WO2013167613A1 - Care enzyme system - Google Patents
Care enzyme system Download PDFInfo
- Publication number
- WO2013167613A1 WO2013167613A1 PCT/EP2013/059527 EP2013059527W WO2013167613A1 WO 2013167613 A1 WO2013167613 A1 WO 2013167613A1 EP 2013059527 W EP2013059527 W EP 2013059527W WO 2013167613 A1 WO2013167613 A1 WO 2013167613A1
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- WO
- WIPO (PCT)
- Prior art keywords
- care
- enzymes
- enzyme
- low temperature
- auxiliary
- Prior art date
Links
- 102000004190 Enzymes Human genes 0.000 title claims abstract description 90
- 108090000790 Enzymes Proteins 0.000 title claims abstract description 90
- 239000000203 mixture Substances 0.000 claims abstract description 47
- 239000004744 fabric Substances 0.000 claims abstract description 44
- 230000002255 enzymatic effect Effects 0.000 claims abstract description 14
- 229920000742 Cotton Polymers 0.000 claims description 13
- 102000005744 Glycoside Hydrolases Human genes 0.000 claims description 8
- 108010031186 Glycoside Hydrolases Proteins 0.000 claims description 8
- 238000000034 method Methods 0.000 claims description 4
- 239000006187 pill Substances 0.000 claims description 4
- 102000004157 Hydrolases Human genes 0.000 claims description 2
- 108090000604 Hydrolases Proteins 0.000 claims description 2
- 230000001461 cytolytic effect Effects 0.000 claims description 2
- 125000003147 glycosyl group Chemical group 0.000 claims description 2
- 229940088598 enzyme Drugs 0.000 description 63
- 108010059892 Cellulase Proteins 0.000 description 16
- 108010084185 Cellulases Proteins 0.000 description 13
- 102000005575 Cellulases Human genes 0.000 description 13
- 235000000346 sugar Nutrition 0.000 description 10
- 238000005406 washing Methods 0.000 description 8
- 229940106157 cellulase Drugs 0.000 description 7
- 150000008163 sugars Chemical class 0.000 description 7
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- DNIAPMSPPWPWGF-UHFFFAOYSA-N Propylene glycol Chemical compound CC(O)CO DNIAPMSPPWPWGF-UHFFFAOYSA-N 0.000 description 6
- 238000003556 assay Methods 0.000 description 6
- AFYNADDZULBEJA-UHFFFAOYSA-N bicinchoninic acid Chemical compound C1=CC=CC2=NC(C=3C=C(C4=CC=CC=C4N=3)C(=O)O)=CC(C(O)=O)=C21 AFYNADDZULBEJA-UHFFFAOYSA-N 0.000 description 5
- 239000003599 detergent Substances 0.000 description 5
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- 101710178123 Endoglucanase 5 Proteins 0.000 description 3
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- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- KRKNYBCHXYNGOX-UHFFFAOYSA-N citric acid Chemical compound OC(=O)CC(O)(C(O)=O)CC(O)=O KRKNYBCHXYNGOX-UHFFFAOYSA-N 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
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- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
- 108010065511 Amylases Proteins 0.000 description 2
- 102000013142 Amylases Human genes 0.000 description 2
- 101710121765 Endo-1,4-beta-xylanase Proteins 0.000 description 2
- 229920001503 Glucan Polymers 0.000 description 2
- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 2
- 229920000057 Mannan Polymers 0.000 description 2
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- 239000004365 Protease Substances 0.000 description 2
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- 239000008103 glucose Substances 0.000 description 2
- 230000007062 hydrolysis Effects 0.000 description 2
- 238000006460 hydrolysis reaction Methods 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 244000005700 microbiome Species 0.000 description 2
- 239000000344 soap Substances 0.000 description 2
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- 239000010414 supernatant solution Substances 0.000 description 2
- 230000002195 synergetic effect Effects 0.000 description 2
- VXWBQOJISHAKKM-UHFFFAOYSA-N (4-formylphenyl)boronic acid Chemical compound OB(O)C1=CC=C(C=O)C=C1 VXWBQOJISHAKKM-UHFFFAOYSA-N 0.000 description 1
- UHPMCKVQTMMPCG-UHFFFAOYSA-N 5,8-dihydroxy-2-methoxy-6-methyl-7-(2-oxopropyl)naphthalene-1,4-dione Chemical compound CC1=C(CC(C)=O)C(O)=C2C(=O)C(OC)=CC(=O)C2=C1O UHPMCKVQTMMPCG-UHFFFAOYSA-N 0.000 description 1
- 241001019659 Acremonium <Plectosphaerellaceae> Species 0.000 description 1
- 239000004382 Amylase Substances 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 102100032487 Beta-mannosidase Human genes 0.000 description 1
- 108010008885 Cellulose 1,4-beta-Cellobiosidase Proteins 0.000 description 1
- 241000193464 Clostridium sp. Species 0.000 description 1
- GUBGYTABKSRVRQ-CUHNMECISA-N D-Cellobiose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)OC(O)[C@H](O)[C@H]1O GUBGYTABKSRVRQ-CUHNMECISA-N 0.000 description 1
- 241000588724 Escherichia coli Species 0.000 description 1
- LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 1
- 241000223218 Fusarium Species 0.000 description 1
- 241000223221 Fusarium oxysporum Species 0.000 description 1
- 102000004366 Glucosidases Human genes 0.000 description 1
- 108010056771 Glucosidases Proteins 0.000 description 1
- 241000223198 Humicola Species 0.000 description 1
- 241001480714 Humicola insolens Species 0.000 description 1
- 102000004882 Lipase Human genes 0.000 description 1
- 108090001060 Lipase Proteins 0.000 description 1
- 239000004367 Lipase Substances 0.000 description 1
- 239000007993 MOPS buffer Substances 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 102000004316 Oxidoreductases Human genes 0.000 description 1
- 108090000854 Oxidoreductases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 108700020962 Peroxidase Proteins 0.000 description 1
- 102000003992 Peroxidases Human genes 0.000 description 1
- 102000015439 Phospholipases Human genes 0.000 description 1
- 108010064785 Phospholipases Proteins 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 description 1
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 0.000 description 1
- 241001313536 Thermothelomyces thermophila Species 0.000 description 1
- 241001494489 Thielavia Species 0.000 description 1
- 241001495429 Thielavia terrestris Species 0.000 description 1
- GSEJCLTVZPLZKY-UHFFFAOYSA-N Triethanolamine Chemical compound OCCN(CCO)CCO GSEJCLTVZPLZKY-UHFFFAOYSA-N 0.000 description 1
- 229920002000 Xyloglucan Polymers 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- LUEWUZLMQUOBSB-ZLBHSGTGSA-N alpha-maltotetraose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@@H]1O[C@@H]1[C@@H](CO)O[C@H](O[C@@H]2[C@H](O[C@H](O[C@@H]3[C@H](O[C@H](O)[C@H](O)[C@H]3O)CO)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O LUEWUZLMQUOBSB-ZLBHSGTGSA-N 0.000 description 1
- 150000001413 amino acids Chemical class 0.000 description 1
- 239000002280 amphoteric surfactant Substances 0.000 description 1
- 229940025131 amylases Drugs 0.000 description 1
- 239000003945 anionic surfactant Substances 0.000 description 1
- 239000004599 antimicrobial Substances 0.000 description 1
- 230000001580 bacterial effect Effects 0.000 description 1
- OCIBBXPLUVYKCH-FYTDUCIRSA-N beta-D-cellohexaose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3[C@H](O[C@@H](O[C@@H]4[C@H](O[C@@H](O[C@@H]5[C@H](O[C@@H](O)[C@H](O)[C@H]5O)CO)[C@H](O)[C@H]4O)CO)[C@H](O)[C@H]3O)CO)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O OCIBBXPLUVYKCH-FYTDUCIRSA-N 0.000 description 1
- 108010055059 beta-Mannosidase Proteins 0.000 description 1
- 239000004327 boric acid Substances 0.000 description 1
- OCIBBXPLUVYKCH-UHFFFAOYSA-N cellopentanose Natural products OC1C(O)C(O)C(CO)OC1OC1C(CO)OC(OC2C(OC(OC3C(OC(OC4C(OC(OC5C(OC(O)C(O)C5O)CO)C(O)C4O)CO)C(O)C3O)CO)C(O)C2O)CO)C(O)C1O OCIBBXPLUVYKCH-UHFFFAOYSA-N 0.000 description 1
- FTNIPWXXIGNQQF-XHCCAYEESA-N cellopentaose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@H](O[C@@H](O[C@@H]3[C@H](O[C@@H](O[C@@H]4[C@H](OC(O)[C@H](O)[C@H]4O)CO)[C@H](O)[C@H]3O)CO)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FTNIPWXXIGNQQF-XHCCAYEESA-N 0.000 description 1
- FYGDTMLNYKFZSV-ZWSAEMDYSA-N cellotriose Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CO)O[C@H]1O[C@@H]1[C@@H](CO)O[C@@H](O[C@@H]2[C@H](OC(O)[C@H](O)[C@H]2O)CO)[C@H](O)[C@H]1O FYGDTMLNYKFZSV-ZWSAEMDYSA-N 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 239000008139 complexing agent Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 230000007797 corrosion Effects 0.000 description 1
- 238000005260 corrosion Methods 0.000 description 1
- 235000014113 dietary fatty acids Nutrition 0.000 description 1
- WWYHAQDAMPXWSI-UHFFFAOYSA-N dodecan-1-ol;methane Chemical compound C.CCCCCCCCCCCCO WWYHAQDAMPXWSI-UHFFFAOYSA-N 0.000 description 1
- 239000000975 dye Substances 0.000 description 1
- 108010005965 endoglycoceramidase Proteins 0.000 description 1
- 239000002979 fabric softener Substances 0.000 description 1
- 239000000194 fatty acid Substances 0.000 description 1
- 229930195729 fatty acid Natural products 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 125000002791 glucosyl group Chemical group C1([C@H](O)[C@@H](O)[C@H](O)[C@H](O1)CO)* 0.000 description 1
- 150000004676 glycans Chemical class 0.000 description 1
- 239000008187 granular material Substances 0.000 description 1
- 239000003752 hydrotrope Substances 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 108010076363 licheninase Proteins 0.000 description 1
- 235000019421 lipase Nutrition 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- 239000002736 nonionic surfactant Substances 0.000 description 1
- 150000002482 oligosaccharides Polymers 0.000 description 1
- 230000003287 optical effect Effects 0.000 description 1
- 108010087558 pectate lyase Proteins 0.000 description 1
- HXITXNWTGFUOAU-UHFFFAOYSA-N phenylboronic acid Chemical class OB(O)C1=CC=CC=C1 HXITXNWTGFUOAU-UHFFFAOYSA-N 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 229920005862 polyol Polymers 0.000 description 1
- 150000003077 polyols Chemical class 0.000 description 1
- 229920001282 polysaccharide Polymers 0.000 description 1
- 239000005017 polysaccharide Substances 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 239000003755 preservative agent Substances 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 239000003352 sequestering agent Substances 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
- ODBPOHVSVJZQRX-UHFFFAOYSA-M sodium;[2-[2-[bis(phosphonomethyl)amino]ethyl-(phosphonomethyl)amino]ethyl-(phosphonomethyl)amino]methyl-hydroxyphosphinate Chemical compound [Na+].OP(=O)(O)CN(CP(O)(O)=O)CCN(CP(O)(=O)O)CCN(CP(O)(O)=O)CP(O)([O-])=O ODBPOHVSVJZQRX-UHFFFAOYSA-M 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 239000013042 solid detergent Substances 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000000758 substrate Substances 0.000 description 1
- 150000005846 sugar alcohols Chemical class 0.000 description 1
- 229910021653 sulphate ion Inorganic materials 0.000 description 1
- 239000000375 suspending agent Substances 0.000 description 1
- 239000002888 zwitterionic surfactant Substances 0.000 description 1
Classifications
-
- D—TEXTILES; PAPER
- D06—TREATMENT OF TEXTILES OR THE LIKE; LAUNDERING; FLEXIBLE MATERIALS NOT OTHERWISE PROVIDED FOR
- D06M—TREATMENT, NOT PROVIDED FOR ELSEWHERE IN CLASS D06, OF FIBRES, THREADS, YARNS, FABRICS, FEATHERS OR FIBROUS GOODS MADE FROM SUCH MATERIALS
- D06M16/00—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic
- D06M16/003—Biochemical treatment of fibres, threads, yarns, fabrics, or fibrous goods made from such materials, e.g. enzymatic with enzymes or microorganisms
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D3/00—Other compounding ingredients of detergent compositions covered in group C11D1/00
- C11D3/16—Organic compounds
- C11D3/38—Products with no well-defined composition, e.g. natural products
- C11D3/386—Preparations containing enzymes, e.g. protease or amylase
- C11D3/38645—Preparations containing enzymes, e.g. protease or amylase containing cellulase
Definitions
- the present invention concerns combinations of fabric care enzymes, and in particular but not exclusively fabric care enzymes in a fabric treatment
- WO95/02675 discloses detergent compositions comprising cellulases capable of providing improved particulate soil removal and cellulases providing a colour clarification. Disclosed are compositions comprising a first cellulase component having retaining type activity and being capable of particulate soil removal a second cellulase component having multiple domains comprising at least one non-catalytic domain attached to a catalytic domain and being capable of colour clarification.
- the present invention provides a low temperature active enzymatic fabric treatment composition comprising the combination of:
- the present invention provides a low temperature enzymatic fabric treatment process comprising the step of treating a fabric with the
- composition of the first aspect of the invention is a composition of the first aspect of the invention.
- the present invention provides use of an auxiliary care enzyme in combination with a primary care enzyme in the treatment of fabrics for a care benefit.
- care of the fabric is improved using a low level of fabric care enzyme whose performance is synergistically improved at low temperature by the use of an auxiliary care enzyme.
- the total amount of the enzymes of the invention ie. the total amount of the primary care enzyme and the auxiliary care enzyme is 0.01 - 1 .75 mg per Litre of the wash liquor
- Washing machines vary in wash liquor volume from 10 L to 48 L. Accordingly the total amount of enzymes of the invention per dose may be from 0.1 - 84 mg .
- the wash liquor may be around 4 - 5 litres in which case the dose may be 0.04 - 8.75 mg of total enzymes of the invention.
- the amount of detergent composition per dose will itself vary (e.g. 35 ml, 10 ml ) depending on water levels, concentration of e.g. surfactants.
- the primary care enzyme may be 0.003 mg/L of wash liquor.
- the auxiliary care enzyme is therefore present either in equal weight (of enzyme protein) or, more preferably greater amounts than the primary care enzyme.
- the primary care enzyme and the auxiliary care enzyme are present in a weight ratio of enzyme protein in the range of from 1 : 1 to 1 :29, more preferably 1 :1 to 1 :9 more preferably 1 :5, more preferably 1 :1 .9.
- the preferred ranges of the invention exclude 1 :30, 1 :10 and 1 :2.
- the one or more primary care enzymes comprises one or more enzymes of the Glycoside Hydrolase Family 45.
- the one or more primary care enzymes comprises one or cellulolytic enzymes (commonly known as cellulases but not restricted to the class
- the one or more auxiliary care enzymes preferably comprise one or more glycosyl hydrolases of Family 5 and/or Family 7.
- Primary care enzymes means enzymes active at restoring colour to fabrics by removing fuzz and pills from the surface of the fabric.
- care benefit means restoration of colour to or improvement of feel of fabrics by removing fuzz and pills from the surface of the fabric.
- auxiliary care enzymes means any enzyme which is active to hydrolyse cellooligosaccharides.
- “Low temperature active” means active at temperatures of 25 degrees Celcius or lower.
- “Cellooligosaccharides” means any subchain of cellulose which is a reaction product of the hydrolysis cellulose by the primary care enzyme.
- DP means degrees of polymerisation).
- Glycoside Hydrolase Family means any Glycoside Hydrolase Family
- Glycoside Hydrolase Family 5" includes the retaining enzymes of chitosanase (EC 3.2.1 .132); ⁇ -mannosidase (EC 3.2.1 .25); cellulase (EC 3.2.1 .4); glucan ⁇ - 1 ,3-glucosidase (EC 3.2.1 .58); licheninase (EC 3.2.1 .73); glucan endo-1 ,6- ⁇ - glucosidase (EC 3.2.1 .75); mannan endo- » -1 ,4-mannosidase (EC 3.2.1 .78);
- endo- » -1 ,4-xylanase (EC 3.2.1 .8); cellulose ⁇ -1 ,4-cellobiosidase (EC 3.2.1 .91 ); ⁇ - 1 ,3-mannanase (EC 3.2.1 .-); xyloglucan-specific endo- » -1 ,4-glucanase (EC 3.2.1 .151 ); mannan transglycosylase (EC 2.4.1 .-); endo- » -1 ,6-galactanase (EC 3.2.1 .164); endoglycoceramidase (EC 3.2.1 .123); ⁇ -primeverosidase (EC 3.2.1 .8); cellulose ⁇ -1 ,4-cellobiosidase (EC 3.2.1 .91 ); ⁇ - 1 ,3-mannanase (EC 3.2.1 .-); xyloglucan-specific endo- » -1 ,4-glucanase (EC 3.
- Glycoside Hydrolase Family 7 includes endo- » -1 ,4-glucanase (EC 3.2.1 .4); reducing end-acting cellobiohydrolase (EC 3.2.1 .176); chitosanase (EC
- Glycoside Hydrolase Family 45 includes the inverting enzymes of
- the enzymes of the invention may be from bacterial or fungal origin. Chemically modified or protein engineered mutants are included.
- the primary care and/or the auxiliary care enzymes are cellulases.
- Preferred 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.
- Especially preferred primary care cellulases are the alkaline or neutral cellulases having color care benefits.
- Such preferred enzymes include those having a molecular weight of from 17kDa to 30 kDa, for example the endoglucanases sold under the tradename Biotouch(R) NCD, DCC and DCL (AB Enzymes, Darmstadt, Germany).
- Other preferred commercially available cellulases include
- auxiliary care cellulases include those active to active to hydrolyse cellooligosaccharides and may include EndolaseTM CellucleanTM.
- enzymes could be included in the fabric treatment composition such as proteases, lipases, phospholipases, amylases, pectate lyases, mannases, peroxidases/oxidases.
- psychrophilic enzymes Whilst mesophilic enzymes are preferred, psychrophilic enzymes may be used and are included in the scope of the invention. Such enzymes include the cellulases and xylanase from e.g. Clostridium sp. PXYL1 (G. Akila, T.S.Chandra (2003) FEMS Microbiol. Letters 219, 63-67). Psychrophilic xylanases include E.coli phagemid (Lee et al. 2006b).
- the fabric treatment composition may comprise a laundry/fabric cleaning/care composition and may comprise one or more surfactants and/or optionally other ingredients.
- compositions of the invention may be in dry solid form e.g. powdered, granules or tableted powders or liquid or gel form. It may also be in the form of a solid detergent bar.
- the composition may be a concentrate to be diluted, rehydrated and/or dissolved in a solvent, including water, before use.
- the composition may also be a ready-to-use (in-use) composition.
- the present invention is suitable for use in industrial or domestic fabric wash compositions, fabric conditioning compositions and compositions for both washing and conditioning fabrics (so-called through the wash conditioner compositions).
- the present invention can also be applied to industrial or domestic non-detergent based fabric care compositions, for example spray-on compositions.
- detergent ingredients may be included including surfactants, builders, sequestring agents, hydrotropes, preservatives, complexing agents, polymers, stabilizers, perfumes, optical brighteners, or other ingredients such as e.g. fabric conditioners including clays, foam boosters, suds suppressors (anti-foams), anti- corrosion agents, soil-suspending agents, anti-soil redeposition agents, antimicrobials, tarnish inhibitors, or combinations of one or more thereof, provided that these ingredients are compatible with the enzymes.
- fabric conditioners including clays, foam boosters, suds suppressors (anti-foams), anti- corrosion agents, soil-suspending agents, anti-soil redeposition agents, antimicrobials, tarnish inhibitors, or combinations of one or more thereof, provided that these ingredients are compatible with the enzymes.
- the fabric wash compositions may comprise a fabric wash detergent material selected from non-soap anionic surfactant, nonionic surfactants, soap, amphoteric surfactants, zwitterionic surfactants and mixtures thereof.
- the surfactants may be present in the composition at a level of from 0.1 % to 60% by weight.
- Any enzyme present in a composition may be stabilized using conventional stabilizing agents, e.g., a polyol such as propylene glycol or glycerol, a sugar or sugar alcohol, lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid.
- a polyol such as propylene glycol or glycerol
- a sugar or sugar alcohol lactic acid, boric acid, or a boric acid derivative, e.g., an aromatic borate ester, or a phenyl boronic acid derivative such as 4-formylphenyl boronic acid.
- Enzymes concentrations/ratios A,B and C were prepared as follows.
- BCA reagent solution was prepared by mixing BCA reagents A and B in a 50:1 (v/v) ratio. BCA reagent solution was then mixed in a 1 :1 (v/v) ratio with 100 ⁇ aliquots of sample supernatant solutions in sealed microplate wells and incubated at 65-70°C for 40 minutes. Microplates were then allowed to cool to room temperature in a refrigerator, before well seals were carefully removed. Absorbance of reaction products was measured at 540nm in a spectrophotometer. Interference by protein was accounted for by subtracting protein only (no cotton linters) control readings. Total reducing sugar released was calculated using a standard curve of glucose from 0 - 200 ⁇ .
- Results Tables 1 ,2 and 3 show the results from A, B and C (respectively) as described above : synergistic release of reducing sugars from cotton linters by a 1 :1 mix of three different Family 45 EG-V type endoglucanases (Carezyme, Renozyme and Biotouch) and a Family 7 EG-I type endoglucanase (Endolase). The assay was carried out at 25°C. No enzyme control values have been subtracted from all data. Table 1
- Table 4- (corresponds to Figure 4) showing synergistic release of reducing sugars from cotton linters by a 1 :1 mix of two different Family 45 EG-V type endoglucanases (Carezyme and Biotouch) and a Family 5 EG-I type endoglucanase (Celludean).
- the assay was carried out at 25°C. No enzyme control values have been subtracted from all data.
- a 1 :1 mix of the two types of cellulase according to the invention was found to act synergistically in the release of reducing sugars from cotton linters at 25°C.
- the first cellulase component in this mix is a primary care enzyme, being a Family 45 EG-V type endoglucanase.
- the secondary cellulase component is an auxiliary care enzyme with low activity towards cotton linters.
- enzymes e.g. amylase and/or protease 1
- the enzymes of the invention are included at 0.02 wt % .
- the viscosity of the above exemplary composition is 2700 cps at 20 s ⁇ 1 . However, lower viscosity formulations are possible.
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biochemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Textile Engineering (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
Priority Applications (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP13721724.6A EP2847313A1 (en) | 2012-05-10 | 2013-05-07 | Care enzyme system |
IN2257MUN2014 IN2014MN02257A (enrdf_load_stackoverflow) | 2012-05-10 | 2013-05-07 | |
AU2013258083A AU2013258083A1 (en) | 2012-05-10 | 2013-05-07 | Care enzyme system |
AU2016200189A AU2016200189B2 (en) | 2012-05-10 | 2016-01-13 | Care enzyme system |
Applications Claiming Priority (2)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
EP12167440.2 | 2012-05-10 | ||
EP12167440 | 2012-05-10 |
Publications (1)
Publication Number | Publication Date |
---|---|
WO2013167613A1 true WO2013167613A1 (en) | 2013-11-14 |
Family
ID=48407537
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
PCT/EP2013/059527 WO2013167613A1 (en) | 2012-05-10 | 2013-05-07 | Care enzyme system |
Country Status (4)
Country | Link |
---|---|
EP (1) | EP2847313A1 (enrdf_load_stackoverflow) |
AU (2) | AU2013258083A1 (enrdf_load_stackoverflow) |
IN (1) | IN2014MN02257A (enrdf_load_stackoverflow) |
WO (1) | WO2013167613A1 (enrdf_load_stackoverflow) |
Cited By (3)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2016206621A1 (en) | 2015-06-26 | 2016-12-29 | Novozymes A/S | Biofinishing system |
WO2017048636A1 (en) | 2015-09-14 | 2017-03-23 | Agri-King, Inc. | Bacteria and enzymes produced therefrom and methods of using same |
US10538720B2 (en) | 2016-03-08 | 2020-01-21 | The Procter & Gamble Company | Particles including enzyme |
Citations (8)
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EP0251446A2 (en) | 1986-04-30 | 1988-01-07 | Genencor International, Inc. | Non-human Carbonyl hydrolase mutants, DNA sequences and vectors encoding same and hosts transformed with said vectors |
WO1991000345A1 (en) | 1989-06-26 | 1991-01-10 | Novo Nordisk A/S | A mutated subtilisin protease |
WO1992006165A1 (en) * | 1991-06-11 | 1992-04-16 | Genencor International, Inc. | Detergent compositions containing cellulase compositions deficient in cbh i type components |
EP0525610A2 (de) | 1991-07-27 | 1993-02-03 | Solvay Enzymes GmbH & Co. KG | Verfahren zur Verbesserung der Stabilität von Enzymen und stabilisierte Enzyme |
WO1994002618A1 (en) | 1992-07-17 | 1994-02-03 | Gist-Brocades N.V. | High alkaline serine proteases |
WO1995002675A1 (en) | 1993-07-12 | 1995-01-26 | Novo Nordisk A/S | A detergent composition comprising two cellulase components |
US5688290A (en) * | 1989-10-19 | 1997-11-18 | Genencor International, Inc. | Degradation resistant detergent compositions based on cellulase enzymes |
WO2000042146A1 (en) * | 1999-01-14 | 2000-07-20 | The Procter & Gamble Company | Detergent compositions comprising an enzyme system |
-
2013
- 2013-05-07 AU AU2013258083A patent/AU2013258083A1/en not_active Abandoned
- 2013-05-07 IN IN2257MUN2014 patent/IN2014MN02257A/en unknown
- 2013-05-07 EP EP13721724.6A patent/EP2847313A1/en not_active Ceased
- 2013-05-07 WO PCT/EP2013/059527 patent/WO2013167613A1/en active Application Filing
-
2016
- 2016-01-13 AU AU2016200189A patent/AU2016200189B2/en active Active
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EP0251446A2 (en) | 1986-04-30 | 1988-01-07 | Genencor International, Inc. | Non-human Carbonyl hydrolase mutants, DNA sequences and vectors encoding same and hosts transformed with said vectors |
WO1991000345A1 (en) | 1989-06-26 | 1991-01-10 | Novo Nordisk A/S | A mutated subtilisin protease |
US5688290A (en) * | 1989-10-19 | 1997-11-18 | Genencor International, Inc. | Degradation resistant detergent compositions based on cellulase enzymes |
WO1992006165A1 (en) * | 1991-06-11 | 1992-04-16 | Genencor International, Inc. | Detergent compositions containing cellulase compositions deficient in cbh i type components |
EP0525610A2 (de) | 1991-07-27 | 1993-02-03 | Solvay Enzymes GmbH & Co. KG | Verfahren zur Verbesserung der Stabilität von Enzymen und stabilisierte Enzyme |
WO1994002618A1 (en) | 1992-07-17 | 1994-02-03 | Gist-Brocades N.V. | High alkaline serine proteases |
WO1995002675A1 (en) | 1993-07-12 | 1995-01-26 | Novo Nordisk A/S | A detergent composition comprising two cellulase components |
WO2000042146A1 (en) * | 1999-01-14 | 2000-07-20 | The Procter & Gamble Company | Detergent compositions comprising an enzyme system |
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ARTUR CAVACO-PAULO: "Mechanism of cellulase action in textile processes", CARBOHYDRATE POLYMERS, vol. 37, 1 January 1998 (1998-01-01), pages 273 - 277, XP055051893 * |
ATSUSHI SHIMONAKA ET AL: "Amino Acid Regions of Family 45 Endoglucanases Involved in Cotton Defibrillation and in Resistance to Anionic Surfactants and Oxidizing Agents", BIOSCIENCE, BIOTECHNOLOGY, AND BIOCHEMISTRY, vol. 70, no. 10, 1 January 2006 (2006-01-01), pages 2460 - 2466, XP055051705, ISSN: 0916-8451, DOI: 10.1271/bbb.60200 * |
G. AKILA; T.S.CHANDRA, FEMS MICROBIOL. LETTERS, vol. 219, 2003, pages 63 - 67 |
J.M. CORTEZ ET AL: "Cellulase finishing of woven, cotton fabrics in jet and winch machines", JOURNAL OF BIOTECHNOLOGY, vol. 89, 1 January 2001 (2001-01-01), pages 239 - 245, XP055051896 * |
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See also references of EP2847313A1 * |
Cited By (8)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
WO2016206621A1 (en) | 2015-06-26 | 2016-12-29 | Novozymes A/S | Biofinishing system |
US10392742B2 (en) | 2015-06-26 | 2019-08-27 | Novozymes A/S | Biofinishing system |
WO2017048636A1 (en) | 2015-09-14 | 2017-03-23 | Agri-King, Inc. | Bacteria and enzymes produced therefrom and methods of using same |
US10138444B2 (en) | 2015-09-14 | 2018-11-27 | Agri-King, Inc. | Bacteria and enzymes produced therefrom and methods of using same |
US10604727B2 (en) | 2015-09-14 | 2020-03-31 | Agri-King, Inc. | Bacteria and enzymes produced therefrom and methods of using same |
US10683473B2 (en) | 2015-09-14 | 2020-06-16 | Agri-King, Inc. | Bacteria and enzymes produced therefrom and methods of using same |
US11008534B2 (en) | 2015-09-14 | 2021-05-18 | Agri-King, Inc. | Bacteria and enzymes produced therefrom and methods of using same |
US10538720B2 (en) | 2016-03-08 | 2020-01-21 | The Procter & Gamble Company | Particles including enzyme |
Also Published As
Publication number | Publication date |
---|---|
AU2016200189B2 (en) | 2017-07-27 |
AU2013258083A1 (en) | 2014-11-20 |
IN2014MN02257A (enrdf_load_stackoverflow) | 2015-07-24 |
AU2016200189A1 (en) | 2016-02-04 |
EP2847313A1 (en) | 2015-03-18 |
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