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EP4324900A1 - Waschmittelzusammensetzung mit enzymen - Google Patents

Waschmittelzusammensetzung mit enzymen Download PDF

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Publication number
EP4324900A1
EP4324900A1 EP22190727.2A EP22190727A EP4324900A1 EP 4324900 A1 EP4324900 A1 EP 4324900A1 EP 22190727 A EP22190727 A EP 22190727A EP 4324900 A1 EP4324900 A1 EP 4324900A1
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EP
European Patent Office
Prior art keywords
cellulase
detergent composition
amylase
protease
amount
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Pending
Application number
EP22190727.2A
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English (en)
French (fr)
Inventor
Elron Gomes
Sayed FARAHAT
Aya KALOU
Susanne Wieland
Natalia FRAGOSO SAUER QUINTO DI CAMELI
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Henkel AG and Co KGaA
Original Assignee
Henkel AG and Co KGaA
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
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Publication date
Application filed by Henkel AG and Co KGaA filed Critical Henkel AG and Co KGaA
Priority to EP22190727.2A priority Critical patent/EP4324900A1/de
Publication of EP4324900A1 publication Critical patent/EP4324900A1/de
Pending legal-status Critical Current

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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
    • 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
    • C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
    • 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

  • the present invention relates to a detergent composition comprising at least one protease, at least one amylase and at least one cellulase in specific amounts and ratios. Furthermore, the present invention relates to a method for preventing or removing greying of a fabric comprising contacting said fabric with a composition comprising at least one cellulase, at least one protease and at least one amylase, and to the use of at least one cellulase in combination with at least one protease and at least one amylase for preventing or removing greying of a fabric.
  • Adding anti-greying cellulase to a detergent such as a liquid detergent is well known.
  • components of a detergent composition can interact with each other and, thus, have a negative impact on the anti-greying or washing performance of the detergent.
  • the present invention relates to a detergent composition, preferably liquid laundry detergent compositions, comprising
  • the present invention relates to a method for preventing or removing greying of a fabric, comprising contacting said fabric with a composition comprising at least one cellulase, at least one protease and at least one amylase and, optionally, at least one lipase, wherein the detergent composition is a composition according to the present invention, in particular during a washing process.
  • the present invention further relates to the use of at least one cellulase in combination with at least one protease and at least one amylase and, optionally, at least one lipase for preventing or removing greying of a fabric, preferably in a washing process, wherein the enzymes are comprised in a detergent composition according to the present invention.
  • At least one means one or more, i.e. 1, 2, 3, 4, 5, 6, 7, 8, 9 or more of the referenced species. Similarly, “one or more”, as used herein, relates to at least one and comprises 1, 2, 3, 4, 5, 6, 7, 8, 9 or more. In connection with a given species, the term does not relate to the total number of molecules, but rather to the type of species. "At least one protease”, for example, thus means that one type of protease or two or more different types of proteases may be present. In connection with amounts, the term relates to the total amount of the referenced species. In case of proteases, for example, this means that the given amount is the total amount of all proteases in the composition.
  • the term "essentially free" within the context of this invention is to be interpreted as the respective compound is contained in the composition in an amount of less than 5 wt.-%, 4 wt.-%, 3 wt.-%, 2 wt.-%, 1.5 wt.-%, 1 wt.-%, 0.75 wt.-%, 0.5 wt.-%, 0.25 wt.-%, 0.1 wt.-%, 0.01 wt.-%, or 0.001 wt.-% based on the total weight of the composition, wherein the amounts are respectively more preferred in descending order. For example, 4 wt.-% is more preferred than 5 wt.-% and 3 wt.-% is more preferred than 4 wt.-%.
  • Variant refers to natural or artificially produced variations of a native enzyme/protein that has a modified amino acid sequence relative to the reference form.
  • a detergent composition comprising
  • Detergent compositions comprise all conceivable textile washing and/or care compositions used in the washing machine or in hand washing. This includes, for example, detergent compositions and compositions for cleaning, care and/or conditioning, pre- and/or posttreatment of all types of textiles, such as garments, carpets, and textile furniture surfaces.
  • the present invention is a laundry detergent composition, preferably a liquid laundry detergent composition.
  • liquid refers to compositions that are flowable and pourable at standard conditions (20 °C and 1013 mbar). Liquid compositions can also comprise gel-like and paste-like compositions. In particular, non-newtonian liquids are comprised as well.
  • the detergent composition is a solid or powdery detergent composition, e.g., a powder, extrudate, granules, or tablet.
  • composition further comprises d) at least one lipase.
  • the detergent composition comprises
  • the composition comprises
  • composition comprises
  • the composition comprises
  • the amount of protease in the detergent composition is reduced to equal to or less than 0.024 wt.-%, most preferably to 0.01 to 0.023 wt.-%, for example equal to or less than 0.02 wt.-% or equal to or less than 0.018 wt.-% or equal to or less than 0.015 wt.-%, based on the active protein content and the total weight of the detergent composition.
  • the reduction of the protease concentration in the detergent composition is helpful to reduce (detrimental) interactions between proteases and cellulases to increase the anti-greying and whitening activity of the detergent composition.
  • the reduction of the protease concentration can also reduce interactions between the protease and further constituents of the detergent composition such as further enzymes different from cellulases, for example lipases and/or amylases.
  • proteases used in the detergent composition according to the invention exhibit enzymatic activity, i.e. they are capable of hydrolyzing peptides and proteins.
  • a protease as used according to the invention is therefore an enzyme which catalyzes the hydrolysis of amide/peptide bonds in protein/peptide substrates and is thus able to cleave proteins or peptides.
  • the protease is preferably a mature protease, i.e. the catalytically active molecule without signal peptide(s) and/or propeptide(s). Unless stated otherwise, the sequences given also refer to mature (processed) enzymes.
  • the protease is a free enzyme. This means that the protease can act directly with all the components of a composition and, if the composition is a liquid composition, that the protease is in direct contact with the solvent of the composition (e.g. water).
  • a composition may contain proteases that form an interaction complex with other molecules or that contain a "coating.”
  • an individual protease molecule or multiple protease molecules may be separated from the other constituents of the composition by a surrounding structure.
  • a separating structure may be formed from, but is not limited to, vesicles such as a micelle or a liposome.
  • the surrounding structure may also be a virus particle, a bacterial cell or a eukaryotic cell.
  • a composition may include cells of Bacillus pumilus or Bacillus subtilis which express the proteases, or cell culture supernatants of such cells.
  • subtilisins BPN' from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis
  • subtilisins PB92 from Bacillus amyloliquefaciens and Carlsberg from Bacillus licheniformis
  • subtilisins 147 and 309 the protease from Bacillus lentus, in particular from Bacillus lentus DSM 5483
  • subtilisin DY subtilisin DY
  • Subtilisin Carlsberg is available in a further developed form under the trade name Alcalase ® from the company Novozymes.
  • Subtilisins 147 and 309 are marketed by Novozymes under the trade names Esperase ® and Savinase ® , respectively.
  • Protease variants are derived from the protease from Bacillus lentus DSM 5483.
  • proteases are, for example, those marketed under the trade names Durazym ® , Relase ® , Everlase ® , Nafizym ® , Natalase ® , Kannase ® , Progress Uno 101L ® and Ovozyme ® from Novozymes, those marketed under the names Purafect ® , Purafect ® OxP, Purafect ® Prime, Excellase ® , Properase ® , Preferenz P100 ® and Preferenz P300 ® from Danisco/DuPont, Lavergy pro 104 LS ® from the company BASF, Protosol ® from Advanced Biochemicals Ltd., Wuxi ® from the company Wuxi Snyder Bioproducts Ltd., Proleather ® and Protease P ® from Amano Pharmaceuticals Ltd., and Proteinase K-16 from the company Kao Corp.
  • Preferred proteases are the proteases from Bacillus gibsonii and Bacillus pumilus that are disclosed in WO 2008/086916 , WO 2007/131656 , WO 2017/215925 , WO 2021/175696 and WO 2021/175697 , for example.
  • Further preferred usable proteases are those disclosed in WO 91/02792 , WO 2008/007319 , WO 93/18140 , WO 01/44452 , GB 1243784 A , WO 96/34946 , WO 02/029024 and WO 03/057246 , for example.
  • proteases are those naturally present in the microorganisms Stenotrophomonas maltophilia, in particular Stenotrophomonas maltophilia K279a, Bacillus intermedius as well as Bacillus sphaericus.
  • Proteases can also be altered, selectively or randomly, by methods known from the prior art, and can thereby be optimized for use in detergent compositions, for example. These methods include, for example, point, deletion or insertion mutagenesis, or fusion with other proteins or protein parts.
  • protease variants can also be used in the detergent compositions according to the invention.
  • the at least one protease is a protease originated from Bacillus lentus or a variant thereof.
  • the at least one protease is an enzyme with proteolytic activity and comprises an amino acid sequence having at least 70%, preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78%, or 79%, more preferably at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88% or 89%, more preferably at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.4%, 98.5%, 98.6%, 98.7% or 98.8% sequence identity to the amino acid sequence set forth in SEQ ID NO:1 over the total length, wherein the amino acid sequence comprises at least one, preferably at least two, more preferably at least three or most preferably four, amino acid substitutions at at least one, preferably at at at at at least
  • the at least one, more preferably at least two, more preferably at least three, most preferably four amino acid substitutions are selected from S3T, V4I, R99E/D and V199I, preferably S3T, V4I, R99E and V199I, based on the numbering of SEQ ID NO:1 over its total length.
  • a further amino acid substitution can be present at position 211 based on the numbering of SEQ ID NO:1 over its total length, preferably the amino acid substitution is 211L.
  • the at least one protease of the detergent composition according to the invention comprises or consists of an amino acid sequence having at least 70%, preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78% or 79%, more preferably at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88% or 89%, more preferably at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.4%, 98.5%, 98.6%, 98.7% or 98.8% sequence identity to the amino acid sequence set forth in SEQ ID NO: 1 over its total length, wherein the amino acid sequence comprises
  • the at least one protease of the detergent composition according to the invention comprises or consists of an amino acid sequence having at least 70%, preferably at least 71%, 72%, 73%, 74%, 75%, 76%, 77%, 78% or 79%, more preferably at least 80%, 81%, 82%, 83%, 84%, 85%, 86%, 87%, 88% or 89%, more preferably at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.4%, 98.5%, 98.6%, 98.7% or 98.8% sequence identity to the amino acid sequence set forth in SEQ ID NO: 1 over its total length, wherein the amino acid sequence comprises
  • the detergent composition according to the invention comprises at least one protease with one of the following amino acid substitution variants:
  • the feature whereby a protease has the given substitutions means that it contains one (of the given) substitution(s) at the relevant position, i.e. at least the given positions are not otherwise mutated or deleted, for example by fragmenting of the protease.
  • the proteases described herein, with the exception of the explicitly mentioned substitutions have the sequence of SEQ ID NO:1, i.e., are 100% identical to the sequence according to SEQ ID NO:1 except for the substituted positions.
  • nucleic acid or amino acid sequences is determined by a sequence comparison.
  • This sequence comparison is based on the commonly used BLAST algorithm established in the prior art (see, for example, Altschul, S.F., Gish, W., Miller, W., Myers, E.W. & Lipman, D.J. (1990) "Basic local alignment search tool.” J. Mol. Biol. 215: 403-410 , and Altschul, Stephan F., Thomas L. Madden, Alejandro A. Schaffer, Jinghui Zhang, Hheng Zhang, Webb Miller, and David J. Lipman (1997): "Gapped BLAST and PSI-BLAST: a new generation of protein database search programs"; Nucleic Acids Res., 25, pp.
  • sequence comparisons using the computer program Vector NTI ® Suite 10.3 (Invitrogen Corporation, 1600 Faraday Avenue, Carlsbad, California, USA) with the specified standard parameters, the AlignX-Modul of which program for the sequence comparisons is based on ClustalW. Unless stated otherwise, the sequence identity given herein is determined by the BLAST algorithm.
  • Such a comparison also allows a statement regarding the similarity of the compared sequences. It is usually given in percent identity, i.e. the proportion of identical nucleotides or amino acid residues in said sequences or in an alignment of corresponding positions.
  • percent identity i.e. the proportion of identical nucleotides or amino acid residues in said sequences or in an alignment of corresponding positions.
  • homology takes conserved amino acid exchanges into account in the case of amino acid sequences, i.e. amino acids having similar chemical activity, since they usually perform similar chemical activities within the protein. Therefore, the similarity between the compared sequences can also be expressed in percent homology or percent similarity.
  • Identity and/or homology information can be provided regarding whole polypeptides or genes or only regarding individual regions. Homologous or identical regions of different nucleic acid or amino acid sequences are therefore defined by matches in the sequences. Such regions often have identical functions.
  • nucleic acid or amino acid sequence can be small and comprise only a few nucleotides or amino acids. Often, such small regions perform essential functions for the overall activity of the protein. It may therefore be expedient to relate sequence matches only to individual, optionally small regions. Unless stated otherwise, however, identity or homology information in the present application relates to the entire length of the particular nucleic acid or amino acid sequence indicated.
  • the indication that an amino acid position corresponds to a numerically designated position in SEQ ID NO:1 therefore means that the corresponding position is associated with the numerically designated position in SEQ ID NO:1 in an alignment as defined above.
  • amino acid exchanges For the description of substitutions relating to exactly one amino acid position (amino acid exchanges), the following convention is used herein: first, the naturally occurring amino acid is designated in the form of the internationally used one-letter code, followed by the associated sequence position and finally the inserted amino acid. Several exchanges within the same polypeptide chain are separated by slashes. For insertions, additional amino acids are named following the sequence position. In the case of deletions, the missing amino acid is replaced by a symbol, for example a star or a dash, or a ⁇ is indicated before the corresponding position.
  • S3T describes the substitution of serine at position 3 by threonine
  • S3TH describes the insertion of histidine following the amino acid threonine at position 3
  • S3* or ⁇ S3 describes the deletion of serine at position 3.
  • the detergent composition comprises at least one amylase.
  • amylases examples include ⁇ -amylases from Bacillus licheniformis , Bacillus amyloliquefaciens or Bacillus stearothermophilus and, in particular, their further developments improved for use in detergents or cleaning agents.
  • the enzyme from Bacillus licheniformis is available from Novozymes under the trade name Termamyl ® and from Danisco/DuPont under the name Purastar ® ST. Further development products of this ⁇ -amylase are available under the trade names Duramyl ® and Termamyl ® ultra (both from Novozymes), Purastar ® OxAm (Danisco/DuPont) and Keistase ® (Daiwa Seiko Inc.).
  • the ⁇ -amylase from Bacillus amyloliquefaciens is marketed by the company Novozymes under the name BAN ® and derived variants of this ⁇ -amylase from Bacillus stearothermophilus under the trade name BSG ® and Novamyl ® (Novozymes). Furthermore, the ⁇ -amylase from Bacillus sp. A 7-7 (DSM 12368) and the cyclodextrin-glucanotransferase (CGTase) from Bacillus agaradherens (DSM 9948) are to be emphasized.
  • amylolytic enzymes can be used, which are disclosed in WO 95/26397 , WO 96/23873 , WO 99/23211 , WO 00/60060 , WO 2003/002711 , WO 2003/054177 , WO 2006/002643 , WO 2007/079938 , WO 2011/100410 and WO 2013/003659 .
  • fusion products of all the molecules mentioned can be used.
  • the further developments of ⁇ -amylases from Aspergillus niger and A. oryzae are suitable, which are available under the trade name Fungamyl ® from Novozymes.
  • Variants of these enzymes obtainable by point mutations can also be used according to the invention.
  • the at least one amylase is an amylase having amylolytic activity and selected from
  • the at least one amylase comprises an amino acid sequence having at least 89%, preferably at least 90%, 90.5%, 91%, 91.5%, 92%, 92.5%, 93%, 93.5%, 94%, 94.5%, 95%, 95.5%, 96%, 96.5%, 97%, 97.5%, 98%, 98.5% or 99% sequence identity to the amino acid sequence set forth in SEQ ID NO:5 over the total length and having at least one deletion at at least one of the positions corresponding to positions 180, 181, 182, 183 and 184 of SEQ ID NO:5, preferably deletions at at least two positions selected from positions 180+181, 181+182, 182+183 and 183+184 of SEQ ID NO:5, more preferably at positions 183+184 of SEQ ID NO:5, in particular the deletions H183*+G184*, and/or at least one substitution at at least one of the positions corresponding to positions 405, 421, 422 and 428 of SEQ ID NO:5 selected from 1405
  • the ⁇ -amylase has the deletions H183*+G184* and additionally the substitutions 1405L, A421H, A422P, and A428T, based on the numbering of SEQ ID NO:5.
  • the amount of amylase in the detergent composition is reduced to equal to or less than 0.0034 wt.-%, most preferably 0.001 to 0.0033 wt.-%, for example equal to or less than 0.003 wt.-% or equal to or less than 0.0028.
  • the reduction of the protease and/or amylase concentration in the detergent composition is helpful to reduce (detrimental) interactions between these enzymes.
  • cellulase refers to an enzyme that catalyzes the hydrolysis of 1,4- ⁇ -D-glucoside bonds in cellulose (cellobiose), and/or lichenin and/or ⁇ -D-glucans. They are often also able to hydrolyze the 1,4-bonds in ⁇ -D-glucans, which have 1,3-bonds in addition to the 1,4-bonds. Cellulases are able to cleave cellulose to ⁇ -glucose. Consequently, cellulases act in particular on cellulose-containing or cellulose derivative-containing residues and catalyze their hydrolysis.
  • the cellulase is an endoglucanase (EC 3.2.1.4). Synonymous names may be used for cellulases, in particular endoglucanase, endo-1,4- ⁇ -glucanase, carboxymethylcellulase, endo-1,4- ⁇ -D-glucanase, ⁇ -1,4-glucanase, ⁇ -1,4-endoglucanhydrolase, celludextrinase or avicelase.
  • the determining factor as to whether an enzyme is a cellulase in the context of the invention is its ability to hydrolyze 1,4- ⁇ -D-glucoside bonds into cellulose.
  • cellulase activity is defined herein as an enzyme that catalyzes the hydrolysis of 1,4- ⁇ -D-glucoside bonds into ⁇ -1,4-glucan (cellulose).
  • Cellulose activity is measured by a standard method, such as the following: Cellulases release glucose from CMC (carboxymethylcellulose). Samples are incubated under defined reaction conditions (100 mM sodium phosphate buffer pH 7.5, 40°C, 15 min) with a substrate (1.25% CMC). Reaction with p-hydroxybenzoic acid hydrazide (PAHBAH) in the presence of bismuth produces a yellow dye that can be determined photometrically at 410 nm. The prerequisite is an alkaline pH during the color reaction. The amount of sugar released corresponding to the coloration is a measure of enzyme activity ( Lever, Anal. Biochem., 1972, 47 & 1977, 81 ).
  • Suitable cellulases include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases are cellulases from the genera Bacillus, Pseudomonas, Humicola, Fusarium, Thielavia, Acremonium, such as fungal cellulases from Humicola insolens, Myceliophthora thermophila and Fusarium oxysporum, which are disclosed in US 4435307 , US 5648263 , US 5691178 , US 5776757 and WO 89/09259 , for example. Particularly suitable cellulases are the alkaline or neutral cellulases with color-maintaining properties.
  • cellulases examples include cellulases, which are described in EP 0495257 , EP 0531372 , WO 96/11262 , WO 96/29397 and WO 98/08940 , for example.
  • Other examples are cellulase variants as described in WO 94/07998 , EP 0531315 , EP 3212777 , EP 3502243 , EP 3653705 , EP 3653706 , US 5457046 , US 5686593 , US 5763254 , WO 95/24471 , WO 98/12307 , WO 99/01544 and WO 2019/122520 , for example.
  • cellulases with endo-1,4-glucanase-activity are described in WO 2002/099091 , e.g., those with a sequence having at least 97% identity with the amino acid sequence of the positions 1 to 773 of SEQ ID NO:2 from WO 2002/099091 .
  • a further example can comprise a GH44-xyloglycanase, e.g., a xyloglucanase enzyme having a sequence of at least 60% identity to the positions 40 to 559 of SEQ ID NO:2 from WO 2001/062903 .
  • cellulases comprise the GH45-cellulases as described in WO 96/29397 and in particular variants thereof having substitutions, insertions and/or deletions at one or more positions corresponding to the following positions of SEQ ID NO:8 from WO 2002/099091 : 2, 4, 7, 8, 10, 13, 15, 19, 20, 21, 25, 26, 29, 32, 33, 34, 35, 37, 40, 42, 42a, 43, 44, 48, 53, 54, 55, 58, 59, 63, 64, 65, 66, 67, 70, 72, 76, 79, 80, 82, 84, 86, 88, 90, 91, 93, 95, 95d, 95h, 95j, 97, 100, 101, 102, 103, 113, 114, 117, 119, 121, 133, 136, 137, 138, 139, 140a, 141, 143a, 145, 146, 147, 150e, 150j, 151, 152, 153,
  • Celluzyme TM Commercially available cellulases comprise Celluzyme TM , Carezyme TM , Carezyme Premium TM , Celluclean TM (e.g. Celluclean TM 5000L and Celluclean TM 4000T), Celluclean Classic TM , Cellusoft TM , Endolase ® , Renozyme ® and Whitezyme TM (Novozymes A/S), Clazinase TM and Puradax HA TM (Genencor International Inc.), KAC-500(B) TM (Kao Corporation), Revitalenz TM 1000, Revitalenz TM 2000 and Revitalenz TM 3000 (DuPont), as well as Ecostone ® and Biotouch ® (AB Enzymes).
  • Celluzyme TM e.g. Celluclean TM 5000L and Celluclean TM 4000T
  • Celluclean Classic TM Cellusoft TM
  • Endolase ® Endolase ®
  • the present detergent composition according to the invention can comprise at least one lipase.
  • Lipases are among the most technically important enzymes of all. Their use for detergents and cleaning agents is industrially established and they are present in virtually all modern, high-performance detergents and cleaning agents.
  • a lipase is an enzyme that catalyzes the hydrolysis of ester bonds in lipid substrates, especially fats and oils. Lipases therefore represent a group of esterases.
  • Lipases are generally versatile enzymes that accept a wide variety of substrates, for example, aliphatic, alicyclic, bicyclic and aromatic esters, thioesters and activated amines. Lipases act against fatty residues in laundry and catalyze their hydrolysis (lipolysis).
  • Lipases with broad substrate spectra are used in particular where inhomogeneous raw materials or substrate mixtures have to be reacted, i.e., for example, in detergents and cleaning agents, since soils can consist of fats and oils with different compositions.
  • the lipases used in detergents or cleaning agents known from the prior art are usually of microbial origin and are usually derived from bacteria or fungi, for example of the genera Thermomyces, Bacillus, Pseudomonas, Acinetobacter, Micrococcus, Humicola, Trichoderma or Trichosporon. Lipases are usually produced by suitable microorganisms using biotechnological methods known per se, for example by transgenic expression hosts of the genera Bacillus or by filamentous fungi.
  • lipases from Thermomyces e.g., from T. lanuginosus (formerly called Humicola lanuginosa ) , as described in EP 0258068 and EP 0305216 , lipases from strains of Pseudomonas (some of these now renamed to Burkholderia ) , e.g., P. alcaligenes or P. pseudoalcaligenes ( EP 0218272 ), P . cepacia ( EP 0331376 ), P. sp. strain SD705 ( WO 95/06720 and WO 96/27002 ), P.
  • wisconsinensis ( WO 96/12012 ), GDSL-type Streptomyces-lipases ( WO 2010/065455 ), lipases from Thermobifida fusca ( WO 2011/084412 ), lipases from Geobacillus stearothermophilus ( WO 2011/084417 ), lipases from Bacillus subtilis ( WO 2011/084599 ), and lipases from Streptomyces griseus ( WO 2011/150157 ) and S. pristinaespiralis ( WO 2012/137147 ).
  • Preferred lipases include, for example, those lipases originally obtainable from Humicola lanuginosa ( Thermomyces lanuginosus ) or those further developed from it, in particular those with one or more of the following amino acid substitutions in the positions D96L, T213R and/or N233R, particularly preferably T213R and N233R, starting from the said lipase.
  • Lipases are commercially available, e.g., from the company Novozymes under the trade names Lipolase ® , Lipolase ® Ultra, LipoPrime ® , Lipozyme ® and Lipex ® .
  • Another advantageously applicable lipase is available under the trade name Lipoclean ® from Novozymes.
  • lipases are, e.g., available from Amano under the names Lipase CE ® , Lipase P ® , Lipase B ® or Lipase CES ® , Lipase AKG ® , Bacillus sp. Lipase ® , Lipase AP ® , Lipase M-AP ® and Lipase AML ® .
  • lipases sometimes referred to as acyltransferases or perhydrolases, e.g., acyltransferases with homology to Candida antarctica lipase A ( WO 2010/111143 ), acyltransferase from Mycobacterium smegmatis ( WO 2005/056782 ), perhydrolases from the CE 7 family ( WO 2009/067279 ), 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 ( WO 2010/100028 ).
  • lipase variants such as those described in EP 0407225 , WO 92/05249 , WO 94/01541 , WO 94/25578 , WO 95/14783 , WO 95/30744 , WO 95/35381 , WO 95/22615 , WO 96/00292 , WO 97/04079 , WO 97/07202 , WO 2000/034450 , WO 2000/060063 , WO 2001/092502 , WO 2007/087508 and WO 2009/109500 .
  • Preferred commercial lipase products include Lipolase TM , Lipex TM , Lipolex TM and Lipoclean TM (Novozymes A/S), Lumafast (Genencor / DuPont) and Lipomax (Gist-Brocades).
  • a suitable lipase comprises an amino acid sequence having at least 70% sequence identity to the amino acid sequence set forth in SEQ ID NO: 6 over the total length thereof and having at least one amino acid substitution at position 83, 86, 87, 89, 90, 92, 93, 95, 113, 174, 202, 203, 205, 206, 207, 208, 209, 211, 227, 252, 253, 256, 258, 259, 260, 264, or 267, each based on the numbering according to SEQ ID NO: 6, preferably such that the lipase comprises at least one of the amino acid substitutions P208N, F211N, P253N, based on the numbering according to SEQ ID NO:6.
  • the lipase according to the invention further comprises the amino acid substitutions T231R and N233R, each based on the numbering according to SEQ ID NO:6.
  • Such lipases which are preferred according to the invention, are indicated in SEQ ID Nos:6-10.
  • the amount of lipase in the detergent composition is increased to equal to or more than 0.003 wt.-% or equal to or more than 0.0033 wt.-% or equal to or more than 0.004 wt.-%, for example 0.0033 to 0.008 wt.-%, based on the active protein content and the total weight of the detergent composition.
  • the lipase concentration is increased to improve the primary washing performance of the detergent composition.
  • Further enzymes that can be comprised in the detergent composition according to the invention is any enzyme which can develop a catalytic activity in the detergent composition according to the invention, in particular, without being limited to that, a hemicellulase, mannanase, tannase, xylanase, xanthanase, xyloglucanase, ⁇ -glucosidase, pectinase, carrageenase, perhydrolase, oxidase, oxidoreductase as well as mixtures thereof.
  • further enzymes can be contained in the detergent composition in an amount of 1 ⁇ 10 -8 to 5 percent by weight, preferably 0.0001 to 1 percent by weight, based on active protein, in each case.
  • the detergent composition is essentially free of or free of any further enzyme, in particular the detergent composition is essentially free of or free of a mannanase.
  • the reduction or removal of mannanase in the detergent composition results in decreased (detrimental) interactions between the mannanase and the protease.
  • the detergent composition according to the invention comprises at least one protease, at least one amylase, at least one cellulase and at least one lipase, in the amounts and ratios as defined herein.
  • the enzymes are comprised in a total amount of from 0.0012 to 5 wt.-%, preferably 0.005 to 1 wt.-%, more preferably 0.008 to 0.8 wt.-%, most preferably 0.01 to 0.8 wt.-%, for example 0.01 to 0.5 or 0.01 to 0.25 wt.-%, based on the active protein content and the total weight of the detergent composition.
  • Protein concentration can be determined by known methods, for example, the BCA (bicinchoninic acid; 2,2'-biquinolyl-4,4'-dicarboxylic acid) method or the Biuret method ( Gornall et al., 1948, J. Biol. Chem., 177:751-766 ).
  • determination of the active protein content can be accomplished by titration of the active sites using a suitable irreversible inhibitor and determination of the residual activity ( Bender et al., 1966, J. Am. Chem. Soc. 88, 24:5890-5913 ).
  • the enzymes to be used may further be formulated together with accompanying substances, such as those derived from fermentation.
  • the enzymes are preferably used as enzyme liquid formulation(s).
  • the enzymes are generally not provided in the form of the pure protein, but rather in the form of stabilized preparations that can be stored and transported.
  • These prepackaged preparations include, for example, the solid preparations obtained by granulation, extrusion or lyophilization or, particularly in the case of liquid or gel form, solutions of the enzymes, advantageously as concentrated as possible, with as little water as possible and/or with stabilizers or other auxiliaries added.
  • the enzymes can be encapsulated for both the solid and liquid dosage forms, for example by spray drying or extrusion of the enzyme solution together with a preferably natural polymer or in the form of capsules, for example those in which the enzymes are enclosed as in a solidified gel or in those of the core-shell type, in which an enzyme-containing core is coated with a water-, air- and/or chemical-impermeable protective layer.
  • Additional active ingredients for example stabilizers, emulsifiers, pigments, bleaching agents or dyes, can be applied in superimposed layers.
  • Such capsules are applied by methods known per se, for example by shaking or rolling granulation or in fluid-bed processes.
  • such granules for example by applying polymeric film formers, are low in dust and stable in storage due to the coating.
  • water-soluble films such as those used in the packaging of detergents and cleaning agents in unit dose form.
  • Such a film allows the enzymes to be released upon contact with water.
  • water soluble refers to a film structure that is preferably completely water soluble.
  • such a film consists of (fully or partially hydrolyzed) polyvinyl alcohol (PVA).
  • the detergent composition according to the invention may comprise one or more surfactants, for example anionic, non-ionic, zwitterionic, amphoteric and/or cationic surfactants, anionic and non-ionic surfactants being significantly preferred for economic reasons and due to the performance spectrum thereof during washing.
  • surfactants for example anionic, non-ionic, zwitterionic, amphoteric and/or cationic surfactants, anionic and non-ionic surfactants being significantly preferred for economic reasons and due to the performance spectrum thereof during washing.
  • Anionic surfactants that are used are those of the sulfonate and sulfate types, for example.
  • Surfactants of the sulfonate type that can be used are preferably C 9-13 alkylbenzene sulfonates, olefin sulfonates, i.e. mixtures of alkene and hydroxyalkane sulfonates, and disulfonates, as obtained, for example, from C 12-18 monoolefins having a terminal or internal double bond by way of sulfonation with gaseous sulfur trioxide and subsequent alkaline or acid hydrolysis of the sulfonation products.
  • Alkane sulfonates obtained from C 12-18 alkanes for example by way of sulfochlorination or sulfoxidation with subsequent hydrolysis or neutralization, are also suitable.
  • the esters of ⁇ -sulfofatty acids are suitable, for example the ⁇ -sulfonated methyl esters of hydrogenated coconut fatty acids, palm kernel fatty acids or tallow fatty acids.
  • Sulfated fatty acid glycerol esters are further suitable anionic surfactants.
  • Fatty acid glycerol esters shall be understood to mean the monoesters, diesters and triesters and mixtures thereof, as they are obtained during preparation by way of the esterification of a monoglycerol with 1 to 3 moles fatty acid or during the transesterification of triglycerides with 0.3 to 2 moles glycerol.
  • Preferred sulfated fatty acid glycerol esters are the sulfation products of saturated fatty acids having 6 to 22 carbon atoms, for example of caproic acid, caprylic acid, capric acid, myristic acid, lauric acid, palmitic acid, stearic acid or behenic acid.
  • alkali salts and in particular the sodium salts of the sulfuric acid half-esters of C 12 -C 18 fatty alcohols for example from coconut fatty alcohol, tallow fatty alcohol, lauryl alcohol, myristyl alcohol, cetyl alcohol or stearyl alcohol, or of C 10 -C 20 oxo alcohols and the half-esters of secondary alcohols having these chain lengths are preferred as alk(en)yl sulfates.
  • Alk(en)yl sulfates of the mentioned chain length that contain a synthetic straight-chain alkyl group prepared on a petrochemical basis and have a degradation behavior similar to that of the adequate compounds based on fat chemical raw materials are also preferred. From a washing perspective, the C 12 -C 16 alkyl sulfates, C 12 -C 15 alkyl sulfates and C 14 -C 15 alkyl sulfates are preferred.
  • the sulfuric acid monoesters of straight-chain or branched C 7-21 alcohols ethoxylated with 1 to 6 mol of ethylene oxide such as 2-methyl-branched C 9-11 alcohols having, on average, 3.5 mol ethylene oxide (EO) or C 12-18 fatty alcohols having 1 to 4 EO, are also suitable.
  • alkyl sulfosuccinic acid which are also referred to as sulfosuccinates or as sulfosuccinic acid esters and represent monoesters and/or diesters of sulfosuccinic acid with alcohols, preferably fatty alcohols, and in particular ethoxylated fatty alcohols.
  • alcohols preferably fatty alcohols, and in particular ethoxylated fatty alcohols.
  • Preferred sulfosuccinates contain C 8-18 fatty alcohol groups or mixtures of these.
  • preferred sulfosuccinates contain a fatty alcohol group that is derived from ethoxylated fatty alcohols, which taken alone represent non-ionic surfactants (for description see below).
  • sulfosuccinates including fatty alcohol groups that derive from ethoxylated fatty alcohols exhibiting a restricted distribution of homologs are particularly preferred.
  • alk(en)yl succinic acid having preferably 8 to 18 carbon atoms in the alk(en)yl chain, or the salts thereof.
  • Saturated fatty acid soaps are suitable, such as the salts of lauric acid, myristic acid, palmitic acid, stearic acid, hydrogenated erucic acid and behenic acid, and in particular soap mixtures derived from natural fatty acids, such as coconut fatty acids, palm kernel fatty acids or tallow fatty acids.
  • the anionic surfactants can be present in the form of the sodium, potassium or ammonium salts thereof, or as soluble salts of organic bases, such as monoethanolamine, diethanolamine or triethanolamine.
  • the anionic surfactants are preferably present in the form of the sodium, potassium or magnesium salts thereof, and in particular in the form of the sodium salts.
  • anionic surfactants There are no general conditions that must be adhered to that would stand in the way of having a degree of freedom in terms of formulation when selecting the anionic surfactants.
  • the use of alkylbenzene sulfonates and fatty alcohol sulfates as anionic surfactants is preferred.
  • Non-ionic surfactants that are preferably used are alkoxylated, advantageously ethoxylated, in particular primary alcohols having preferably 8 to 18 C atoms and, on average, 1 to 12 mols of ethylene oxide (EO) per mol of alcohol, in which the alcohol group can be linear or preferably methyl-branched in the 2 position, or can contain linear and methyl-branched groups in admixture, as are usually present in oxo alcohol groups.
  • EO ethylene oxide
  • alcohol ethoxylates having linear groups of alcohols of native origin having 12 to 18 C atoms, for example of coconut, palm, tallow fatty or oleyl alcohol, and an average of 2 to 8 EO per mol of alcohol are particularly preferred.
  • Examples of preferred ethoxylated alcohols include C 12-14 alcohols having 3 EO or 4 EO, C 9-11 alcohol having 7 EO, C 13-15 alcohols having 3 EO, 5 EO, 7 EO or 8 EO, C 12-18 alcohols having 3 EO, 5 EO or 7 EO, and mixtures thereof, such as mixtures of C 12-14 alcohol having 3 EO and C 12-18 alcohol having 5 EO.
  • the degrees of ethoxylation indicated represent statistical averages that can correspond to an integer or a fractional number for a specific product.
  • Preferred alcohol ethoxylates have a narrowed homolog distribution (narrow range ethoxylates, NRE).
  • fatty alcohols having more than 12 EO can also be used. Examples of these are tallow fatty alcohols having 14 EO, 25 EO, 30 EO, or 40 EO.
  • non-ionic surfactants which are used either as the only non-ionic surfactant or in combination with other non-ionic surfactants, are alkoxylated, preferably ethoxylated or ethoxylated and propoxylated fatty acid alkyl esters, preferably having 1 to 4 carbon atoms in the alkyl chain, in particular fatty acid methyl esters.
  • alkyl polyglycosides Another class of non-ionic surfactants that can advantageously be used is the alkyl polyglycosides (APG).
  • Alkyl polyglycosides that can be used satisfy the general formula RO(G)z, in which R represents a linear or branched, in particular methyl-branched at the 2-position, saturated or unsaturated aliphatic group having 8 to 22, preferably 12 to 18, C atoms, and G is the symbol that represents a glycose unit having 5 or 6 C atoms, preferably glucose.
  • the degree of glycosidation z is between 1.0 and 4.0, preferably between 1.0 and 2.0, and in particular between 1.1 and 1.4.
  • Linear alkyl polyglycosides are preferably used, which is to say alkyl polyglycosides in which the polyglycol group is a glucose group and the alkyl group is an n-alkyl group.
  • Non-ionic surfactants of the amine oxide type for example N-cocoalkyl-N,N-dimethylamine oxide and N-tallow alkyl-N,N-dihydroxyethylamine oxide, and of the fatty acid alkanolamides may also be suitable.
  • the quantity of these non-ionic surfactants is preferably no more than that of the ethoxylated fatty alcohols, in particular no more than half thereof.
  • the polyhydroxy fatty acid amides are known substances that can usually be obtained by the reductive amination of a reducing sugar with ammonia, an alkylamine or an alkanolamine, and subsequent acylation with a fatty acid, a fatty acid alkyl ester or a fatty acid chloride.
  • the group of polyhydroxy fatty acid amides also includes compounds of formula (II), in which R denotes a linear or branched alkyl or alkenyl group having 7 to 12 carbon atoms, R 1 denotes a linear, branched or cyclic alkyl group or an aryl group having 2 to 8 carbon atoms, and R 2 denotes a linear, branched or cyclic alkyl group or an aryl group or an oxy alkyl group having 1 to 8 carbon atoms, C 1-4 alkyl or phenyl groups being preferred, and [Z] denotes a linear polyhydroxyalkyl group, the alkyl chain of which is substituted with at least two hydroxyl groups, or alkoxylated, preferably ethoxylated or propoxylated derivatives of this group.
  • R denotes a linear or branched alkyl or alkenyl group having 7 to 12 carbon atoms
  • R 1 denotes a linear, branched or cycl
  • [Z] is preferably obtained by the reductive amination of a reduced sugar, for example glucose, fructose, maltose, lactose, galactose, mannose or xylose.
  • a reduced sugar for example glucose, fructose, maltose, lactose, galactose, mannose or xylose.
  • the N-alkoxy- or N-aryloxy-substituted compounds can then be converted, by reaction with fatty acid methyl esters in the presence of an alkoxide as the catalyst, to the desired polyhydroxy fatty acid amides, for example according to the teaching of the international application WO-A-95/07331.
  • the detergent composition is free of cationic surfactants.
  • the detergent compositions according to the invention may comprise at least one surfactant in an amount of preferably 1 to 70 wt.-%, more preferably 1 to 60 wt.-% and in particular 1 to 50 wt.-%, based on the total weight of the detergent composition.
  • the detergent composition according to the invention preferably the liquid laundry detergent composition, comprises at least one surfactant, preferably at least one anionic and/or nonionic surfactant, more preferably in an amount of from 1 to 50 wt.-%, preferably 2 to 35 wt.-%, more preferably 5 to 35 wt.-%, most preferably 10 to 30 wt.-%, for example 12 to 30 wt.-% or 15 to 28 wt.-%, based on the total weight of the detergent composition.
  • at least one surfactant preferably at least one anionic and/or nonionic surfactant, more preferably in an amount of from 1 to 50 wt.-%, preferably 2 to 35 wt.-%, more preferably 5 to 35 wt.-%, most preferably 10 to 30 wt.-%, for example 12 to 30 wt.-% or 15 to 28 wt.-%, based on the total weight of the detergent composition.
  • the detergent composition according to the invention further comprises at least one acid, preferably citric acid and/or boric acid or salt thereof.
  • Suitable salts of these acids are known in the art and comprise alkali metal salts as well as salts with ammonium or organic cations. While in the following reference is made to acids, it is understood that the respective embodiments also comprise the respective salts of these acids.
  • the at least one acid is/are comprised in the composition in an amount of from 0.01 to 15 wt.-%, preferably 0.1 to 10 wt.-%, more preferably 0.5 to 4 wt.-%, more preferably 0.9 to 3 wt.-%, most preferably in an amount of less than 2.3 wt.-%, for example less than 2.2 wt.-% such as 2.0 wt.-%, 2.1 wt.-% or 2.09 wt.-%, based on the total weight of the detergent composition.
  • the at least one acid is boric acid, wherein boric acid is comprised in the detergent composition in an amount of from 0.01 to 15wt.-%, preferably 0.1 to 10 wt.-%, more preferably 0.1 to 5 wt.-%, more preferably 0.1 to 3 wt.-%, more preferably 0.1 to 2 wt.-%, more preferably in an amount of less than 1 wt.-%, more preferably less than 0.9 wt.-%, more preferably less than 0.88 wt.-%, more preferably less than 0.85 wt.-%, most preferably less than 0.8 wt.-% such as 0.79 wt.-%, 0.75 wt.- %, 0.70 wt.-% or 0.5 wt.-%, based on the total weight of the detergent composition.
  • boric acid is comprised in the detergent composition in an amount of from 0.01 to 15wt.-%, preferably 0.1 to 10 wt.-%,
  • the detergent composition can also comprise boric acid and citric acid together.
  • citric acid is comprised in the detergent composition in amounts of from 0.01 to 15 wt.-%, preferably 0.1 to 10 wt.-%, more preferably 0.5 to 6 wt.-%, most preferably 0.8 to 1.8 wt.-% such as 1 wt.-%, 1.3 wt.-% or 1.5 wt.-%.
  • citric acid is comprised in amounts of less than 2 wt.-%, preferably less than 1.8 wt.-%, more preferably less than 1.5 wt.-% such as 1.3 wt.-%, based on the total weight of the detergent composition.
  • the detergent composition can be free of boric acid. It is also possible, in various embodiments, that the detergent composition is essentially free or completely free of boron-containing compounds.
  • the detergent composition is a liquid laundry detergent composition, it can comprise more than 40 wt.- % water, preferably 50 to 90 wt.-% and particularly preferably 60 to 80 wt.-% water.
  • the detergent composition according to the invention can also comprise any further constituent that is typical for detergent compositions, in particular for liquid laundry detergent compositions.
  • Suitable further constituents or additives are selected from the group of bleaching agents, complexing agents, builders, preservatives, electrolytes, thickeners, non-aqueous solvents, pH adjusters, alkalis, fragrances, fragrance carriers, fluorescing agents, dyes, hydrotropic substances, suds control agents, silicone oils, anti-redeposition agents, further greying inhibitors, anti-shrink agents, anti-crease agents, dye transfer inhibitors, antimicrobial active ingredients, germicides, fungicides, antioxidants, rheology modifier, rheology stabilizer, corrosion inhibitors, antistatic agents, bittering agents, ironing aids, repellents and impregnating agents, anti-swelling and anti-slip agents, softening components and UV absorbers, preferably from fragrances, dyes, alkalis, preservatives, fluorescing agents, suds control agents, rheology modifier, rheology stabilizer, non-aqueous solvents, builders and thickeners and mixtures thereof
  • the detergent composition may have a pH in the range of from approx. 6 to approx. 11, preferably approx. 6.5 to approx. 10.5, more preferably approx. 7 to approx. 10, in particular approx. 8 to approx. 9 such as 8.6, 8.4 or 8.2, e.g. in a 1 wt.-% solution with deionized water at 20 °C.
  • the detergent composition has a viscosity at 20 °C of 500 to 100,000 mPa ⁇ s, preferably 1000 to 2000 mPa ⁇ s, more preferably 1100 to 1900 mPa ⁇ s such as 1500 mPa ⁇ s, preferably measured with a Brookfield viscometer (spindle 3, speed 20).
  • a further aspect according to the invention is an agent or article, preferably a detergent, more preferably a liquid laundry detergent, comprising or (essentially) consisting of the detergent composition, preferably the liquid laundry detergent composition, as described herein.
  • the detergent composition according to the invention preferably the liquid laundry detergent composition, is an agent or article in unit dose, e.g. pouches, preferably with a water-soluble film.
  • the invention relates to a method for preventing or removing greying of a fabric, comprising contacting said fabric with a composition comprising at least one cellulase, at least one protease and at least one amylase and optionally at least one lipase, preferably with a detergent composition or an agent or article as described herein.
  • a composition comprising at least one cellulase, at least one protease and at least one amylase and optionally at least one lipase, preferably with a detergent composition or an agent or article as described herein.
  • contacting said fabric with said composition, agent or article is carried out during a washing process.
  • fabric includes any type of textile, for example, garments, carpets, and textile furniture surfaces.
  • the at least one protease is present in the composition used in the method in an amount of from 0.001 to 0.1 wt.-%, preferably 0.001 to 0.05 wt.-%, more preferably 0.001 to 0.03 wt.- %, more preferably 0.005 to 0.029 wt.-%, more preferably 0.01 to 0.026 wt.-%, for example equal to or less than 0.024 wt.-%, most preferably 0.01 to 0.023 wt.-%, for example equal to or less than 0.02 wt.- %; and/or the at least one amylase is present in the composition in an amount of from 0.0001 to 0.01 wt.-%, preferably 0.0001 to 0.005 wt.-%, more preferably 0.001 to 0.005 wt.-%, more preferably 0.001 to 0.004 wt.-%, for example equal to or less than 0.0034 wt.-%,
  • composition used in the method comprises
  • the weight ratio of the amount of protease to cellulase is in the range of from 97:3 to 80:20; and/or the weight ratio of the amount of protease to amylase is in the range of from 95:5 to 75:25; and/or the weight ratio of the amount of amylase to cellulase is in the range of from 80:20 to 60:40; preferably
  • the composition used in the method according to the invention comprises at least one protease, at least one amylase, at least one lipase and at least one cellulase.
  • the composition does not comprise any further enzyme, in particular the composition is essentially free of or free of a mannanase.
  • the washing process is a machine-washing process or a hand-washing process, preferably a machine-washing process.
  • the washing process comprises at least one step in which the temperature is between 20 °C and 60 °C, preferably 20 °C and 50 °C, more preferably 20 °C and 40 °C, more preferably 25 °C and 40 °C, most preferably around 30 °C, preferably the washing process is carried out at a temperature between 20 °C and 60 °C, preferably 20 °C and 50 °C, more preferably, 20 °C and 40 °C, more preferably 25 °C and 40 °C, most preferably around 30 °C.
  • the invention relates to the use of at least one cellulase in combination with at least one protease and at least one amylase and optionally at least one lipase for preventing or removing greying of a fabric, preferably in a washing process, more preferably the enzymes are comprised in a detergent composition or an agent or article as described herein.
  • the enzyme amounts and ratios are as described above for detergent compositions according to the invention or for compositions used in and described for the method according to the invention.
  • All embodiments and examples described herein for the detergent composition according to the invention also apply to the agent, to the article, to the method for preventing or removing greying of a fabric and to the use of at least one cellulase in combination with at least one protease and at least one amylase, and vice versa.
  • Table 1 Preferred detergent composition (Gel) according to the invention (detergent composition 3 with 0.1 wt.-% cellulase formulation and enzyme and boric acid optimization).
  • Perfume/Fragrances 1 100 0.63 0.63 Dye/Colorants 1 85 0.00085 0.001 Dye/Colorants 2 85 0.00031161 0.0003666 Anionic surfactant Na-LAS 3.60 Anionic surfactant LAS 96 3.370 3.510174419 Further anionic surfactant 70 6.00 8.571428571
  • Non-ionic surfactant 100 5.2 5.2 Fatty acids, palm kernel oil (soap) 100 1.6 1.6 Alkalis 48 1.962793039 4.089152164 Citric acid 91.4 1.18 1.291028446 Boric acid 100 0.79 0.7900 Preservatives 7.5 0.0075 0.1 Protease formulation 100 0.3 0.3 Lipase formulation 100 0.2 0.2 Amylase formulation 100 0.12 0.12 Cellulase formulation 100 0.1 0.1 Fluorescent whitening agents 90 0.035 0.0389 Suds control agent 20 0.008 0.04 Rheology modifier 30 0.255 0.85 Glycerin 99 2 2.020 Builder 40 0.2 0.5 Sodium Ch
  • Detergent composition 3 with 0.1 wt.-% cellulase formulation and enzyme and boric acid optimization Citric acid 1.3 1.3 1.3 Boric acid 1 1 0.79 Protease formulation 0.55 0.55 0.3 Lipase formulation 0.125 0.125 0.2 Amylase formulation 0.1625 0.1625 0.12 Mannanase formulation 0.0816 0 0 Cellulase formulation 0 0.1 0.1 Table 4: Stability results of detergent composition 3 according to the invention (i.O. means "ok", k.v. means “minimally changed", k.v.-I.v. means “minimally to slightly changed” and I.v.

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WO2025040693A1 (en) * 2023-08-22 2025-02-27 SkyLab AG A cleaning composition comprising a glycosyl hydrolase targeting (1,4)-alpha-d-glucoside bonds and at least one glycosyl hydrolase targeting beta-glycoside bonds

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