EP3158044B1 - Enzymbehandlungszusammensetzung - Google Patents
Enzymbehandlungszusammensetzung Download PDFInfo
- Publication number
- EP3158044B1 EP3158044B1 EP15728019.9A EP15728019A EP3158044B1 EP 3158044 B1 EP3158044 B1 EP 3158044B1 EP 15728019 A EP15728019 A EP 15728019A EP 3158044 B1 EP3158044 B1 EP 3158044B1
- Authority
- EP
- European Patent Office
- Prior art keywords
- composition
- stain
- arginine
- enzymes
- removal
- 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.)
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- 238000010348 incorporation Methods 0.000 description 1
- 238000004900 laundering Methods 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- AGBQKNBQESQNJD-UHFFFAOYSA-N lipoic acid Chemical compound OC(=O)CCCCC1CCSS1 AGBQKNBQESQNJD-UHFFFAOYSA-N 0.000 description 1
- 238000000691 measurement method Methods 0.000 description 1
- 125000002496 methyl group Chemical group [H]C([H])([H])* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000003094 microcapsule Substances 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 239000003921 oil Substances 0.000 description 1
- JRZJOMJEPLMPRA-UHFFFAOYSA-N olefin Natural products CCCCCCCC=C JRZJOMJEPLMPRA-UHFFFAOYSA-N 0.000 description 1
- 239000003605 opacifier Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- 239000012188 paraffin wax Substances 0.000 description 1
- 239000006072 paste Substances 0.000 description 1
- WTJKGGKOPKCXLL-RRHRGVEJSA-N phosphatidylcholine Chemical compound CCCCCCCCCCCCCCCC(=O)OC[C@H](COP([O-])(=O)OCC[N+](C)(C)C)OC(=O)CCCCCCCC=CCCCCCCCC WTJKGGKOPKCXLL-RRHRGVEJSA-N 0.000 description 1
- 150000008104 phosphatidylethanolamines Chemical class 0.000 description 1
- 150000004714 phosphonium salts Chemical class 0.000 description 1
- 229920001983 poloxamer Polymers 0.000 description 1
- 229920000728 polyester Polymers 0.000 description 1
- 229920001184 polypeptide Polymers 0.000 description 1
- 229920000136 polysorbate Polymers 0.000 description 1
- 229920001592 potato starch Polymers 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
- 102000004196 processed proteins & peptides Human genes 0.000 description 1
- 238000000746 purification Methods 0.000 description 1
- 150000003242 quaternary ammonium salts Chemical class 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000000518 rheometry Methods 0.000 description 1
- 230000000630 rising effect Effects 0.000 description 1
- 102220049163 rs35498994 Human genes 0.000 description 1
- 238000005204 segregation Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 239000000344 soap Substances 0.000 description 1
- 239000011734 sodium Substances 0.000 description 1
- 229910052708 sodium Inorganic materials 0.000 description 1
- RPACBEVZENYWOL-XFULWGLBSA-M sodium;(2r)-2-[6-(4-chlorophenoxy)hexyl]oxirane-2-carboxylate Chemical compound [Na+].C=1C=C(Cl)C=CC=1OCCCCCC[C@]1(C(=O)[O-])CO1 RPACBEVZENYWOL-XFULWGLBSA-M 0.000 description 1
- 230000003381 solubilizing effect Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 238000006467 substitution reaction Methods 0.000 description 1
- 125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
- BDHFUVZGWQCTTF-UHFFFAOYSA-N sulfonic acid Chemical compound OS(=O)=O BDHFUVZGWQCTTF-UHFFFAOYSA-N 0.000 description 1
- RWSOTUBLDIXVET-UHFFFAOYSA-O sulfonium Chemical compound [SH3+] RWSOTUBLDIXVET-UHFFFAOYSA-O 0.000 description 1
- 239000011593 sulfur Substances 0.000 description 1
- 125000004434 sulfur atom Chemical group 0.000 description 1
- 239000001117 sulphuric acid Substances 0.000 description 1
- 235000011149 sulphuric acid Nutrition 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- NJGWOFRZMQRKHT-UHFFFAOYSA-N surfactin Natural products CC(C)CCCCCCCCCC1CC(=O)NC(CCC(O)=O)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)NC(C(C)C)C(=O)NC(CC(O)=O)C(=O)NC(CC(C)C)C(=O)NC(CC(C)C)C(=O)O1 NJGWOFRZMQRKHT-UHFFFAOYSA-N 0.000 description 1
- NJGWOFRZMQRKHT-WGVNQGGSSA-N surfactin C Chemical compound CC(C)CCCCCCCCC[C@@H]1CC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](CC(C)C)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@H](CC(C)C)C(=O)N[C@@H](CC(C)C)C(=O)O1 NJGWOFRZMQRKHT-WGVNQGGSSA-N 0.000 description 1
- 108010075550 termamyl Proteins 0.000 description 1
- RJSZFSOFYVMDIC-UHFFFAOYSA-N tert-butyl n,n-dimethylcarbamate Chemical compound CN(C)C(=O)OC(C)(C)C RJSZFSOFYVMDIC-UHFFFAOYSA-N 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 239000004753 textile Substances 0.000 description 1
- 239000002562 thickening agent Substances 0.000 description 1
- 235000013311 vegetables Nutrition 0.000 description 1
- 230000000007 visual effect Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/26—Organic compounds containing nitrogen
- C11D3/33—Amino carboxylic acids
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/26—Organic compounds containing nitrogen
-
- 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
- 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
- C11D7/00—Compositions of detergents based essentially on non-surface-active compounds
- C11D7/22—Organic compounds
- C11D7/32—Organic compounds containing nitrogen
- C11D7/3245—Aminoacids
-
- 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
- C11D7/00—Compositions of detergents based essentially on non-surface-active compounds
- C11D7/22—Organic compounds
- C11D7/32—Organic compounds containing nitrogen
- C11D7/3254—Esters or carbonates 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
- C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
- C11D2111/10—Objects to be cleaned
- C11D2111/14—Hard surfaces
Definitions
- This invention relates to enzymatic stain removal of stains from substrates.
- the invention relates to a stain removal composition for removal of stains by direct application or pre-treatment of a stain on a stained substrate.
- Enzymes are used in detergent formulations to aid cleaning and stain removal.
- US3707505 discloses an enzyme-bearing detergent compositions which are enhanced in terms of enzyme storage stability by the presence of N-Acyl amino acid and its salts and esters, the N-acyl group being the radical of a fatty acid having 6-20 carbon atoms.
- Example 10 describes a liquid washing detergent obtained by adding 0.1g of protease and 1g. of amylase to a mixture of 15g. of lauryl alcohol ether sulphate, 10g. of alkylamide of coconut fatty acid, 5 g. of ethyl alcohol and 2g. of N-myristoyl-L-arginine butyl ester lactate.
- WO97/45510 describes an acidic cleansing gel including amphoteric or non-ionic surfactants, an acid and gelling agent forming an associative inter-polymer gel network.
- DE1942236 describes detersive compositions containing C4-C11 amino acids optionally containing further carboxyl and/or amino groups and the use of such compositions in the removal of protein stains.
- EP2305785 describes use of specific carboxylic or amino compounds for facilitating the removal of soil from a hard surface.
- the objective of the invention is to improve low / ambient temperature enzyme stain removal of stains on stained substrates such as fabrics and hard surfaces.
- the invention relates to an ambient stain removal composition comprising the combinations of one or more enzymes and one or more arginine compounds.
- the present invention provides an ambient active stain removal composition for removal of stains from stained substrates, the composition comprising the combination of:
- the invention provides use of an arginine alkyl ester in combination with one or more enzymes, in the removal of a stain from a stained substrate under ambient conditions.
- the arginine alkyl ester enhances the enzymatic removal of stains present on fabric 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 arginine alkyl ester improves the removal of based stains at ambient temperature and thus may significantly reduce the energy cost for each wash.
- substrate includes fabric, for example clothing, and other surfaces such as cutlery, crockery and other domestic hard surfaces.
- the terms "arginine ester”/ "arginine alkyl ester” is intended to include stereoisomeric and racemic forms, salts thereof, and any mixtures thereof.
- the arginine alkyl ester 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 arginine alkyl ester is present in any composition of the invention in a concentration in the range 40 mg - 5000 mg per dose, preferably 320mg - 4000 mg per dose.
- the composition may be provided as a single dose format or as multiple dose, free flowing format (for example, powder, liquid, gel, paste) 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 formulations, so may be 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 Celsius and preferably 22 degrees Celsius or less, more preferably 15 degrees or less but always greater than 1 degree Celsius and "active" means effective in achieving stain removal.
- treatment in the context of enzymatic 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).
- the wash liquor has a pH in the range 4 - 9.5.
- 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°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 even be a mesophilic, thermophilic 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 may be selected from the group comprising: amylases, cellulases, lipases, phospholipases, cutinases, esterases, peroxidases/oxidases, oxidoreductases, pectases, lyases, pectate lyases, mannanases and mixtures thereof.
- the one or more enzymes preferably comprises an amylase.
- Suitable amylases 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. licheniformis, described in more detail in GB 1,296,839 , or the Bacillus sp. strains disclosed in WO 95/026397 or WO 00/060060 . Preferably the enzyme is in liquid form when admixed to the detergent composition.
- 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 (Novozymes).
- the enzymes are preferably present at 0.001 - 5%wt more preferably 0.01 - 3%.
- 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:
- 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, 1131, 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 M21L 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.
- 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 .
- cellulases include CelluzymeTM, CarezymeTM, EndolaseTM, RenozymeTM (Novozymes A/S), ClazinaseTM and Puradax HATM (Genencor International Inc.), and KAC-500(B)TM (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 sourced.
- 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 Specifically contemplated pectate lyase variants are disclosed in WO 02/006442 , especially the variants disclosed in the Examples in WO 02/006442 .
- Examples of commercially available alkaline pectate lyases include BIOPREPTM and SCOURZYMETM 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.
- 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. 11, 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.
- mannanase from Bacillus amyloliquefaciens is disclosed in WO 97/11164 .
- 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 .
- Bacillus sp. mannanases concerned in the Examples in WO 99/64619 are especially contemplated.
- mannanases 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.
- the composition preferably comprises a surfactant.
- the surfactant may be a synthetic surfactant.
- the surfactant comprises a biosurfactant which is mircrobially synthesized e.g. from bacteria, fungi or other microbe.
- the biosurfactant comprises a glycolipid biosurfactant which may be a rhamnolipid or sophorolipid or trehalolipid or a mannosylerythritol lipid (MEL).
- 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 composition according 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 6-11.
- nonionic surfactant may be used.
- fatty acid alkoxylates especially ethoxylates, having an alkyl chain of from C 8 -C 35 , preferably C 8 -C 30 , more preferably C 10 -C 24 , especially C 10 -C 18 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 Cognis (Düsseldorf, Germany) and n-alkylpyrrolidones, such as the Surfadone series of products marketed by ISP (Wayne, N.J., USA).
- 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 (Goud
- '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 11.
- Preferred anionic surfactants are the alkali metal salts of organic sulphur reaction products having in their molecular structure an alkyl radical containing from 6 to 24 carbon atoms and a radical selected from the group consisting of sulphonic and sulphuric acid ester radicals.
- 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 R 1 R 2 R 3 R 4 N + X - , for example where R 1 is a C 12 -C 14 alkyl group, R 2 and R 3 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 composition according 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 11.
- 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 8 to 18 carbon atoms and at least one water solubilizing radical selected from the group consisting of sulfate, sulfonate, carboxylate, phosphate or phosphonate.
- R 1 (R 2 ) x Y + R 3 Z - wherein R 1 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; R 2 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; R 3 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 C 8 to C 18 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 composition according 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)-1-ethane sulfate.
- the sulfobetaines such as: 3-(dodecyldimethyl-ammonium)-2-hydroxy-1-propane sulfonate; 3-(tetradecyl-dimethylammonium)-1-propane sulfonate; 3-(C 12 -C 14 alkyl-amidopropyldimethylammonium)-2-hydroxy-1-propane sulfonate; and 3-(cocodimethylammonium)-1-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).
- dodecyldimethylammonium acetate also known as lauryl betaine
- tetradecyldimethylammonium) acetate also known as myristyl betaine
- cocodimethylammonium) acetate also known as coconut betaine
- the sulfoniumbetaines such as: (dodecyldimethylsulfonium) acetate; and 3-(cocodimethyl-sulfonium)-1-propane sulfonate.
- the phosphoniumbetaines such as 4-(trimethylphosphonium)-1-hexadecane sulfonate; 3-(dodecyldimethylphosphonium)-1-propanesulfonate; and 2-(dodecyldimethylphosphonium)-1-ethane sulfate.
- 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 composition comprises enzymes.
- the composition preferably excludes or is at least substantially free of protease and/or amylase.
- composition preferably excludes or is at least substantially free of alkyl amides of coconut fatty acid.
- a suitable laundry application to which the arginine alkyl ester can be added at the levels hereindescribed is as follows Ingredient % by weight of total Composition A Non-ionic surfactant Neodol 25-7 6.2 Anionic surfactant LAS acid 11.8 Anionic surfactant SLES 3EO 6.5 Lauric Fatty Acid P5908 5.2 Glycerol 5.0 Monopropylene Glycol 9.0 Citric acid 3.9 Minors 2.0 Arginine alkyl ester As per dose required Water balance to 100
- Enzyme Stainzyme 5 mg/L 20 ⁇ l
- Laundry detergent composition 5 mg/L 100 ⁇ l Arginine methyl ester dilution* 20 ⁇ l Distilled water 60 ⁇ l *Arginine methyl ester diluted to the following mg/ml concentrations in distilled water: 0.08, 0.16, 0.32, 0.64, 1.28, 2.56 and 5.12
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
Claims (11)
- Umgebungsaktive Fleckenentfernungszusammensetzung zum Entfernen von Flecken von befleckten Substraten, wobei die Zusammensetzung die Kombination(i) einem oder mehreren Enzymen und(ii) einem Argininalkylesterumfasst.
- Zusammensetzung nach Anspruch 1, wobei der Argininalkylester ein Argininmethylester oder ein Argininethylester oder eine Kombination davon ist.
- Zusammensetzung nach Anspruch 1, ferner umfassend ein oder mehrere Tenside.
- Zusammensetzung nach irgendeinem vorhergehenden Anspruch, dadurch gekennzeichnet, dass das eine oder die mehreren Enzyme aus der Gruppe ausgewählt sind, die Amylasen, Cellulasen, Lipasen, Phospholipasen, Cutinasen, Esterasen, Peroxidasen/-oxidasen, Oxidoreduktasen, Pektasen, Lyasen, Pektatlyasen, Mannanasen und Mischungen davon umfasst.
- Vorbehandlungsvorrichtung, umfassend (i) eine Vorratskammer zum Lagern der umgebungsaktiven Fleckenentfernungszusammensetzung nach einem der Ansprüche 1 bis 4 und (ii) einen Spender zum lokalen Auftragen der Fleckenentfernungszusammensetzung auf einen Flecken auf einem Substrat.
- Verfahren zum Entfernen von Flecken von einem befleckten Substrat, umfassend den Schritt des Behandelns des Fleckens mit der Zusammensetzung nach einem der Ansprüche 1 bis 4.
- Verfahren nach Anspruch 6, dadurch gekennzeichnet, dass das Verfahren unter Umgebungsbedingungen abläuft.
- Verfahren nach Anspruch 6 oder 7, wobei die Zusammensetzung direkt auf den Flecken aufgetragen wird.
- Verfahren nach Anspruch 8, wobei das Aufbringen der Zusammensetzung direkt auf den Flecken einen Vorbehandlungsschritt darstellt.
- Verfahren nach einem der Ansprüche 6-9, wobei das Substrat textilen Stoff, Essbesteck, Geschirr und andere häusliche harte Oberflächen umfasst.
- Verwendung eines Argininalkylesters in Kombination mit einem oder mehreren Enzymen zum Entfernen eines Fleckens von einem befleckten Substrat unter Umgebungsbedingungen.
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EP14173222 | 2014-06-20 | ||
PCT/EP2015/063235 WO2015193206A1 (en) | 2014-06-20 | 2015-06-12 | Enzyme treatment composition |
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EP3158044A1 EP3158044A1 (de) | 2017-04-26 |
EP3158044B1 true EP3158044B1 (de) | 2018-06-06 |
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EP (1) | EP3158044B1 (de) |
CN (1) | CN106414694B (de) |
BR (1) | BR112016029564B1 (de) |
TR (1) | TR201808289T4 (de) |
WO (1) | WO2015193206A1 (de) |
ZA (1) | ZA201608406B (de) |
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CN110997890B (zh) * | 2017-07-07 | 2021-11-05 | 宝洁公司 | 包含非烷氧基化酯胺的清洁组合物 |
CA3102399C (en) * | 2018-06-29 | 2023-03-14 | The Procter & Gamble Company | Cleaning compositions comprising esteramines |
WO2024083819A1 (en) * | 2022-10-20 | 2024-04-25 | Novozymes A/S | Lipid removal in detergents |
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DE1942236A1 (de) * | 1969-08-20 | 1971-03-04 | Henkel & Cie Gmbh | Eiweissloesende Wasch-,Waschhilfs- und Reinigungsmittel |
JPS5014651B1 (de) * | 1969-12-30 | 1975-05-29 | ||
AU3144497A (en) * | 1996-05-30 | 1998-01-05 | Salient Science, Inc. | Foaming acidic detergent/cleansing gel |
EP2305785A1 (de) * | 2009-10-02 | 2011-04-06 | Unilever N.V. | Verwendung einer Carboxyl- oder Aminoverbindung als Reinigungshilfe für harte Flächen und Verfahren zur Reinigung von harten Flächen |
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- 2015-06-12 BR BR112016029564-1A patent/BR112016029564B1/pt active IP Right Grant
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CN106414694B (zh) | 2020-05-29 |
EP3158044A1 (de) | 2017-04-26 |
WO2015193206A1 (en) | 2015-12-23 |
ZA201608406B (en) | 2019-03-27 |
BR112016029564A2 (pt) | 2017-08-22 |
CN106414694A (zh) | 2017-02-15 |
BR112016029564B1 (pt) | 2022-07-05 |
TR201808289T4 (tr) | 2018-07-23 |
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