W, X216V, X217 [Q, D, E] , X218 [D, E, S] , X232V
  • the protease of the invention is a variant comprising any of the following substitution sets compared to a parent protease, wherein the parent protease has the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2 or has at least 80%sequence identity to SEQ ID NO: 1 or SEQ ID NO: 2, wherein position numbers correspond to the positions of BPN’ (SEQ ID NO: 1) , wherein “X” represents any amino acid residue present in the specified position in the parent protease, and wherein the substitution set is selected from the group consisting of:
  • protease variant has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 1 or 2.
  • the protease variant of the invention comprises the amino acid sequence of SEQ ID NO: 2 with the substitutions Y167A + R170S + A194P , wherein the variant has protease activity and wherein the positions correspond to the positions of SEQ ID NO: 1.
  • the protease variant of the invention comprises the amino acid sequence of SEQ ID NO: 2 with the substitutions S9E + N43R + N76D + V205I + Q206L + Y209W + S259D + N261W + L262E, wherein the variant has protease activity and wherein position numbers correspond to the positions of SEQ ID NO: 1.
  • the protease of the invention is an enzyme having or consisting of the amino acid sequence of SEQ ID NO: 2, 3, 4 or 5.
  • Suitable commercially available protease enzymes may include those sold under the trade nam es Duralase TM , Durazym TM , Ultra, Ultra, Primase TM , Ultra, Ultra, Pro, Blaze 100T, Blaze 125T, Blaze 150T, Blaze 200T, Uno, In and Excel (Novozymes A/S) , those sold under the tradename Maxatase TM , Maxacal TM , Ox, OxP, FN2 TM , FN3 TM , FN4 exTM , Excellenz TM P1000, Excellenz TM P1250, Eraser TM , P100, P300, Purafect Prime, Preferenz P110 TM , Effectenz P1000 TM , Effectenz P1050 TM , Ox, Effectenz TM P2000, Purafast TM , Opticlean TM and (Danisco/DuPont) , BLAP (sequence shown in Figure 29
  • the variants of the enzymes comprise a substitution, deletion, and/or insertion at one or more positions.
  • the number of amino acid substitutions, deletions and/or insertions introduced into the mature polypeptide of e.g. SEQ ID NO: 2, 3, 5, 6, 10, or 11 is no more than 20, e.g., 1-15, such as 1, 2, 3, 4, 5, 6, 7, 8, 9 or 10.
  • 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 or alanine-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 proteas activity, cellulase activity or mannanase 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 labeling, 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.
  • the enzymes suitable for replacing a whiteness/color-maintaining agent of a detergent composition is an enzyme combination of the protease, the mannanase and/or the cellulase as described above.
  • the enzymes suitable for replacing a whiteness/color-maintaining agent is an enzyme combination of a protease and a mannanase, wherein the protease is a polypeptide comprising or consisting of SEQ ID NO: 2, wherein the mannanase is a polypeptide having or consisting of SEQ ID NO: 6, 7, 8, 9, 10 or 11.
  • the protease is the polypeptide of SEQ ID NO: 2 with the substitutions S9E + N43R + N76D + V205I +Q206L + Y209W + S259D + N261W + L262E, wherein position numbers are based on the numbering of SEQ ID NO: 1, and wherein the mannanase is a polypeptide having or consisting of SEQ ID NO: 6 or 7.
  • the enzymes suitable for replacing the whiteness/color-maintaining agent is an enzyme combination of a protease and a cellulase, wherein the protease comprises or consisting of the polypeptide of SEQ ID NO: 2, wherein the cellulase is a polypeptide having or consisting of SEQ ID NO: 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or 23.
  • the protease is the polypeptide of SEQ ID NO: 2 with the substitutions S9E + N43R + N76D + V205I + Q206L + Y209W + S259D + N261W + L262E, wherein position numbers are based on the numbering of SEQ ID NO: 1, and wherein the cellulase is a polypeptide having or consisting of SEQ ID NO: 18, 21 or 22.
  • the enzymes suitable for replacing the whiteness/color-maintaining agent is an enzyme combination of a mannanase and a cellulase, wherein the mannanase is a polypeptide comprising or consisting of SEQ ID NO: 6, 7, 8, 9, 10 or 11, wherein the cellulase is a polypeptide comprising or consisting of SEQ ID NO: 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or 23.
  • the mannanase is a polypeptide comprising or consisting of SEQ ID NO: 6 or 7, and wherein the cellulase is a polypeptide having or consisting of SEQ ID NO: 18, 21 or 22.
  • the enzymes suitable for replacing a whiteness/color-maintaining agent is an enzyme combination of a protease, a mannanase and a cellulase, wherein the protease is a polypeptide comprising or consisting of SEQ ID NO: 2, wherein the mannanase is a polypeptide having or consisting of SEQ ID NO: 6, 7, 8, 9, 10 or 11 and wherein the cellulase is a polypeptide having or consisting of SEQ ID NO: 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or 23.
  • the protease is the polypeptide of SEQ ID NO: 2 with the substitutions S9E +N43R + N76D + V205I + Q206L + Y209W + S259D + N261W + L262E, wherein position numbers are based on the numbering of SEQ ID NO: 1, and the mannanase is a polypeptide having or consisting of SEQ ID NO: 6 or 7, and the cellulase is a polypeptide having or consisting of SEQ ID NO: 18, 21 or 22.
  • the protease is the polypeptide of SEQ ID NO: 2 and the mannanase is a polypeptide having or consisting of SEQ ID NO: 7, and the cellulase is a polypeptide having or consisting of SEQ ID NO: 18 or 21.
  • the enzyme (s) 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
  • the textile is selected from the group consisting of: cellulose based textiles and textiles which partly is made of cellulose-based textile.
  • the textile is cotton, or a mixture of cotton with other types of fabric, such as a mixture of at least 50%polyester and at least 20%cotton, or a mixture of at least 30%polyester and at least 40%cotton.
  • the optical brightener may be present at most 0.6 %by weight of the composition, such as at most 0.4 %by weight of the composition, at most 0.3 %by weight of the composition, at most 0.25 %by weight of the composition, at most 0.2 %by weight of the composition, at most 0.15 %by weight of the composition, at most 0.1 %by weight of the composition, at most 0.08 %by weight of the composition, at most 0.05 %by weight of the composition, at most 0.04 %by weight of the composition, at most 0.02 %by weight of the composition or at most 0.01%by weight of the composition.
  • the anti-redeposition polymer may be present at most 1 %by weight of the composition, such as at most 0.8 %by weight of the composition, at most 0.6 %by weight of the composition, at most 0.4 %by weight of the composition, at most 0.2 %by weight of the composition, at most 0.15 %by weight of the composition, at most 0.1 %by weight of the composition, at most 0.08 % by weight of the composition, at most 0.05 %by weight of the composition, at most 0.04 %by weight of the composition.
  • the detergent 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 mixture of one or more nonionic surfactants and one or more anionic surfactants.
  • the surfactant (s) is typically present at a level of from about 0.1%to 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 includes any conventional surfactant (s) known in the art. Any surfactant known in the art for use in detergents may be utilized.
  • the detergent When included therein the detergent will usually contain from about 1%to about 40%by weight, such as from about 5%to about 30%, including from about 5%to about 15%, or from about 20%to about 25%of an anionic surfactant.
  • anionic surfactants include sulfates and sulfonates, in particular, linear alkylbenzenesulfonates (LAS) , isomers of LAS, branched alkylbenzenesulfonates (BABS) , phenylalkanesulfonates, alpha-olefinsulfonates (AOS) , olefin sulfonates, alkene sulfonates, alkane-2, 3-diylbis (sulfates) , hydroxyalkanesulfonates and disulfonates, alkyl sulfates (AS) such as sodium dodecyl sulfate (SDS) , fatty alcohol sulfates (FAS) ,
  • the detergent When included therein the detergent will usually contain from about 1%to about 40%by weight of a cationic surfactant.
  • cationic surfactants include alklydimethylehanolamine quat (ADMEAQ) , cetyltrimethylammonium bromide (CTAB) , dimethyldistearylammonium chloride (DSDMAC) , and alkylbenzyldimethylammonium, and combinations thereof, Alkyl quaternary ammonium compounds, Alkoxylated quaternary ammonium (AQA) .
  • the detergent When included therein the detergent will usually contain from about 0.2%to about 60%by weight of a non-ionic surfactant, for example from about 0.3 to about 40%, such as 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%, or from about 8%to about 12%.
  • a non-ionic surfactant for example from about 0.3 to about 40%, such as 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%, or from about 8%to about 12%.
  • Non-limiting examples of non-ionic surfactants include alcohol ethoxylates (AE or AEO) , alcohol propoxylates, propoxylated fatty alcohols (PFA) , alkoxylated fatty acid alkyl esters, such as ethoxylated and/or propoxylated fatty acid alkyl esters, alkylphenol ethoxylates (APE) , nonylphenol ethoxylates (NPE) , alkylpolyglycosides (APG) , alkoxylated amines, fatty acid monoethanolamides (FAM) , fatty acid diethanolamides (FADA) , ethoxylated fatty acid monoethanolamides (EFAM) , propoxylated fatty acid monoethanolamide (PFAM) , polyhydroxy alkyl fatty acid amides, or N-acyl N-alkyl derivatives of glucosamine (glucamides, GA, or fatty acid glucamide, FAGA)
  • the detergent When included therein the detergent will usually contain from about 1%to about 40%by weight of a semipolar surfactant.
  • semipolar surfactants include amine oxides (AO) such as alkyldimethylamineoxide, N- (coco alkyl) -N, N-dimethylamine oxide and N-(tallow-alkyl) -N, N-bis (2-hydroxyethyl) amine oxide, fatty acid alkanolamides and ethoxylated fatty acid alkanolamides, and combinations thereof.
  • AO amine oxides
  • the detergent When included therein the detergent will usually contain from about 1%to about 40%by weight of a zwitterionic surfactant.
  • zwitterionic surfactants include betaine, alkyldimethylbetaine, and sulfobetaine, and combinations thereof.
  • the detergent composition may contain about 0-65%by weight of a detergent builder or co-builder, or a mixture thereof.
  • the level of builder is typically 40-65%, particularly 50-65%.
  • the builder and/or co-builder may particularly be a chelating agent that forms water-soluble complexes with Ca 2+ and Mg 2+ . Any builder and/or co-builder known in the art for use in laundry 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 Hoechst) , disilicates, ethanolamines such as 2-aminoethan-1-ol (MEA) , iminodiethanol (DEA) and 2, 2’ , 2” -nitrilotriethanol (TEA) , and carboxymethylinulin (CMI) , and combinations thereof.
  • 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 Hoechst) , disilicates, ethanolamines such
  • the detergent composition may also contain 0-65%by weight of a detergent co-builder, or a mixture thereof.
  • the detergent composition may include include a co-builder alone, or in combination with a builder, for example a zeolite builder.
  • co-builders include homopolymers of polyacrylates or copolymers thereof, such as poly (acrylic acid) (PAA) or copoly (acrylic acid/maleic acid) (PAA/PMA) .
  • 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 etheylenediaminetetraacetic acid
  • DTPA diethylenetriaminepentaacetic acid
  • IDS iminodisuccinic acid
  • EDDS ethylenediamine-N, N’ -disuccinic acid
  • MGDA methylglycinediacetic acid
  • GLDA glutamic acid-N, N-diacetic acid
  • HEDP 1-hydroxyethane-1, 1-diylbis (phosphonic acid)
  • EDTMPA ethylenediaminetetrakis
  • DTPMPA diethylenetriaminepentakis (methylene) pentakis (phosphonic acid)
  • DTPMPA N- (2-hydroxyethyl) iminodiacetic acid
  • EDG N- (2-hydroxyethyl) iminodiacetic acid
  • EDG N- (2-hydroxyethyl) iminodiacetic acid
  • the detergent may contain 0-40%by weight, such as about 5%to about 25%, of a bleaching system.
  • a bleaching system Any bleaching system known in the art for use in laundry detergents may be utilized. Suitable bleaching system components include bleaching catalysts, photobleaches, bleach activators, sources of hydrogen peroxide such as sodium percarbonate and sodium perborates, preformed peracids and mixtures thereof.
  • the detergent in addition to the anti-redeposition polymer as mentioned above, may further contain 0-10%by weight, such as 0.5-5%, 2-5%, 0.5-2%or 0.2-1%of another type of polymer.
  • the polymer may function as a co-builder as mentioned above, or may provide 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. Any polymer known in the art for use in detergents may be utilized.
  • the detergent additive as well as the detergent composition may comprise one or more additional enzymes such as lipases, amylases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, malanases, ⁇ -glucanases, arabinosidases, hyaluronidase, laccase, deoxyribonucleases (DNases) , hexosaminidases, and any mixture thereof.
  • additional enzymes such as lipases, amylases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, lignina
  • the properties of the selected enzyme (s) should be compatible with the selected detergent, (i.e., pH-optimum, compatibility with other enzymatic and non-enzymatic ingredients, etc. ) , and the enzyme (s) should be present in effective amounts.
  • the enzyme (s) when present in a cleaning composition, may be present at levels of at least 0.001 mg of enzyme protein, at least 0.006 mg of enzyme protein, at least 0.008 mg of enzyme protein, at least 0.01 mg of enzyme protein, at least 0.1 mg of enzyme protein, at least 0.5 mg of enzyme protein, at least 1 mg of enzyme protein, or at least 2 mg of enzyme protein.
  • the enzyme of the invention may be formulated as a granule for example as a co-granule that combines one or more enzymes. Each enzyme will then be present in more granules securing a more uniform distribution of enzymes in the detergent. This also reduces the physical segregation of different enzymes due to different particle sizes.
  • Methods for producing multi-enzyme co-granulates for the detergent industry are disclosed in the IP. com disclosure IPCOM000200739D.
  • WO 2013/188331 Another example of formulation of enzymes by the use of co-granulates is disclosed in WO 2013/188331, which relates to a cleaning composition comprising (a) a multi-enzyme co-granule; (b) less than 10 wt zeolite (anhydrous basis) ; and (c) less than 10 wt phosphate salt (anhydrous basis) , wherein said enzyme co-granule comprises from 10 to 98 wt%moisture sink component and the composition additionally comprises from 20 to 80 wt%detergent moisture sink component.
  • WO 2013/188331 also relates to a method of treating and/or cleaning a surface, comprising the steps of (i) contacting said surface with the cleaning composition as claimed and described herein in an aqueous wash liquor, (ii) rinsing and/or drying the surface.
  • the multi-enzyme co-granule may comprise an enzyme of the invention and one or more enzymes selected from the group consisting of lipases, amylases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases, malanases, ⁇ -glucanases, arabinosidases, hyaluronidase, laccase, deoxyribonucleases (DNases) , hexosaminidases, and any mixture thereof.
  • lipases amylases, hemicellulases, peroxidases, xylanases, phospholipases, esterases, cutinases, keratinases, reductases, oxidases, phenoloxidases, lipoxygenases
  • an enzyme for replacement of a whiteness-maintaining agent in a cleaning composition wherein the enzyme is selected from the group consisting of a protease, a mannanase, a cellulase and combinations thereof.
  • the whiteness-maintaining agent is selected from the group consisting of an optical brightener, an anti-redeposition polymer and mixture thereof.
  • the protease has at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%or 100%sequence identity to the polypeptide of SEQ ID NO: 1, 2, 3, 4 or 5.
  • the protease is a variant of the polypeptide of SEQ ID NO: 2 comprising an alteration at one or more positions corresponding to positions 3, 4, 9, 15, 43, 68, 76, 99, 101, 103, 104, 160, 167, 170, 194, 199, 205, 206, 209, 217, 218, 222, 245, 261 and 262, wherein position numbers correspond to the positions of SEQ ID NO: 1, wherein each alteration is independently a substitution, deletion or insertion, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to the polypeptide of SEQ ID NO: 2.
  • protease is:
  • a variant of the polypeptide of SEQ ID NO: 2 comprising one or more substitutions selected from the group consisting of: S3T, V4I, S9E, S9R, A15T, V68A, N76D, S99D, S99G, S99A, S99SE, S101E, S101N, S101R, S103A, V104I, G160S, Y167A, R170S, A194P, V199M, V205I, Q206L, Y209W, L217D, L217Q, N218D, M222S, Q245R, N261W and L262E, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%,
  • a variant of the polypeptide of SEQ ID NO: 2 comprising the substitutions N76D + Y209W, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2;
  • variants of the polypeptide of SEQ ID NO: 2 comprising the substitution S87N, wherein the variant has protease activity and wherein the position corresponds to the position of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2;
  • a variant of the polypeptide of SEQ ID NO: 2 comprising the substitutions Y167A + R170S + A194P, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2;
  • variants of the polypeptide of SEQ ID NO: 2 comprising the substitutions S9E + N43R + N76D + V205I + Q206L + Y209W + S259D + N261W + L262E, wherein position numbers correspond to the positions of SEQ ID NO: 1, and wherein the variant has protease activity and has at least 80, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 2;
  • variants of the polypeptide of SEQ ID NO: 4 comprising the substitutions A68S + T77N + T78I + G127S + A128P + G165Q + N184Q + A202V + N217S + S258P, wherein position numbers correspond to the positions of SEQ ID NO: 4, and wherein the variant has protease activity and has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 4;
  • variants comprising a substitution at one or more positions corresponding to positions 171, 173, 175, 179 or 180 of SEQ ID NO: 1 of WO2004/067737, wherein the variant has protease activity and has a sequence identity of at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%to SEQ ID NO: 1 of WO2004/067737;
  • a protease variant comprising one or more substitutions compared to a parent protease, selected from the group consisting of X3V, X9 [E, R] , X22 [R, A] , X43R, X61 [E, D] , X62 [E, D] , X76 [D] , X87N, X101 [E, G, D, N, M] , X103A, X104I, X118 [V, R] , X120V, X128 [A, L, S] , X129Q, X130A, X160D, X185 [E, D] , 188 [E, D] , X191N, X194P, X205I, X206L, X209W, X216V, X217 [Q, D, E] , X218 [D, E, S] , X232V, X245R
  • a protease variant comprising any of the following substitution sets compared to a parent protease, wherein the parent protease has the amino acid sequence of SEQ ID NO: 1 or SEQ ID NO: 2 or has at least 80%sequence identity to SEQ ID NO: 1 or SEQ ID NO: 2, wherein position numbers correspond to the positions of BPN’ (SEQ ID NO: 1) , wherein “X” represents any amino acid residue present in the specified position in the parent protease, and wherein the substitution set is selected from the group consisting of:
  • protease variant has at least 80%, at least 85%, at least 90%, at least 91%, at least 92%, at least 93%, at least 94%, at least 95%, at least 96%, at least 97%, at least 98%, or at least 99%, but less than 100%sequence identity to SEQ ID NO: 1 or 2.
  • the protease variant comprises the amino acid sequence of SEQ ID NO: 2 with the substitutions Y167A + R170S + A194P, wherein the variant has protease activity, and wherein position numbers correspond to the positions of SEQ ID NO: 1.
  • the protease variant comprises the amino acid sequence of SEQ ID NO: 2 with the substitutions S9E + N43R + N76D + V205I + Q206L + Y209W + S259D + N261W + L262E, wherein the variant has protease activity and wherein position numbers correspond to the positions of SEQ ID NO: 1.
  • the protease variant comprises the amino acid sequence of SEQ ID NO: 2 with the substitutions S3T + N43R + N76D + S87N + G118M + S128Q + N184E + V205I + Q206L + Y209W + S259D + N261W + L262E, wherein the variant has protease activity and wherein position numbers correspond to the positions of SEQ ID NO: 1.
  • protease is an enzyme having or consisting of the amino acid sequence of SEQ ID NO: 2, 3, 4 or 5.
  • cellulase is an enzyme having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%or 100%sequence identity to SEQ ID NO: 13, 14, 15, 16, 17, 18, 19, 20, 21, 22 or 23.
  • mannanase is an enzyme having at least 60%, at least 65%, at least 70%, at least 75%, at least 80%, at least 85%, at least 90%, at least 95%, at least 96%, at least 97%, at least 98%, at least 99%or 100%sequence identity to SEQ ID NO: 6, 7, 8, 9, 10, 11 or 12.
  • a cleaning composition free of at least one whiteness-maintaining agent wherein the composition comprises at least two enzymes selected from the group consisting of a protease, a mannanase and a cellulase.
  • the whiteness-maintaining agent is selected from the group consisting of an optical brightener, an anti-redeposition polymer and mixture thereof, and preferably the cleaning composition is a laundry detergent.
  • a method for maintaining or improving the whiteness and/or color of a textile comprising: (a) exposing said textile to a wash liquor comprising the detergent composition according to any of preceding paragraphs 17-19; and optionally (b) rinsing the textile.
  • Suc-AAPF-pNA is an abbreviation for N-Succinyl-Alanine-Alanine-Proline-Phenylalanine-p-Nitroanilide, and is a blocked peptide which can be cleaved by endo-proteases. Following proteolytic cleavage, a free pNA molecule having a yellow color is liberated and can be measured by visible spectrophotometry at wavelength 405nm.
  • the Suc-AAPF-PNA substrate is manufactured by Bachem (cat. no. L1400, dissolved in DMSO) .
  • the protease sample to be analyzed is diluted in residual activity buffer (100mM Tris pH 8.6) .
  • the assay is performed by transferring 30 ⁇ l of diluted enzyme samples to 96 well micro-titer plate and adding 70 ⁇ l substrate working solution (0.72mg/ml in 100mM Tris pH 9) .
  • the solution is mixed at room temperature and absorption is measured every 20 sec. over 5 minutes at OD 405 nm.
  • the slope (absorbance per minute) of the time dependent absorption-curve is directly proportional to the activity of the protease in question under the given set of conditions.
  • the protease sample should be diluted to a level where the slope is linear.
  • Mannanase activity is determined by using insoluble Azo-carob-galactomannan substrate from Megazyme. Substrate was incubated with enzyme for 20 min at 25°C, shaking at 800 rpm. The reaction mixture was kept static for 10 min to allow insoluble substrate to settle. Enzyme activity was measured by reading the optical density of supernatant at 590 nm.
  • Cellulase activity is determined as the ability of an enzyme to catalyze hydrolysis of 1, 4-beta-D-glucosidic linkages in beta-1, 4-glucan (cellulose) .
  • cellulase activity is determined using AZCL-HE-cellulose (from Megazyme) as the reaction substrate. Substrate was incubated with enzyme for 20 min at 30°C, shaking at 800 rpm. The reaction mixture was kept static for 10 min to allow insoluble substrate to settle. Enzyme activity was measured by reading the optical density of supernatant at 590 nm.
  • Protease polypeptide of SEQ ID NO: 2 with the following mutations: S9E + N43R + N76D + V205I + Q206L + Y209W + S259D + N261W + L26E, wherein position numbers are based on the numbering of SEQ ID NO: 1.
  • Mannanase a mannanase corresponding to the polypeptide of SEQ ID NO: 7.
  • Cellulase A a cellulase corresponding to the polypeptide of SEQ ID NO: 18.
  • Cellulase B a cellulase corresponding to the polypeptide of SEQ ID NO: 21.
  • Cellulase C a cellulase corresponding to the polypeptide of SEQ ID NO: 14.
  • the Tergo-To-Meter 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 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/polymer 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 provides the link between small scale experiments and the more time-consuming full-scale experiments.
  • the water bath with 16 steel beakers and 1 rotating arm per beaker with capacity of 1L detergent solution. Temperature ranges from 5°C to 80°C.
  • the water bath has to be filled up with deionised water. Rotational speed can be set up to 70 to 120rpm/min.
  • 1L wash solution is added into a TOM beaker.
  • the wash solution or wash liquor is agitated at 120rpm and one or more enzymes, optical brighteners or polymers are added to the beaker.
  • the whiteness tracers are sprinkled into the beaker and then the ballast load. Time measurement starts when the swatches and ballast are added to the beaker. The swatches are washed for 20 or 30 minutes after which agitation is terminated.
  • the wash load is subsequently transferred from the TOM beaker to a sieve and rinse with cold tap water.
  • the soil swatches are separated from the ballast load.
  • the soil swatches are transferred to a 5L beaker with cold tap water under running water for 5 minutes.
  • the ballast load is kept separately for the coming inactivation.
  • the water is gently pressed out of the swatches by hand and placed on a tray covered with a paper.
  • the swatches are allowed to dry overnight before subjecting the swatches to analysis, such as measuring the delta REM.
  • Whiteness can be expressed as the Remission (R) , which is a measure for the light reflected or emitted from the test material when illuminated with white light.
  • the Remission of the textiles is measured at 460 nm using a Macbeth Color Eye 7000 reflectance spectrophotometer with very small aperture The measurements were made without UV in the incident light and remission at 460 nm (R460) was extracted. The measurements are done per the manufacturer's protocol. Whiteness performance is evaluated by R460 or ⁇ R460.
  • ⁇ R460 may be calculated as: R460 value of the tracer washed by detergent + other additives (OB, ARD polymer or enzymes) minus the R460 value of the tracer wash by a comparable detergent e.g., a detergent without at least one of said additives.
  • Example 1 Whiteness performance evaluation on white tracers
  • WE1 Sum of ⁇ R460 (detergent + enzyme (s) ) minus Sum of ⁇ R460 (detergent + OB +ARD polymer) . So, “WE1” indicates the whiteness improvement over a detergent comprising both OB and ARD polymer but free of the enzyme (s) of the invention.
  • WE2 Sum of ⁇ R460 (detergent + enzyme (s) ) minus Sum of ⁇ R460 (detergent + OB) . So, “WE2” indicates the whiteness improvement over a detergent comprising an optical brightener but free of the enzyme (s) of the invention.
  • whiteness-maintaining agent such as OB or ARD polymer
  • OB or ARD polymer can improve the whiteness performance of a detergent composition, in other words, can prevent/reduce the loss of whiteness of a textile.
  • Replacing said agent with single enzyme (protease, mannanase or cellulase) of the invention can further improve the whiteness performance of the detergent composition.
  • Example 2 Whiteness performance evaluation on white tracers
  • WE3 Sum of R460 (detergent + enzyme (s) ) minus Sum of R460 (detergent + OB +cleaning polymer) . So, “WE3” indicates the whiteness improvement over a detergent comprising both OB and cleaning polymer but free of the enzyme (s) of the invention.
  • WE4 Sum of R460 (detergent + enzyme (s) ) minus Sum of R460 (detergent + OB) . So, “WE4” indicates the whiteness improvement over a detergent comprising an optical brightener but free of the enzyme (s) of the invention.
  • WE5 Sum of R460 (detergent + enzyme (s) ) minus Sum of R460 (detergent + cleaning polymer) . So, “WE5” indicates the whiteness improvement over a detergent comprising a cleaning polymer but free of the enzyme (s) of the invention.
  • WE2 Sum of ⁇ R460 (detergent + enzyme (s) ) minus Sum of ⁇ R460 (detergent + OB) . So, “WE2” indicates the whiteness improvement over a detergent comprising an optical brightener but free of the enzyme (s) of the invention.

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Abstract

L'invention concerne l'utilisation d'une enzyme pour remplacer un agent de maintien de la blancheur dans une composition de nettoyage, l'enzyme étant choisie dans le groupe constitué d'une protéase, d'une mannanase, d'une cellulase et de combinaisons de ces dernières.
PCT/CN2023/120395 2022-09-21 2023-09-21 Utilisation d'une enzyme pour remplacer un agent de maintien de la blancheur dans une composition de nettoyage WO2024061317A1 (fr)

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Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5457046A (en) * 1990-05-09 1995-10-10 Novo Nordisk A/S Enzyme capable of degrading cellullose or hemicellulose
CN1768137A (zh) * 2003-01-30 2006-05-03 诺和酶股份有限公司 枯草杆菌酶
WO2020074499A1 (fr) * 2018-10-09 2020-04-16 Novozymes A/S Compositions de nettoyage et leurs utilisations
WO2020074498A1 (fr) * 2018-10-09 2020-04-16 Novozymes A/S Compositions de nettoyage et leurs utilisations
US20200255774A1 (en) * 2017-10-24 2020-08-13 Novozymes A/S Compositions Comprising Polypeptides Having Mannanase Activity

Patent Citations (5)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US5457046A (en) * 1990-05-09 1995-10-10 Novo Nordisk A/S Enzyme capable of degrading cellullose or hemicellulose
CN1768137A (zh) * 2003-01-30 2006-05-03 诺和酶股份有限公司 枯草杆菌酶
US20200255774A1 (en) * 2017-10-24 2020-08-13 Novozymes A/S Compositions Comprising Polypeptides Having Mannanase Activity
WO2020074499A1 (fr) * 2018-10-09 2020-04-16 Novozymes A/S Compositions de nettoyage et leurs utilisations
WO2020074498A1 (fr) * 2018-10-09 2020-04-16 Novozymes A/S Compositions de nettoyage et leurs utilisations

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