WO2015193204A1 - Enzyme treatment composition - Google Patents

Enzyme treatment composition Download PDF

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Publication number
WO2015193204A1
WO2015193204A1 PCT/EP2015/063231 EP2015063231W WO2015193204A1 WO 2015193204 A1 WO2015193204 A1 WO 2015193204A1 EP 2015063231 W EP2015063231 W EP 2015063231W WO 2015193204 A1 WO2015193204 A1 WO 2015193204A1
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WO
WIPO (PCT)
Prior art keywords
fabric
enzymes
stain removal
removal composition
stain
Prior art date
Application number
PCT/EP2015/063231
Other languages
French (fr)
Inventor
Ravine Anthony Gungabissoon
Jordan Todorov Petkov
Original Assignee
Unilever Plc
Unilever N.V.
Conopco, Inc., D/B/A Unilever
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.)
Filing date
Publication date
Application filed by Unilever Plc, Unilever N.V., Conopco, Inc., D/B/A Unilever filed Critical Unilever Plc
Priority to BR112016029722A priority Critical patent/BR112016029722A2/en
Priority to EP15728860.6A priority patent/EP3158045A1/en
Priority to CN201580033105.XA priority patent/CN106459838A/en
Publication of WO2015193204A1 publication Critical patent/WO2015193204A1/en
Priority to ZA2016/08404A priority patent/ZA201608404B/en

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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
    • C11D1/86—Mixtures of anionic, cationic, and non-ionic compounds
    • 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
    • C11D3/26—Organic compounds containing nitrogen
    • C11D3/30—Amines; Substituted amines ; Quaternized amines
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D17/00—Detergent materials or soaps characterised by their shape or physical properties
    • C11D17/04—Detergent materials or soaps characterised by their shape or physical properties combined with or containing other objects
    • C11D17/041—Compositions releasably affixed on a substrate or incorporated into a dispensing means
    • 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
    • C11D3/02—Inorganic compounds ; Elemental compounds
    • C11D3/04—Water-soluble compounds
    • C11D3/046—Salts
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2041—Dihydric alcohols
    • C11D3/2044—Dihydric alcohols linear
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2003—Alcohols; Phenols
    • C11D3/2065—Polyhydric alcohols
    • 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
    • C11D3/20—Organic compounds containing oxygen
    • C11D3/2075—Carboxylic acids-salts thereof
    • C11D3/2086—Hydroxy carboxylic acids-salts thereof
    • 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
    • C11D3/34—Organic compounds containing sulfur
    • C11D3/3427—Organic compounds containing sulfur containing thiol, mercapto or sulfide groups, e.g. thioethers or mercaptales
    • 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
    • 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
    • C11D3/38609—Protease or amylase in solid compositions only
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/02—Anionic compounds
    • C11D1/12—Sulfonic acids or sulfuric acid esters; Salts thereof
    • C11D1/22—Sulfonic acids or sulfuric acid esters; Salts thereof derived from aromatic compounds
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/38—Cationic compounds
    • C11D1/40—Monoamines or polyamines; Salts thereof
    • C—CHEMISTRY; METALLURGY
    • C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
    • C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
    • C11D1/00—Detergent compositions based essentially on surface-active compounds; Use of these compounds as a detergent
    • C11D1/66—Non-ionic compounds
    • C11D1/72—Ethers of polyoxyalkylene glycols
    • C11D2111/12—

Definitions

  • This invention relates to enzymatic stain removal of stains from fabrics.
  • the invention relates to fabric stain removal composition for stain removal by direct application or pre-treatment of a stain on a stained fabric.
  • Enzymes are used in detergent laundry detergent compositions to aid cleaning and stain removal.
  • the objective of the invention is to improve low / ambient temperature enzyme stain removal of stains on stained fabrics.
  • the present invention provides a fabric stain-removal composition comprising the combination of:
  • the invention provides a fabric stain-removal composition comprising the combination of;
  • X1 and X2 are hydrogen bond donor or acceptor groups independently selected from
  • R is a linker independently selected from:
  • said stains comprise biological material, preferably proteinaceous and/or starch material deposited on fabric.
  • the composition is ambient-active.
  • composition comprises one or more surfactants.
  • the invention provides a process for removing a stain from a stained fabric substrate, comprising the step of treating the stain with the composition of the first aspect of the invention.
  • the method takes place in ambient conditions and preferably this is ambient water temperature.
  • the method of the second aspect comprises the step of applying said composition directly to the stained fabric, with or without the addition of water.
  • the step of applying the composition may itself be a main washing process or it may be as a pre- step (as a pre-treatment) to a further, subsequent ('main') washing process steps.
  • Such further, subsequent washing steps main comprise any manual washing process or any washing process in a fabric washing machine.
  • the invention provides a fabric stain removal treatment device comprising a storage chamber for storing the composition of the first aspect of the invention and a treatment member for applying said composition directly to a substrate, preferably using the method of the second aspect.
  • the invention provides use of a diamine compound in the enzymatic removal of fabric stains.
  • the invention provides use of a compound comprising the structure :
  • enzymatic removal of stains present on fabric is enhanced and is effective at lower temperatures.
  • This offers improved laundry (i.e. fabric) cleaning of stained fabrics in regions where ambient water washing is prevalent.
  • Improved washing performance at lower temperatures may help inhibit the adoption of hot water washing in these countries, a rising trend as standards of living increase and more people are able to afford washing machines.
  • the invention provides enzymatic performance of
  • the composition of the invention improves the removal of based stains at ambient temperature and thus may significantly reduce the energy cost for each wash.
  • substrate includes fabric, clothing etc.
  • diamine compound is intended to include any suitable diamine compound including stereoisomeric and racemic forms, derivatives, and substituted derivatives, salts thereof, and any mixtures thereof.
  • the diamine preferably comprises anyone of the following structures:
  • Diaminopropane (Sigma, CAS Number 109-76-2), propane-1 ,2-diamine, propane-1 ,3- diamine, pentane-1 ,3-diamine, 2-aminoethanol, 2-aminopropan-1 -ol, 2-aminobutan-1-ol, 2-aminopentan-1-ol, 2-aminohexan-1-ol, 2-aminodecan-1 -ol, 2-aminoundecan-1-ol, 2- aminododecan-1-ol, 3-aminopropan-1-ol, 2-aminoethanethiol, 2-aminoethanol, 1 - aminopropan-2-ol, 3-aminopropan-1-ol, 4-aminobutan-2-ol, ethane-1 ,2-diol, propane-1 ,2- diol, butane-1 ,2-diol, pentane-1 ,2-diol, hexane-1 ,2-d
  • the compound of the invention is present in any wash liquor in a concentration in the range 0.01 mg/ml - 10mg/ml and more preferably in the range 0.01 - 0.32 mg/ml, more preferably 0.08-0.16 mg/ml.
  • the diamine comprises diaminopropane present in the range 0.1 -10mg/ml (wash liquor) and the enzyme is a protease.
  • the diamine comprises diaminobutane present in the range 0.15-0.62 (wash liquor) and the enzyme is a protease.
  • the diamine comprises diaminobutane present in the range 0.1 - 10 mg/ml (wash liquor) and the enzyme is an amylase.
  • the diamine comprises diaminobutane present in the range 0.15-0.62 (wash liquor) and the enzyme is an amylase.
  • the compound is present in any composition of the invention in a concentration in the range 40 mg - 5000 mg per dose, preferable 320mg - 4000 mg per dose.
  • the composition may be provided as a single dose format or as multiple dose, free flowing format (powder, liquid, gel, paste etc) which is measured out by the consumer using a dosing device.
  • the dose may range from 10 ml to 100ml.
  • concentration within the composition may be higher and the concentration per dose higher than in main wash laundry detergent compositions, so may in the range 300- 5000 mg per dose, preferably 500 mg - 2000 mg per dose.
  • Pre-treatment device dose levels may vary from 0.1 - 10ml.
  • ambient-active is intended to mean less that 25 degrees Celcius and preferably 22 degrees Celcius or less, more preferably 15 degrees or less but always greater than 1 degree Celcius and “active” means effective in achieving stain removal.
  • treatment in the context of enzymatic fabric treatment composition preferably means cleaning and more preferably stain removal.
  • stain removal is measured in terms of Remission units or a Remission index.
  • Stain removal is preferably shown when there is a remission equal to or greater than 2 Remission units and more preferably greater or equal to 5 units. This is represents effective stain removal for a visible (by the human eye) effect.
  • enzyme includes enzyme variants (produced, for example, by recombinant techniques) are included. Examples of such enzyme variants are disclosed, e.g., in EP 251 ,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV). All percentages mentioned herein are by weight calculated on the total composition, unless specified otherwise. The abbreviation 'wt%' is to be understood as % by weight of the total composition. Preferably the pre-treatment composition is ambient-active.
  • the temperature of the wash liquor step of aqueous washing process is therefore less than 40°C and preferably less than 30°C and more preferably less than 25°C and more preferably less than 22°C further more preferably 15°C or less at all times during the washing but excluding drying.
  • Encouraging low temperature wash liquor is advantageous
  • the enzymatic treatment composition is preferably packaged with
  • the low temperatures being preferably less than 40 °C, more preferably less than 30°C even more preferably less than 25°C preferably at 22°C or less most preferably at 15 degrees °C.
  • the invention is especially advantageous for the particular situation where one requires enzymatic cleaning of stains in a ambient temperature cleaning processes (i.e.with ambient temperature wash liquor) but where compositions are unavoidably stored at higher temperatures.
  • Psychrophilic enzymes are effective at low temperatures but are sensitive to raised temperatures due to their flexibility.
  • Mesophilic (and thermophilic) enzymes are stable at raised temperatures, but have reduced performance in low temperature washing conditions.
  • the invention affords low temperature enzymatic cleaning of a substrate using mesophilic enzymes.
  • the enzyme system preferably comprises a mesophilic or thermophilic enzyme system.
  • the enzyme system may alternatively comprise a mesophilic and/or thermophilic and/or psychrophilic enzyme system.
  • Enzymes may be from animal, vegetable, bacterial origin (derived from bacteria) or fungal origin (derived from fungus) however enzymes from bacterial origin are preferred.
  • Chemically modified or protein engineered mutants are included. Genes encoding such enzymes can be transferred from one host to a preferred expression production host which may or may not be the same as the original host.
  • the one or more enzymes preferably comprises a protease.
  • Preferred proteases are serine proteases or metallo proteases, preferably an alkaline microbial protease or a trypsin-like protease.
  • protease enzymes include AlcalaseTM, SavinaseTM, PrimaseTM, DuralaseTM, DyrazymTM, EsperaseTM, EverlaseTM, PolarzymeTM, and KannaseTM, (Novozymes A S), MaxataseTM, MaxacalTM, MaxapemTM, ProperaseTM, PurafectTM, Purafect OxPTM, FN2TM, and FN3TM (Genencor International Inc.).
  • the one or more enzymes preferably comprises an amylase.
  • Suitable amylases include those of bacterial or fungal origin.
  • Amylases include, for example, alpha-amylases obtained from Bacillus, e.g. a special strain of B. Iicheniformis, described in more detail in GB 1 ,296,839, or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060.
  • amylases are DuramylTM, TermamylTM, Termamyl UltraTM, NatalaseTM, StainzymeTM, FungamylTM and BANTM (Novozymes A/S), RapidaseTM and PurastarTM (from Genencor International IncCommercially available amylases include StainzymeTM and ResilienceTM(Novozymes).
  • the one or more enzymes may comprises a protease in combination with an amylase and the diamine compound is underivitised diamine.
  • the enzymes are preferably present at 0.001 - 5% wt more preferably 0.01 - 3%.
  • the composition preferably comprises further enzymes.
  • the composition preferably comprises a lipase; the preferred lipases including so called ' first wash' lipases which comprise a polypeptide having an amino acid sequence which has at least 90 percent sequence identity with the wild-type lipase derived from Humicola lanuginosa strain DSM 4109 and compared to said wild-type lipase, comprises a substitution of an electrically neutral or negatively charged amino acid within 15 A of E1 or Q249 with a positively charged amino acid; and may further comprise:
  • i. comprises a negatively charged amino acid in position E210 of said wild-type lipase
  • ii comprises a negatively charged amino acid in the region corresponding to positions 90-101 of said wild-type lipase
  • iii. comprises a neutral or negatively charged amino acid at a position
  • iv. has a negative charge or neutral charge in the region corresponding to
  • LipexTM Novozymes
  • a similar enzyme from Novozymes but believed to fall outside of the above definition has been disclosed by Novozymes under the name LipocleanTM and this is also preferred.
  • Other possible lipases include lipases from Humicola (synonym Thermomyces), e.g. from other H. lanuginosa (T. lanuginosus) strains or from H. insolens, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp.
  • strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis, a Bacillus lipase, e.g. from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Acta, 1 131 , 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).
  • lipase enzymes include LipolaseTM and Lipolase UltraTM, and the Bacterial enzyme, Lipomax ® ex Genecor. This is a bacterially derived Lipase, of variant M21 L of the lipase of Pseudomonas alcaligenes as described in WO 94/25578 to Gist- Brocades (M. M.M.J. Cox, H.B.M. Lenting, L.J.S.M. Mulleners and J.M. van der Laan).
  • the composition preferably comprises a phospholipase classified as EC 3.1 .1 .4 and/or EC 3.1.1 .32.
  • phospholipase is an enzyme which has activity towards phospholipids.
  • Phospholipids such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1 ) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol.
  • Phospholipases are enzymes which participate in the hydrolysis of phospholipids.
  • phospholipases A1 and A2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid
  • lysophospholipase or phospholipase B
  • Phospholipase C and phospholipase D release diacyl glycerol or phosphatidic acid respectively.
  • the composition preferably comprises a cutinase. classified in EC 3.1 .1.74.
  • the cutinase used according to the invention may be of any origin.
  • Preferably cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
  • the composition preferably comprises a cellulase include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola,
  • Fusarium, Thielavia, Acremonium e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307.
  • Commercially available cellulases include
  • the composition preferably comprises peroxidases/oxidases, especially of bacterial origin. Chemically modified or protein engineered mutants are included.
  • An example of an oxidative bacterium is, but not limited to, are Aeromonas sp wherefrom oxidases can be sou reed.
  • the composition preferably comprises a pectate lyase (also called polygalacturonate lyases) include pectate lyases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as from Bacillus subtilis (Nasser et al. (1993) FEBS Letts. 335:319-326) and Bacillus sp. YA-14 (Kim et al. (1994) Biosci. Biotech. Biochem. 58:947-949).
  • pectate lyase also called polygalacturonate lyases
  • the pectate lyase comprises the pectate lyase disclosed in Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331 -334 and Henrissat et al., (1995) Plant Physiol. 107: 963-976.
  • pectatel lyases are disclosed in WO 99/27083 and WO 99/27084.
  • pectate lyases derived from Bacillus licheniformis
  • US patent no. 6,284,524 which document is hereby incorporated by reference
  • pectate lyase variants are disclosed in WO 02/006442, especially the variants disclosed in the Examples in WO 02/006442 (which document is hereby incorporated by reference).
  • alkaline pectate lyases include BIOPREPTM and SCOURZYMETM L from Novozymes A/S, Denmark.
  • the composition preferably comprises a mannanase:
  • mannanases include mannanases of bacterial and fungal origin.
  • the mannanase is derived from a strain of the filamentous fungus genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus (WO 94/25576).
  • WO 93/24622 discloses a mannanase isolated from Trichoderma reseei. Mannanases have also been isolated from several bacteria, including Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, No. 1 1 , pp.
  • JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp.
  • JP-A-63056289 describes the production of an alkaline, thermostable beta-mannanase.
  • JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase.
  • JP-A-08051975 discloses alkaline beta- mannanases from alkalophilic Bacillus sp. AM-001 .
  • a purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/1 1 164.
  • WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active.
  • mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp., and Humicola insolens disclosed in WO 99/64619.
  • Bacillus sp. mannanases concerned in the Examples in WO 99/64619 examples include MannawayTM available from Novozymes A/S Denmark.
  • the enzyme and any perfume/fragrance or pro-fragrance present may show some interaction and should be chosen such that this interaction is not negative. Some negative interactions may be avoided by encapsulation of one or other of enzyme and pro-fragrance and/or other segregation within the product.
  • composition preferably comprises a surfactant.
  • the surfactant may be a synthetic surfactant or a biosurfactant which is mircrobially synthesized e.g. from bacteria, fungi or other microbe.
  • the biosurfactant preferably comprises a microbially-derived biosurfactant.
  • it comprises a glycolipid biosurfactant which may be a rhamnolipid or sophorolipid or trehalolipid or a
  • the biosurfactant may advantageously comprise a cellobiose, peptide based biosurfactants, lipoproteins and lipopeptides e.g. surfactin, fatty acids e.g. corynomucolic acids (preferably with hydrocarbon chain C12- C14) , phospholipids e.g.
  • Phosphatidylethanolamine produced by Rhodococcus erythropolis grown on n-alkane resulted in the lowering of interfacial tension between water and hexadecane to less than 1 mN m-1 and CMC of 30 mg L-1 (Kretschner et al., 1982) and Spiculisporic acid; polymeric biosurfactants including emulsan, liposan, mannoprotein and polysaccharide-protein complexes.
  • the biosurfactant comprises a rhamnolipid.
  • the detergent compositionccording to the invention comprises a surfactant, preferably a detersive surfactant.
  • a detersive surfactant we mean that the surfactant, or at least one surfactant of any surfactant mixture, provides a detersive, i.e. cleaning effect to textile fabrics treated as part of a laundering process.
  • Other surfactants which may or may not be detersive surfactants, can be used as part of the composition.
  • the detersive surfactant is present by weight in the laundry detergent compositions at a level of from 3 to 85% by weight, preferably from 3 to 60% by weight, more preferably from 3 to 40% by weight, most preferably from 3 to 35% by weight.
  • Additional surfactants can also be incorporated in the laundry compositions of the invention; these may be detersive or non-detersive surfactants.
  • the detersive surfactant comprises anionic surfactant, nonionic surfactant or a mixture of the two. More preferably the detersive surfactant mixture comprises anionic and nonionic surfactants. Cationic surfactant may optionally be present as part of the detersive surfactant.
  • anionic surfactant is present at a level of from 0.1 to 95% by weight, preferably from 1 to 50% by weight, more preferably from 1.5 to 25% by weight based on total weight of surfactants present.
  • Nonionic surfactant if present, is incorporated at a level of from 0.1 to 95% by weight, preferably from 1 to 50% by weight, more preferably from 1 .5 to 25% by weight based on total weight of surfactants present. If a detersive surfactant mixture is used that incorporates both anionic and nonionic surfactants, then preferably the ratio of anionic surfactant to nonionic surfactant is from 10:1 to 1 :10.
  • 'nonionic surfactant' shall be defined as amphiphilic molecules with a molecular weight of less than about 10,000, unless otherwise noted, which are substantially free of any functional groups that exhibit a net charge at the normal wash pH of 6-1 1 .
  • nonionic surfactant may be used.
  • fatty acid alkoxylates especially ethoxylates, having an alkyl chain of from C8-C35, preferably C8-C30, more preferably C10-C24, especially C10-C18 carbon atoms, and having preferably 3 to 25, more preferred 5 to 15 ethylene oxide groups, for example, Neodols from Shell (The Hague, The Netherlands); ethylene oxide/propylene oxide block polymers which may have molecular weight from 1 ,000 to 30,000, for example, Pluronic (trademark) from BASF (Ludwigshafen, Germany); and alkylphenol ethoxylates, for example Triton X-100, available from Dow Chemical (Midland, Mich., USA).
  • nonionic surfactants considered within the scope of this invention include condensates of alkanolamines with fatty acids, such as cocamide DEA, polyol-fatty acid esters, such as the Span series available from Uniqema (Gouda, The Netherlands), ethoxylated polyol-fatty acid esters, such as the Tween series available from Uniqema (Gouda, The Netherlands), alkylpolyglucosides, such as the APG line available from
  • n-alkylpyrrolidones such as the Surfadone series of products marketed by ISP (Wayne, N.J . , USA).
  • 'Anionic surfactants' are defined herein as amphiphilic molecules comprising one or more functional groups that exhibit a net anionic charge when in aqueous solution at the normal wash pH of between 6 and 1 1.
  • Preferred anionic surfactants are the alkali metal salts of organic sulphur reaction products having in their molecular structure an alkyl radical containing from about 6 to 24 carbon atoms and a radical selected from the group consisting of sulphonic and sulphuric acid ester radicals.
  • any anionic surfactant hereinafter described can be used, such as alkyl ether sulphates, soaps, fatty acid ester sulphonates, alkyl benzene sulphonates,
  • sulphosuccinate esters primary alkyl sulphates, olefin sulphonates, paraffin sulphonates and organic phosphate
  • preferred anionic surfactants are the alkali and alkaline earth metal salts of fatty acid carboxylates, fatty alcohol sulphates, preferably primary alkyl sulfates, more preferably they are ethoxylated, for example alkyl ether sulfates; and alkylbenzene sulfonates or mixtures thereof.
  • cationic, amphoteric surfactants and/or zwitterionic surfactants may be present in the compositions according to the invention.
  • Preferred cationic surfactants are quaternary ammonium salts of the general formula Ri R2R3 4 N + X " , for example where Ri is a Ci2-Ci 4 alkyl group, R2 and R3 are methyl groups, R 4 is a 2-hydroxyethyl group, and X " is a chloride ion.
  • This material is available commercially as Praepagen (Trade Mark) HY from Clariant GmbH, in the form of a 40% by weight aqueous solution.
  • the detergent compositionccording to the invention comprises an amphoteric or zwitterionic surfactant.
  • Amphoteric surfactants are molecules that contain both acidic and basic groups and will exist as zwitterions at the normal wash pH of between 6 and 1 1 .
  • an amphoteric or zwitterionic surfactant is present at a level of from 0.1 to 20% by weight, more preferably from 0.25 to 15% by weight, even more preferably from 0.5 to 10% by weight.
  • Suitable zwitterionic surfactants are exemplified as those which can be broadly described as derivatives of aliphatic quaternary ammonium, sulfonium and phosphonium
  • Ri contains an alkyl, alkenyl or hydroxyalkyl group with 8 to 18 carbon atoms, from 0 to 10 ethylene-oxy groups or from 0 to 2 glyceryl units;
  • Y is a nitrogen, sulfur or phosphorous atom;
  • R2 is an alkyl or hydroxyalkyl group with 1 to 3 carbon atoms;
  • x is 1 when Y is a sulfur atom and 2 when Y is a nitrogen or phosphorous atom;
  • R3 is an alkyl or hydroxyalkyl group with 1 to 5 carbon atoms and Z is a radical selected from the group consisting of sulfate, sulfonate, carboxylate, phosphate or phosphonate.
  • Preferred amphoteric surfactants are amine oxides, for example coco dimethyl amine oxide.
  • Preferred zwitterionic surfactants are betaines, and especially amidobetaines.
  • Preferred betaines are Cs to C18 alkyl amidoalkyl betaines, for example coco amido betaine. These may be included as co-surfactants, preferably present in an amount of from 0 to 10 wt %, more preferably 1 to 5 wt %, based on the weight of the total composition.
  • Preferred amphoteric or zwitterionic surfactants for incorporation in the detergent compositionccording to the present invention are betaine surfactants. Examples of these are mentioned in the following list.
  • the sulfatobetaines such as 3-(dodecyldimethylammonium)-1 -propane sulfate; and 2- (cocodimethylammonium)-l-ethane sulfate.
  • the sulfobetaines such as: 3-(dodecyldimethyl-ammonium)-2-hydroxy-1 -propane sulfonate; 3-(tetradecyl-dimethylammonium)-1 -propane sulfonate; 3-(Ci2-Ci 4 alkyl- amidopropyldimethylammonium)-2-hydroxy-1 -propane sulfonate; and 3-
  • carboxybetaines such as (dodecyldimethylammonium) acetate (also known as lauryl betaine); (tetradecyldimethylammonium) acetate (also known as myristyl betaine);
  • oleyldimethylammonium also known as oleyl betaine
  • the sulfoniumbetaines such as: (dodecyldimethylsulfonium) acetate; and 3- (cocodimethyl-sulfonium)-l -propane sulfonate.
  • the phosphoniumbetaines such as 4-(trimethylphosphonium)-1-hexadecane sulfonate; 3-(dodecyldimethylphosphonium)-1-propanesulfonate; and
  • compositions according to the present invention preferably comprise
  • the treatment composition may comprise other ingredients commonly found in detergent liquids. Especially polyester substantive soil release polymers, hydrotropes, opacifiers, colorants, perfumes, other enzymes, other surfactants, microcapsules of ingredients such as perfume or care additives, softeners, polymers for anti redeposition of soil, bleach, bleach activators and bleach catalysts, antioxidants, pH control agents and buffers, thickeners, external structurants for rheology modification, visual cues, either with or without functional ingredients embedded therein and other ingredients known to those skilled in the art.
  • diamine and enzyme combinations in laundry detergent detergent compositions were tested to determine their ability to treat i.e. stains from cotton fabric in various ways. All values throughout are wt%.
  • Figures 1 -2 show the results of diamine compounds in combination with enzymes in tested for ability to treat various fat stains as follows:
  • Figure 1 Cotton fabric soiled with milk, ink and blood (EMPA-1 17) was washed in a range of concentrations of (a) 1 ,4 Diaminobutane dihydrochloride and (b) 1 ,3
  • Diaminopropane with protease enzyme Savinase 16L and Laundry detergent composition for 1 hour at room temperature.
  • the "0" value shows washing in Savinase 16L and Laundry detergent composition without diamine.
  • FIG. 2 Cotton fabric soiled with coloured potato starch (CS-27) was washed in a range of concentrations of (a) 1 ,4 Diaminobutane dihydrochloride and (b) 1 ,3 Diaminopropane with amylase enzyme Stainzyme 12L and Laundry detergent composition for 1 hour at room temperature. The "0" value shows washing in Stainzyme 12L and Laundry detergent composition without diamine.
  • Amylase Stainzyme 12L, 4.25 mg/L working concentration (Novozymes)
  • the soiled fabric discs were pre-washed to remove any residual free stain as follows:
  • the soiled fabrics were washed at 250 rpm for 1 hour at room temperature. After washing, the wash liquor was then removed and fabric washed 4 X 5 mins with 200 ul distilled water on a plate shaker at 250 rpm. The fabric was then left to dry over night at room temperature before scanning.
  • the whiteness of the cloth represents efficacy of the stain treatment composition.
  • the Results are shown in figures 1 and 2.
  • the diamines 1 ,4 Diaminobutane dihydrochloride and 1 ,3 Diaminopropane improve the cleaning of fat soiled fabrics in combination with enzymes Savinase and Stainzyme when included directly in the main wash. Cleaning improvement is dose dependent generally but specifically,
  • Diaminopropane performed better at all concentrations than diaminobutane for the combination with the protease enzyme Savinase (fig 1 )
  • Diaminobutane performed most optimally in the concentration range 0.15-0.62 mg/ml (wash liquor) when in combination with the protease enzyme Savinase (fig
  • a suitable method for testing pre-treatment of soiled fabric with diamines followed by main wash is give as follows by way of example>
  • Test and Control Mixtures are added to a well plate (such as above described) :
  • the soiled fabric is incubated in the pre-treatment solution for 5 mins at room temperature with no agitation.
  • the pre-treatment wash liquor is then removed.
  • the soiled fabric is washed (250 rpm, 1 hour, room temperature) in the following mixture:
  • wash liquor is then removed and fabric washed 4 X 5 mins with 200 ul distilled water on a plate shaker at 250 rpm. The fabric is then left to dry over night at room temperature before visually inspecting, photographing or scanning.

Abstract

An enzymatic fabric treatment composition comprising the combination of:• one or more enzymes; and • one or more diamine compounds. A pretreatment device comprising said composition. A process for removing a stain from a stained fabric. The use of a diamine compound in the removal of a stain from a stained fabric.

Description

ENZYME TREATMENT COMPOSITION
This invention relates to enzymatic stain removal of stains from fabrics. In particular but not exclusively the invention relates to fabric stain removal composition for stain removal by direct application or pre-treatment of a stain on a stained fabric.
Enzymes are used in detergent laundry detergent compositions to aid cleaning and stain removal.
In many climates and in developing countries, laundering is performed at cold or ambient temperatures. These temperatures are a challenge for laundry stain removal products which rely on enzymes which work optimally between 50 - 70 degrees. In the case of modern washing machines, stain removal mainly relies largely on the heating of water above ambient temperatures in the washing machine and this accounts for a large proportion of the laundry related greenhouse gas footprint - which needs reducing for environmental reasons. The objective of the invention is to improve low / ambient temperature enzyme stain removal of stains on stained fabrics.
In a first aspect, the present invention provides a fabric stain-removal composition comprising the combination of:
(i) one or more enzymes; and
(ii) one or more diamine compounds.
In a second aspect the invention provides a fabric stain-removal composition comprising the combination of;
(i) one or more enzymes; and
(ii) one or more compounds comprising the structure of: i
\
R X2
(CH2)n /
CH3
wherein
X1 and X2 are hydrogen bond donor or acceptor groups independently selected from
NH2, OH, SH and NH; and
R is a linker independently selected from:
a. -CH- la. -CH-CH2- c. -CH-CH2-CH2- and n is an integer where n=0 to 10.
Preferably said stains comprise biological material, preferably proteinaceous and/or starch material deposited on fabric.
Preferably the composition is ambient-active.
Preferably the composition comprises one or more surfactants.
In a second aspect, the invention provides a process for removing a stain from a stained fabric substrate, comprising the step of treating the stain with the composition of the first aspect of the invention.
Preferably the method takes place in ambient conditions and preferably this is ambient water temperature. Preferably the method of the second aspect comprises the step of applying said composition directly to the stained fabric, with or without the addition of water. The step of applying the composition may itself be a main washing process or it may be as a pre- step (as a pre-treatment) to a further, subsequent ('main') washing process steps. Such further, subsequent washing steps main comprise any manual washing process or any washing process in a fabric washing machine.
Accordingly, in a third aspect the invention provides a fabric stain removal treatment device comprising a storage chamber for storing the composition of the first aspect of the invention and a treatment member for applying said composition directly to a substrate, preferably using the method of the second aspect.
In a further aspect the invention provides use of a diamine compound in the enzymatic removal of fabric stains.
In a further aspect the invention provides use of a compound comprising the structure :
Figure imgf000004_0001
wherein X1 and X2 are hydrogen bond donor or acceptor groups independently selected from NH2, OH, SH and NH; and R is a linker independently selected from (a). -CH- (b). - CH-CH2- (c). -CH-CH2-CH2- and n is an integer where n=0 to 10;
in the enzymatic removal of fabric stains.
With the invention, enzymatic removal of stains present on fabric is enhanced and is effective at lower temperatures. This offers improved laundry (i.e. fabric) cleaning of stained fabrics in regions where ambient water washing is prevalent. Improved washing performance at lower temperatures may help inhibit the adoption of hot water washing in these countries, a rising trend as standards of living increase and more people are able to afford washing machines. The invention provides enzymatic performance of
proteinaceous and/or starch based soil and/or stains in an ambient temperature cleaning processes (with low temperature wash liquor) without serious consideration to the temperature sensitivity of the enzyme during storage. The enzyme can therefore be selected more freely, on the basis of other considerations. The composition of the invention improves the removal of based stains at ambient temperature and thus may significantly reduce the energy cost for each wash.
As used herein, the term "substrate" includes fabric, clothing etc.
As used herein, the term "diamine compound" is intended to include any suitable diamine compound including stereoisomeric and racemic forms, derivatives, and substituted derivatives, salts thereof, and any mixtures thereof. The diamine preferably comprises anyone of the following structures:
1 ,4 Diaminobutane dihydrochloride (Sigma, CAS Number 333-93-7) ; 1 ,3
Diaminopropane (Sigma, CAS Number 109-76-2), propane-1 ,2-diamine, propane-1 ,3- diamine, pentane-1 ,3-diamine, 2-aminoethanol, 2-aminopropan-1 -ol, 2-aminobutan-1-ol, 2-aminopentan-1-ol, 2-aminohexan-1-ol, 2-aminodecan-1 -ol, 2-aminoundecan-1-ol, 2- aminododecan-1-ol, 3-aminopropan-1-ol, 2-aminoethanethiol, 2-aminoethanol, 1 - aminopropan-2-ol, 3-aminopropan-1-ol, 4-aminobutan-2-ol, ethane-1 ,2-diol, propane-1 ,2- diol, butane-1 ,2-diol, pentane-1 ,2-diol, hexane-1 ,2-diol, octane-1 ,2-diol, decane-1 ,2-diol, dodecane-1 ,2-diol, propane-1 ,3-diol, butane-1 ,3-diol, 2-mercaptoethanol, 1- mercaptopropan-2-ol, 3-mercaptopropan-1 -ol, 2-aminoethanethiol, 2-mercaptoethanol, 3- mercaptopropan-1-ol, ethane-1 ,2-dithiol, propane-1 ,3-dithiol, butane-1 ,3-dithiol.
Preferably the compound of the invention is present in any wash liquor in a concentration in the range 0.01 mg/ml - 10mg/ml and more preferably in the range 0.01 - 0.32 mg/ml, more preferably 0.08-0.16 mg/ml.
Preferably the diamine comprises diaminopropane present in the range 0.1 -10mg/ml (wash liquor) and the enzyme is a protease. Alternatively or additionally, preferably the diamine comprises diaminobutane present in the range 0.15-0.62 (wash liquor) and the enzyme is a protease.
Preferably the diamine comprises diaminobutane present in the range 0.1 - 10 mg/ml (wash liquor) and the enzyme is an amylase. Alternatively or additionally, preferably the diamine comprises diaminobutane present in the range 0.15-0.62 (wash liquor) and the enzyme is an amylase.
Preferably the compound is present in any composition of the invention in a concentration in the range 40 mg - 5000 mg per dose, preferable 320mg - 4000 mg per dose. The composition may be provided as a single dose format or as multiple dose, free flowing format (powder, liquid, gel, paste etc) which is measured out by the consumer using a dosing device. The dose may range from 10 ml to 100ml. For pre-treatment devices for localised stain treatment / pre-treatment, concentration within the composition may be higher and the concentration per dose higher than in main wash laundry detergent compositions, so may in the range 300- 5000 mg per dose, preferably 500 mg - 2000 mg per dose. Pre-treatment device dose levels may vary from 0.1 - 10ml.
The term "ambient-active" is intended to mean less that 25 degrees Celcius and preferably 22 degrees Celcius or less, more preferably 15 degrees or less but always greater than 1 degree Celcius and "active" means effective in achieving stain removal. As used herein the term "treatment" in the context of enzymatic fabric treatment composition preferably means cleaning and more preferably stain removal.
Preferably "stain removal" is measured in terms of Remission units or a Remission index. "Stain removal" is preferably shown when there is a remission equal to or greater than 2 Remission units and more preferably greater or equal to 5 units. This is represents effective stain removal for a visible (by the human eye) effect.
As used herein the term "enzyme" includes enzyme variants (produced, for example, by recombinant techniques) are included. Examples of such enzyme variants are disclosed, e.g., in EP 251 ,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610 (Solvay) and WO 94/02618 (Gist-Brocades NV). All percentages mentioned herein are by weight calculated on the total composition, unless specified otherwise. The abbreviation 'wt%' is to be understood as % by weight of the total composition. Preferably the pre-treatment composition is ambient-active. Accordingly, the temperature of the wash liquor step of aqueous washing process is therefore less than 40°C and preferably less than 30°C and more preferably less than 25°C and more preferably less than 22°C further more preferably 15°C or less at all times during the washing but excluding drying. Encouraging low temperature wash liquor is advantageous
environmentally and financially.
Accordingly, the enzymatic treatment composition is preferably packaged with
instructions to treat a substrate at low temperatures using the composition for example in the method described herein, the low temperatures being preferably less than 40 °C, more preferably less than 30°C even more preferably less than 25°C preferably at 22°C or less most preferably at 15 degrees °C.
The invention is especially advantageous for the particular situation where one requires enzymatic cleaning of stains in a ambient temperature cleaning processes (i.e.with ambient temperature wash liquor) but where compositions are unavoidably stored at higher temperatures. Psychrophilic enzymes are effective at low temperatures but are sensitive to raised temperatures due to their flexibility. Mesophilic (and thermophilic) enzymes are stable at raised temperatures, but have reduced performance in low temperature washing conditions. The invention affords low temperature enzymatic cleaning of a substrate using mesophilic enzymes.
Accordingly, the enzyme system preferably comprises a mesophilic or thermophilic enzyme system. The enzyme system may alternatively comprise a mesophilic and/or thermophilic and/or psychrophilic enzyme system.
Enzymes may be from animal, vegetable, bacterial origin (derived from bacteria) or fungal origin (derived from fungus) however enzymes from bacterial origin are preferred.
Chemically modified or protein engineered mutants are included. Genes encoding such enzymes can be transferred from one host to a preferred expression production host which may or may not be the same as the original host.
The one or more enzymes preferably comprises a protease.
Preferred proteases are serine proteases or metallo proteases, preferably an alkaline microbial protease or a trypsin-like protease.
Commercially available protease enzymes include Alcalase™, Savinase™, Primase™, Duralase™, Dyrazym™, Esperase™, Everlase™, Polarzyme™, and Kannase™, (Novozymes A S), Maxatase™, Maxacal™, Maxapem™, Properase™, Purafect™, Purafect OxP™, FN2™, and FN3™ (Genencor International Inc.).
The one or more enzymes preferably comprises an amylase.
Suitable amylases (alpha and/or beta) include those of bacterial or fungal origin.
Chemically modified or protein engineered mutants are included. Amylases include, for example, alpha-amylases obtained from Bacillus, e.g. a special strain of B. Iicheniformis, described in more detail in GB 1 ,296,839, or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060.
Commercially available amylases are Duramyl™, Termamyl™, Termamyl Ultra™, Natalase™, Stainzyme™, Fungamyl™ and BAN™ (Novozymes A/S), Rapidase™ and Purastar™ (from Genencor International IncCommercially available amylases include Stainzyme™ and Resilience™(Novozymes).
The one or more enzymes may comprises a protease in combination with an amylase and the diamine compound is underivitised diamine. The enzymes are preferably present at 0.001 - 5% wt more preferably 0.01 - 3%.
The composition preferably comprises further enzymes. The composition preferably comprises a lipase; the preferred lipases including so called ' first wash' lipases which comprise a polypeptide having an amino acid sequence which has at least 90 percent sequence identity with the wild-type lipase derived from Humicola lanuginosa strain DSM 4109 and compared to said wild-type lipase, comprises a substitution of an electrically neutral or negatively charged amino acid within 15 A of E1 or Q249 with a positively charged amino acid; and may further comprise:
(I) a peptide addition at the C-terminal;
(II) a peptide addition at the N-terminal;
(III) the following limitations:
i. comprises a negatively charged amino acid in position E210 of said wild-type lipase;
ii comprises a negatively charged amino acid in the region corresponding to positions 90-101 of said wild-type lipase; and
iii. comprises a neutral or negatively charged amino acid at a position
corresponding to N94 of said wild-type lipase; and/or
iv. has a negative charge or neutral charge in the region corresponding to
positions 90-101 of said wild-type lipase; and
v. mixtures thereof.
These are available under the Lipex™ brand from Novozymes. A similar enzyme from Novozymes but believed to fall outside of the above definition has been disclosed by Novozymes under the name Lipoclean™ and this is also preferred. Other possible lipases include lipases from Humicola (synonym Thermomyces), e.g. from other H. lanuginosa (T. lanuginosus) strains or from H. insolens, a Pseudomonas lipase, e.g. from P. alcaligenes or P. pseudoalcaligenes, P. cepacia, P. stutzeri, P. fluorescens, Pseudomonas sp. strain SD 705 (WO 95/06720 and WO 96/27002), P. wisconsinensis, a Bacillus lipase, e.g. from B. subtilis (Dartois et al. (1993), Biochemica et Biophysica Acta, 1 131 , 253-360), B. stearothermophilus (JP 64/744992) or B. pumilus (WO 91/16422).
Commercially available lipase enzymes include Lipolase™ and Lipolase Ultra™, and the Bacterial enzyme, Lipomax ® ex Genecor. This is a bacterially derived Lipase, of variant M21 L of the lipase of Pseudomonas alcaligenes as described in WO 94/25578 to Gist- Brocades (M. M.M.J. Cox, H.B.M. Lenting, L.J.S.M. Mulleners and J.M. van der Laan).
The composition preferably comprises a phospholipase classified as EC 3.1 .1 .4 and/or EC 3.1.1 .32. As used herein, the term phospholipase is an enzyme which has activity towards phospholipids. Phospholipids, such as lecithin or phosphatidylcholine, consist of glycerol esterified with two fatty acids in an outer (sn-1 ) and the middle (sn-2) positions and esterified with phosphoric acid in the third position; the phosphoric acid, in turn, may be esterified to an amino-alcohol. Phospholipases are enzymes which participate in the hydrolysis of phospholipids. Several types of phospholipase activity can be distinguished, including phospholipases A1 and A2 which hydrolyze one fatty acyl group (in the sn-1 and sn-2 position, respectively) to form lysophospholipid; and lysophospholipase (or phospholipase B) which can hydrolyze the remaining fatty acyl group in lysophospholipid. Phospholipase C and phospholipase D (phosphodiesterases) release diacyl glycerol or phosphatidic acid respectively.
The composition preferably comprises a cutinase. classified in EC 3.1 .1.74. The cutinase used according to the invention may be of any origin. Preferably cutinases are of microbial origin, in particular of bacterial, of fungal or of yeast origin.
The composition preferably comprises a cellulase include those of bacterial or fungal origin. Chemically modified or protein engineered mutants are included. Suitable cellulases include cellulases from the genera Bacillus, Pseudomonas, Humicola,
Fusarium, Thielavia, Acremonium, e.g. the fungal cellulases produced from Humicola insolens, Thielavia terrestris, Myceliophthora thermophila, and Fusarium oxysporum disclosed in US 4,435,307, US 5,648,263, US 5,691 ,178, US 5,776,757, WO 89/09259, WO 96/029397, and WO 98/012307. Commercially available cellulases include
Celluzyme™, Carezyme™, Endolase™, Renozyme™ (Novozymes A/S), Clazinase™ and Puradax HA™ (Genencor International Inc.), and KAC-500(B)™ (Kao Corporation).
The composition preferably comprises peroxidases/oxidases, especially of bacterial origin. Chemically modified or protein engineered mutants are included. An example of an oxidative bacterium is, but not limited to, are Aeromonas sp wherefrom oxidases can be sou reed.
The composition preferably comprises a pectate lyase (also called polygalacturonate lyases) include pectate lyases that have been cloned from different bacterial genera such as Erwinia, Pseudomonas, Klebsiella and Xanthomonas, as well as from Bacillus subtilis (Nasser et al. (1993) FEBS Letts. 335:319-326) and Bacillus sp. YA-14 (Kim et al. (1994) Biosci. Biotech. Biochem. 58:947-949). Purification of pectate lyases with maximum activity in the pH range of 8-10 produced by Bacillus pumilus (Dave and Vaughn (1971 ) J. Bacteriol. 108:166-174), B. polymyxa (Nagel and Vaughn (1961 ) Arch. Biochem. Biophys. 93:344-352), B. stearothermophilus (Karbassi and Vaughn (1980) Can. J. Microbiol. 26:377-384), Bacillus sp. (Hasegawa and Nagel (1966) J. Food Sci. 31 :838-845) and Bacillus sp. RK9 (Kelly and Fogarty (1978) Can. J. Microbiol. 24:1 164-1 172) have also been described. Any of the above, as well as divalent cation-independent and/or thermostable pectate lyases, may be used in practicing the invention. In preferred embodiments, the pectate lyase comprises the pectate lyase disclosed in Heffron et al., (1995) Mol. Plant-Microbe Interact. 8: 331 -334 and Henrissat et al., (1995) Plant Physiol. 107: 963-976. Specifically contemplated pectatel lyases are disclosed in WO 99/27083 and WO 99/27084. Other specifically contemplated pectate lyases (derived from Bacillus licheniformis) are disclosed in US patent no. 6,284,524 (which document is hereby incorporated by reference). Specifically contemplated pectate lyase variants are disclosed in WO 02/006442, especially the variants disclosed in the Examples in WO 02/006442 (which document is hereby incorporated by reference). Examples of commercially available alkaline pectate lyases include BIOPREP™ and SCOURZYME™ L from Novozymes A/S, Denmark.
The composition preferably comprises a mannanase: Examples of mannanases (EC 3.2.1 .78) include mannanases of bacterial and fungal origin. In a specific embodiment the mannanase is derived from a strain of the filamentous fungus genus Aspergillus, preferably Aspergillus niger or Aspergillus aculeatus (WO 94/25576). WO 93/24622 discloses a mannanase isolated from Trichoderma reseei. Mannanases have also been isolated from several bacteria, including Bacillus organisms. For example, Talbot et al., Appl. Environ. Microbiol., Vol.56, No. 1 1 , pp. 3505-3510 (1990) describes a beta- mannanase derived from Bacillus stearothermophilus. Mendoza et al., World J. Microbiol. Biotech., Vol. 10, No. 5, pp. 551 -555 (1994) describes a beta-mannanase derived from Bacillus subtilis. JP-A-03047076 discloses a beta-mannanase derived from Bacillus sp. JP-A-63056289 describes the production of an alkaline, thermostable beta-mannanase. JP-A-63036775 relates to the Bacillus microorganism FERM P-8856 which produces beta-mannanase and beta-mannosidase. JP-A-08051975 discloses alkaline beta- mannanases from alkalophilic Bacillus sp. AM-001 . A purified mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/1 1 164. WO 91/18974 describes a hemicellulase such as a glucanase, xylanase or mannanase active. Contemplated are the alkaline family 5 and 26 mannanases derived from Bacillus agaradhaerens, Bacillus licheniformis, Bacillus halodurans, Bacillus clausii, Bacillus sp., and Humicola insolens disclosed in WO 99/64619. Especially contemplated are the Bacillus sp. mannanases concerned in the Examples in WO 99/64619. Examples of commercially available mannanases include Mannaway™ available from Novozymes A/S Denmark.
The enzyme and any perfume/fragrance or pro-fragrance present may show some interaction and should be chosen such that this interaction is not negative. Some negative interactions may be avoided by encapsulation of one or other of enzyme and pro-fragrance and/or other segregation within the product.
Surfactant The composition preferably comprises a surfactant.
The surfactant may be a synthetic surfactant or a biosurfactant which is mircrobially synthesized e.g. from bacteria, fungi or other microbe. The biosurfactant preferably comprises a microbially-derived biosurfactant. Preferably it comprises a glycolipid biosurfactant which may be a rhamnolipid or sophorolipid or trehalolipid or a
mannosylerythritol lipid (MEL). Alternatively, the biosurfactant may advantageously comprise a cellobiose, peptide based biosurfactants, lipoproteins and lipopeptides e.g. surfactin, fatty acids e.g. corynomucolic acids (preferably with hydrocarbon chain C12- C14) , phospholipids e.g. Phosphatidylethanolamine produced by Rhodococcus erythropolis grown on n-alkane resulted in the lowering of interfacial tension between water and hexadecane to less than 1 mN m-1 and CMC of 30 mg L-1 (Kretschner et al., 1982) and Spiculisporic acid; polymeric biosurfactants including emulsan, liposan, mannoprotein and polysaccharide-protein complexes. Preferably the biosurfactant comprises a rhamnolipid.
The detergent compositionccording to the invention comprises a surfactant, preferably a detersive surfactant. By a detersive surfactant we mean that the surfactant, or at least one surfactant of any surfactant mixture, provides a detersive, i.e. cleaning effect to textile fabrics treated as part of a laundering process. Other surfactants, which may or may not be detersive surfactants, can be used as part of the composition.
The detersive surfactant is present by weight in the laundry detergent compositions at a level of from 3 to 85% by weight, preferably from 3 to 60% by weight, more preferably from 3 to 40% by weight, most preferably from 3 to 35% by weight. Additional surfactants can also be incorporated in the laundry compositions of the invention; these may be detersive or non-detersive surfactants. Preferably the detersive surfactant comprises anionic surfactant, nonionic surfactant or a mixture of the two. More preferably the detersive surfactant mixture comprises anionic and nonionic surfactants. Cationic surfactant may optionally be present as part of the detersive surfactant. If present, anionic surfactant is present at a level of from 0.1 to 95% by weight, preferably from 1 to 50% by weight, more preferably from 1.5 to 25% by weight based on total weight of surfactants present. Nonionic surfactant, if present, is incorporated at a level of from 0.1 to 95% by weight, preferably from 1 to 50% by weight, more preferably from 1 .5 to 25% by weight based on total weight of surfactants present. If a detersive surfactant mixture is used that incorporates both anionic and nonionic surfactants, then preferably the ratio of anionic surfactant to nonionic surfactant is from 10:1 to 1 :10. Nonionic surfactant
For the purposes of this disclosure, 'nonionic surfactant' shall be defined as amphiphilic molecules with a molecular weight of less than about 10,000, unless otherwise noted, which are substantially free of any functional groups that exhibit a net charge at the normal wash pH of 6-1 1 .
Any type of nonionic surfactant may be used. Highly preferred are fatty acid alkoxylates, especially ethoxylates, having an alkyl chain of from C8-C35, preferably C8-C30, more preferably C10-C24, especially C10-C18 carbon atoms, and having preferably 3 to 25, more preferred 5 to 15 ethylene oxide groups, for example, Neodols from Shell (The Hague, The Netherlands); ethylene oxide/propylene oxide block polymers which may have molecular weight from 1 ,000 to 30,000, for example, Pluronic (trademark) from BASF (Ludwigshafen, Germany); and alkylphenol ethoxylates, for example Triton X-100, available from Dow Chemical (Midland, Mich., USA).
Other nonionic surfactants considered within the scope of this invention include condensates of alkanolamines with fatty acids, such as cocamide DEA, polyol-fatty acid esters, such as the Span series available from Uniqema (Gouda, The Netherlands), ethoxylated polyol-fatty acid esters, such as the Tween series available from Uniqema (Gouda, The Netherlands), alkylpolyglucosides, such as the APG line available from
Cognis (Dusseldorf, Germany) and n-alkylpyrrolidones, such as the Surfadone series of products marketed by ISP (Wayne, N.J . , USA).
Anionic surfactant
'Anionic surfactants' are defined herein as amphiphilic molecules comprising one or more functional groups that exhibit a net anionic charge when in aqueous solution at the normal wash pH of between 6 and 1 1.
Preferred anionic surfactants are the alkali metal salts of organic sulphur reaction products having in their molecular structure an alkyl radical containing from about 6 to 24 carbon atoms and a radical selected from the group consisting of sulphonic and sulphuric acid ester radicals. Although any anionic surfactant hereinafter described can be used, such as alkyl ether sulphates, soaps, fatty acid ester sulphonates, alkyl benzene sulphonates,
sulphosuccinate esters, primary alkyl sulphates, olefin sulphonates, paraffin sulphonates and organic phosphate; preferred anionic surfactants are the alkali and alkaline earth metal salts of fatty acid carboxylates, fatty alcohol sulphates, preferably primary alkyl sulfates, more preferably they are ethoxylated, for example alkyl ether sulfates; and alkylbenzene sulfonates or mixtures thereof.
Cationic, amphoteric surfactants and/or zwitterionic surfactants
Also cationic, amphoteric surfactants and/or zwitterionic surfactants may be present in the compositions according to the invention.
Preferred cationic surfactants are quaternary ammonium salts of the general formula Ri R2R3 4N+ X", for example where Ri is a Ci2-Ci4 alkyl group, R2 and R3 are methyl groups, R4 is a 2-hydroxyethyl group, and X" is a chloride ion. This material is available commercially as Praepagen (Trade Mark) HY from Clariant GmbH, in the form of a 40% by weight aqueous solution.
In a preferred embodiment the detergent compositionccording to the invention comprises an amphoteric or zwitterionic surfactant. Amphoteric surfactants are molecules that contain both acidic and basic groups and will exist as zwitterions at the normal wash pH of between 6 and 1 1 . Preferably an amphoteric or zwitterionic surfactant is present at a level of from 0.1 to 20% by weight, more preferably from 0.25 to 15% by weight, even more preferably from 0.5 to 10% by weight.
Suitable zwitterionic surfactants are exemplified as those which can be broadly described as derivatives of aliphatic quaternary ammonium, sulfonium and phosphonium
compounds with one long chain group having about 8 to about 18 carbon atoms and at least one water solubilizing radical selected from the group consisting of sulfate, sulfonate, carboxylate, phosphate or phosphonate. A general formula for these compounds is:
Ri(R2)xY+R3Z- wherein Ri contains an alkyl, alkenyl or hydroxyalkyl group with 8 to 18 carbon atoms, from 0 to 10 ethylene-oxy groups or from 0 to 2 glyceryl units; Y is a nitrogen, sulfur or phosphorous atom; R2 is an alkyl or hydroxyalkyl group with 1 to 3 carbon atoms; x is 1 when Y is a sulfur atom and 2 when Y is a nitrogen or phosphorous atom; R3 is an alkyl or hydroxyalkyl group with 1 to 5 carbon atoms and Z is a radical selected from the group consisting of sulfate, sulfonate, carboxylate, phosphate or phosphonate.
Preferred amphoteric surfactants are amine oxides, for example coco dimethyl amine oxide. Preferred zwitterionic surfactants are betaines, and especially amidobetaines. Preferred betaines are Cs to C18 alkyl amidoalkyl betaines, for example coco amido betaine. These may be included as co-surfactants, preferably present in an amount of from 0 to 10 wt %, more preferably 1 to 5 wt %, based on the weight of the total composition.
Preferred amphoteric or zwitterionic surfactants for incorporation in the detergent compositionccording to the present invention are betaine surfactants. Examples of these are mentioned in the following list.
The sulfatobetaines, such as 3-(dodecyldimethylammonium)-1 -propane sulfate; and 2- (cocodimethylammonium)-l-ethane sulfate.
The sulfobetaines, such as: 3-(dodecyldimethyl-ammonium)-2-hydroxy-1 -propane sulfonate; 3-(tetradecyl-dimethylammonium)-1 -propane sulfonate; 3-(Ci2-Ci4 alkyl- amidopropyldimethylammonium)-2-hydroxy-1 -propane sulfonate; and 3-
(cocodimethylammonium)-l -propane sulfonate.
The carboxybetaines, such as (dodecyldimethylammonium) acetate (also known as lauryl betaine); (tetradecyldimethylammonium) acetate (also known as myristyl betaine);
(cocodimethylammonium) acetate (also known as coconut betaine);
(oleyldimethylammonium) acetate (also known as oleyl betaine);
(dodecyloxymethyldimethylammonium) acetate; and (cocoamido- propyldimethylammonium) acetate (also known as cocoamido-propyl betaine or CAPB).
The sulfoniumbetaines, such as: (dodecyldimethylsulfonium) acetate; and 3- (cocodimethyl-sulfonium)-l -propane sulfonate. The phosphoniumbetaines, such as 4-(trimethylphosphonium)-1-hexadecane sulfonate; 3-(dodecyldimethylphosphonium)-1-propanesulfonate; and
2-(dodecyldimethylphosphonium)-1 -ethane sulfate. The compositions according to the present invention preferably comprise
carboxybetaines or sulphobetaines as amphoteric or zwitterionic surfactants, or mixtures thereof. Especially preferred is lauryl betaine.
The treatment composition may comprise other ingredients commonly found in detergent liquids. Especially polyester substantive soil release polymers, hydrotropes, opacifiers, colorants, perfumes, other enzymes, other surfactants, microcapsules of ingredients such as perfume or care additives, softeners, polymers for anti redeposition of soil, bleach, bleach activators and bleach catalysts, antioxidants, pH control agents and buffers, thickeners, external structurants for rheology modification, visual cues, either with or without functional ingredients embedded therein and other ingredients known to those skilled in the art.
The invention will now be further described with reference to the following non-limiting examples as follows:
Examples
In these examples, diamine and enzyme combinations in laundry detergent detergent compositions were tested to determine their ability to treat i.e. stains from cotton fabric in various ways. All values throughout are wt%.
Figures 1 -2 show the results of diamine compounds in combination with enzymes in tested for ability to treat various fat stains as follows: Figure 1 : Cotton fabric soiled with milk, ink and blood (EMPA-1 17) was washed in a range of concentrations of (a) 1 ,4 Diaminobutane dihydrochloride and (b) 1 ,3
Diaminopropane with protease enzyme Savinase 16L and Laundry detergent composition for 1 hour at room temperature. The "0" value shows washing in Savinase 16L and Laundry detergent composition without diamine.
Figure 2: Cotton fabric soiled with coloured potato starch (CS-27) was washed in a range of concentrations of (a) 1 ,4 Diaminobutane dihydrochloride and (b) 1 ,3 Diaminopropane with amylase enzyme Stainzyme 12L and Laundry detergent composition for 1 hour at room temperature. The "0" value shows washing in Stainzyme 12L and Laundry detergent composition without diamine.
End-point Stain Removal Assay
Reagents:
• The following soiled cotton fabric samples were hole punched into discs and
transferred to 300 μΙ 96 well plates:
Protein soil: Milk, Ink, Blood (EMPA-1 17) (Testfabrics Inc)
Starch soil: Coloured Potato Starch (CS-27) (Centre from Testmaterials BV) Fat soils: Violet Dyed Used Frying Fat (CS-46), Coloured Beef Fat (CS-61 ), Fat and Blood (CS-75)
• Laundry detergent composition: Working concentration stock dilution = 1 :428 (i.e. the below stock was diluted 1 :428 times in the wash liquor)
Laundry Detergent Composition
Ingredient % by weight
Non-ionic surfactant Neodol 25-9* 6.2
Alcohol ethoxy sulphate 1 1.8
Linear alkylbenzene sulfonate 6.5
Sodium citrate dihydrate 5.2
Sorbitol 5.0
Propylene Glycol 9.0
Sodium tetraborate pentahydrate 3.0
Minor additives and water balance to 100 *Ci2-Ci5 alkoxylated (9EO) chain group
• Enzymes:
• Protease: Savinase 16L, 2.5 mg/L working concentration (Novozymes)
• Amylase: Stainzyme 12L, 4.25 mg/L working concentration (Novozymes)
• Diamines:
• 1 ,4 Diaminobutane dihydrochloride (Sigma, CAS Number 333-93-7)
• 1 ,3 Diaminopropane (Sigma, CAS Number 109-76-2)
Procedure:
Pre-washing of soiled fabric
The soiled fabric discs were pre-washed to remove any residual free stain as follows:
• 200 μΙ of distilled water was added to each well
· Plates agitated on a plate shaker at 250 rpm for 2 mins
• Water removed
Main wash of soiled fabric with diamines The following Test and Control Mixtures were added to the wells:
• Test Mixture
Laundry detergent composition 100 ul
Distilled Water 60 ul
• Enzyme 20 ul
Diamine* 20 ul • Control Mixture (no diamine negative control )
• Detergent composition 100 ul
• Distilled Water 100 ul
· Enzyme 20 ul
The soiled fabrics were washed at 250 rpm for 1 hour at room temperature. After washing, the wash liquor was then removed and fabric washed 4 X 5 mins with 200 ul distilled water on a plate shaker at 250 rpm. The fabric was then left to dry over night at room temperature before scanning.
(3) Visual inspection of washed fabric
After drying, the soiled fabric 96 well plates were visually inspected and photographed.
The whiteness of the cloth represents efficacy of the stain treatment composition. The Results are shown in figures 1 and 2.
Conclusion
The diamines 1 ,4 Diaminobutane dihydrochloride and 1 ,3 Diaminopropane improve the cleaning of fat soiled fabrics in combination with enzymes Savinase and Stainzyme when included directly in the main wash. Cleaning improvement is dose dependent generally but specifically,
• Diaminopropane performed better at all concentrations than diaminobutane for the combination with the protease enzyme Savinase (fig 1 )
• Diaminobutane performed most optimally in the concentration range 0.15-0.62 mg/ml (wash liquor) when in combination with the protease enzyme Savinase (fig
1 )
• Diaminobutane performed better across the range of concentrations for the
combination with the amylase enzyme (fig 2) • Diaminopropane performed most optimally in the concentration 0.15 - 0.62 mg/ml (wash liquor) in combination with amylase enzyme (fig 2)
A suitable method for testing pre-treatment of soiled fabric with diamines followed by main wash is give as follows by way of example>
The following Test and Control Mixtures are added to a well plate (such as above described) :
• Test Mixture:
• Laundry detergent composition 100 ul
• Distilled Water 80 ul
· Diamine dilution* 20 ul
*The diamines diluted to a final concentration of 5 mg/ml
• Control Mixture (Laundry detergent composition only negative control) · Laundry detergent composition 100 ul
• Distilled Water 100 ul
The soiled fabric is incubated in the pre-treatment solution for 5 mins at room temperature with no agitation. The pre-treatment wash liquor is then removed.
Following pre-treatment, the soiled fabric is washed (250 rpm, 1 hour, room temperature) in the following mixture:
• Laundry detergent composition 100 ul
• Distilled Water 100 ul
After washing, the wash liquor is then removed and fabric washed 4 X 5 mins with 200 ul distilled water on a plate shaker at 250 rpm. The fabric is then left to dry over night at room temperature before visually inspecting, photographing or scanning.

Claims

1. A fabric stain removal composition comprising the combination of:
(i) one or more enzymes; and
(ii) one or more diamine compound compounds.
2. A fabric stain removal composition comprising the structure of:
Xi
\
R X2
(CH2)n / CH3
wherein
X1 and X2 are hydrogen bond donor or acceptor groups independently selected from NH2, OH, SH and NH; and
R is a linker independently selected from:
a. -CH- la. -CH-CH2- c. -CH-CH2-CH2- and n is an integer where n=0 to 10.
3. A fabric stain removal composition according to any of claims 1-2 characterised in that it is ambient-active.
4. A fabric stain removal composition according to any of claims 1 - 3characterised in that it comprises one or more surfactants.
5. A fabric stain removal composition according to any of claims 1 -4 characterised in that the one or more enzymes comprises a protease.
6. A fabric stain removal composition according to any of claims 1 -5 characterised in that the one or more enzymes comprises an amylase.
7. A fabric stain removal composition according to any previous claim characterised in that the diamine comprises diaminopropane.
8. A fabric stain removal composition according to any previous claim characterised in that the diamine comprises diaminobutane.
9. A fabric stain removal composition according to claim 7 characterised in that the diamine comprises diaminopropane and the one or more enzymes comprise a protease.
10. A fabric stain removal composition according to claim 8 characterised in that the diamine comprises diaminobutane and the one or more enzymes comprise an amylase.
1 1 . A pre-treatment device comprising (i) a storage chamber storing the fabric stain
removal composition of any of claims 1-8 and a (i) dispenser for locally applying said fabric stain removal composition to a stain on a fabric.
12. A process for removing a stain from a stained fabric, comprising the step of treating the stain with the composition of any of claims 1-8.
13. A process according to claim 10 characterised in that method takes place in ambient conditions such that any wash liquor is at ambient temperature.
14. A process according to claim 10 or 1 1 characterised in that the composition is applied directly to the stain, said step optionally being a pre-treatment step,
15. A process according to any of claims 10-12 wherein the compound is present in a wash liquor in the range of 0.01 - 10mg/ml.
16. A process according to any of claims 10-13 wherein the step of applying the fabric stain removal composition is a pre-treatment step using the pre-treatment device of claim 9.
17. Use of an diamine compound in combination with one or enzymes, said one or more enzymes being preferably a protease and/or an amylase, in the removal of a stain from a stained fabric.
18. Use of compound comprising the structure:
i
\
R X2
(CH2)n /
CH3
wherein
X1 and X2 are hydrogen bond donor or acceptor groups independently selected from NH2, OH, SH and NH; and R is a linker independently selected from: a. -CH- la. -CH-CH2- c. -CH-CH2-CH2- and n is an integer where n=0 to 10;
in combination with one or enzymes, said one or more enzymes being preferably a protease and/or an amylase, in the removal of a stain from a stained fabric
PCT/EP2015/063231 2014-06-19 2015-06-12 Enzyme treatment composition WO2015193204A1 (en)

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BR112016029722A BR112016029722A2 (en) 2014-06-19 2015-06-12 fabric stain removal composition, pretreatment device, process for removing a stain from a stained fabric and use of a diamine compound
EP15728860.6A EP3158045A1 (en) 2014-06-19 2015-06-12 Enzyme treatment composition
CN201580033105.XA CN106459838A (en) 2014-06-19 2015-06-12 Enzyme treatment composition
ZA2016/08404A ZA201608404B (en) 2014-06-19 2016-12-06 Enzyme treatment composition

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Citations (6)

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Publication number Priority date Publication date Assignee Title
WO1999063034A1 (en) * 1998-06-02 1999-12-09 The Procter & Gamble Company Dishwashing detergent compositions containing organic diamines
WO2000046331A1 (en) * 1999-02-08 2000-08-10 The Procter & Gamble Company Diols and polymeric glycols in dishwashing detergent compositions
WO2001025379A1 (en) * 1999-10-04 2001-04-12 The Procter & Gamble Company Fluid cleaning compositions having high levels of amine oxide
US6365561B1 (en) * 1996-12-20 2002-04-02 Procter & Gamble Company Dishwashing detergent compositions containing organic diamines for improved grease cleaning sudsing, low temperature stability and dissolution
US20030028974A1 (en) * 2001-03-19 2003-02-13 Moe Kevin David Stain removal methods and products associated therewith
US6740627B1 (en) * 1999-02-08 2004-05-25 The Procter & Gamble Company Diols and polymeric glycols in dishwashing detergent compositions

Family Cites Families (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
IL130186A0 (en) * 1996-12-20 2000-06-01 Procter & Gamble Dishwashing detergent compositions containing organic diamines

Patent Citations (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
US6365561B1 (en) * 1996-12-20 2002-04-02 Procter & Gamble Company Dishwashing detergent compositions containing organic diamines for improved grease cleaning sudsing, low temperature stability and dissolution
WO1999063034A1 (en) * 1998-06-02 1999-12-09 The Procter & Gamble Company Dishwashing detergent compositions containing organic diamines
WO2000046331A1 (en) * 1999-02-08 2000-08-10 The Procter & Gamble Company Diols and polymeric glycols in dishwashing detergent compositions
US6740627B1 (en) * 1999-02-08 2004-05-25 The Procter & Gamble Company Diols and polymeric glycols in dishwashing detergent compositions
WO2001025379A1 (en) * 1999-10-04 2001-04-12 The Procter & Gamble Company Fluid cleaning compositions having high levels of amine oxide
US20030028974A1 (en) * 2001-03-19 2003-02-13 Moe Kevin David Stain removal methods and products associated therewith

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