CN105887421B - The system of sequential enzyme delivery - Google Patents
The system of sequential enzyme delivery Download PDFInfo
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- CN105887421B CN105887421B CN201610102346.1A CN201610102346A CN105887421B CN 105887421 B CN105887421 B CN 105887421B CN 201610102346 A CN201610102346 A CN 201610102346A CN 105887421 B CN105887421 B CN 105887421B
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- enzyme
- lipase
- washing
- bacillus
- protease
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- BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical compound [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 241000194105 Paenibacillus polymyxa Species 0.000 description 1
- 108090001050 Phosphoric Diester Hydrolases Proteins 0.000 description 1
- 102000004861 Phosphoric Diester Hydrolases Human genes 0.000 description 1
- ABLZXFCXXLZCGV-UHFFFAOYSA-N Phosphorous acid Chemical class OP(O)=O ABLZXFCXXLZCGV-UHFFFAOYSA-N 0.000 description 1
- 206010035742 Pneumonitis Diseases 0.000 description 1
- 229920002504 Poly(2-vinylpyridine-N-oxide) Polymers 0.000 description 1
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- 239000002202 Polyethylene glycol Substances 0.000 description 1
- 239000004642 Polyimide Substances 0.000 description 1
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- OFOBLEOULBTSOW-UHFFFAOYSA-N Propanedioic acid Natural products OC(=O)CC(O)=O OFOBLEOULBTSOW-UHFFFAOYSA-N 0.000 description 1
- 241000588769 Proteus <enterobacteria> Species 0.000 description 1
- 241000588767 Proteus vulgaris Species 0.000 description 1
- 241000588768 Providencia Species 0.000 description 1
- 241000589540 Pseudomonas fluorescens Species 0.000 description 1
- 241000589630 Pseudomonas pseudoalcaligenes Species 0.000 description 1
- 241000589776 Pseudomonas putida Species 0.000 description 1
- 241000577556 Pseudomonas wisconsinensis Species 0.000 description 1
- 241001361634 Rhizoctonia Species 0.000 description 1
- 241000813090 Rhizoctonia solani Species 0.000 description 1
- 241000235525 Rhizomucor pusillus Species 0.000 description 1
- 241000235527 Rhizopus Species 0.000 description 1
- 240000005384 Rhizopus oryzae Species 0.000 description 1
- 235000013752 Rhizopus oryzae Nutrition 0.000 description 1
- 241000235546 Rhizopus stolonifer Species 0.000 description 1
- 241001638069 Rigidoporus microporus Species 0.000 description 1
- 241001292348 Salipaludibacillus agaradhaerens Species 0.000 description 1
- 241000607142 Salmonella Species 0.000 description 1
- 241000293869 Salmonella enterica subsp. enterica serovar Typhimurium Species 0.000 description 1
- 108010022999 Serine Proteases Proteins 0.000 description 1
- 102000012479 Serine Proteases Human genes 0.000 description 1
- 241000270295 Serpentes Species 0.000 description 1
- XUIMIQQOPSSXEZ-UHFFFAOYSA-N Silicon Chemical compound [Si] XUIMIQQOPSSXEZ-UHFFFAOYSA-N 0.000 description 1
- 239000004115 Sodium Silicate Substances 0.000 description 1
- 241000187176 Streptomyces violaceoruber Species 0.000 description 1
- 241001655322 Streptomycetales Species 0.000 description 1
- ULUAUXLGCMPNKK-UHFFFAOYSA-N Sulfobutanedioic acid Chemical class OC(=O)CC(C(O)=O)S(O)(=O)=O ULUAUXLGCMPNKK-UHFFFAOYSA-N 0.000 description 1
- 241000223257 Thermomyces Species 0.000 description 1
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- 241000223238 Trichophyton Species 0.000 description 1
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- 229910001491 alkali aluminosilicate Inorganic materials 0.000 description 1
- 229910052783 alkali metal Inorganic materials 0.000 description 1
- 150000001340 alkali metals Chemical class 0.000 description 1
- 125000003342 alkenyl group Chemical group 0.000 description 1
- 150000005215 alkyl ethers Chemical group 0.000 description 1
- 125000005227 alkyl sulfonate group Chemical group 0.000 description 1
- 150000008052 alkyl sulfonates Chemical class 0.000 description 1
- PNEYBMLMFCGWSK-UHFFFAOYSA-N aluminium oxide Inorganic materials [O-2].[O-2].[O-2].[Al+3].[Al+3] PNEYBMLMFCGWSK-UHFFFAOYSA-N 0.000 description 1
- ANBBXQWFNXMHLD-UHFFFAOYSA-N aluminum;sodium;oxygen(2-) Chemical compound [O-2].[O-2].[Na+].[Al+3] ANBBXQWFNXMHLD-UHFFFAOYSA-N 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- 150000001414 amino alcohols Chemical class 0.000 description 1
- 239000002280 amphoteric surfactant Substances 0.000 description 1
- 238000004458 analytical method Methods 0.000 description 1
- 125000000129 anionic group Chemical group 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 230000000845 anti-microbial effect Effects 0.000 description 1
- 238000000149 argon plasma sintering Methods 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 229920001400 block copolymer Polymers 0.000 description 1
- KGBXLFKZBHKPEV-UHFFFAOYSA-N boric acid Chemical compound OB(O)O KGBXLFKZBHKPEV-UHFFFAOYSA-N 0.000 description 1
- 229910052796 boron Inorganic materials 0.000 description 1
- 238000005282 brightening Methods 0.000 description 1
- HKPHPIREJKHECO-UHFFFAOYSA-N butachlor Chemical compound CCCCOCN(C(=O)CCl)C1=C(CC)C=CC=C1CC HKPHPIREJKHECO-UHFFFAOYSA-N 0.000 description 1
- KDYFGRWQOYBRFD-NUQCWPJISA-N butanedioic acid Chemical compound O[14C](=O)CC[14C](O)=O KDYFGRWQOYBRFD-NUQCWPJISA-N 0.000 description 1
- 229910001424 calcium ion Inorganic materials 0.000 description 1
- 239000002775 capsule Substances 0.000 description 1
- 239000001768 carboxy methyl cellulose Substances 0.000 description 1
- 235000010948 carboxy methyl cellulose Nutrition 0.000 description 1
- 239000008112 carboxymethyl-cellulose Substances 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 239000001913 cellulose Substances 0.000 description 1
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- 238000012512 characterization method Methods 0.000 description 1
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- 239000012141 concentrate Substances 0.000 description 1
- 230000003750 conditioning effect Effects 0.000 description 1
- 229910052593 corundum Inorganic materials 0.000 description 1
- 238000002425 crystallisation Methods 0.000 description 1
- 230000008025 crystallization Effects 0.000 description 1
- 230000000593 degrading effect Effects 0.000 description 1
- 238000000151 deposition Methods 0.000 description 1
- 150000001982 diacylglycerols Chemical class 0.000 description 1
- 238000010790 dilution Methods 0.000 description 1
- 239000012895 dilution Substances 0.000 description 1
- 239000001177 diphosphate Substances 0.000 description 1
- XPPKVPWEQAFLFU-UHFFFAOYSA-J diphosphate(4-) Chemical compound [O-]P([O-])(=O)OP([O-])([O-])=O XPPKVPWEQAFLFU-UHFFFAOYSA-J 0.000 description 1
- 235000011180 diphosphates Nutrition 0.000 description 1
- 238000009826 distribution Methods 0.000 description 1
- 238000001035 drying Methods 0.000 description 1
- 230000032050 esterification Effects 0.000 description 1
- 238000005886 esterification reaction Methods 0.000 description 1
- RTZKZFJDLAIYFH-UHFFFAOYSA-N ether Substances CCOCC RTZKZFJDLAIYFH-UHFFFAOYSA-N 0.000 description 1
- 229940093500 ethoxyquin Drugs 0.000 description 1
- DECIPOUIJURFOJ-UHFFFAOYSA-N ethoxyquin Chemical group N1C(C)(C)C=C(C)C2=CC(OCC)=CC=C21 DECIPOUIJURFOJ-UHFFFAOYSA-N 0.000 description 1
- 235000019285 ethoxyquin Nutrition 0.000 description 1
- 239000002979 fabric softener Substances 0.000 description 1
- 150000004665 fatty acids Chemical class 0.000 description 1
- 150000002191 fatty alcohols Chemical group 0.000 description 1
- 239000000835 fiber Substances 0.000 description 1
- 239000000945 filler Substances 0.000 description 1
- 244000144992 flock Species 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 238000009472 formulation Methods 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 235000004611 garlic Nutrition 0.000 description 1
- 239000003292 glue Substances 0.000 description 1
- 229910001385 heavy metal Inorganic materials 0.000 description 1
- 229940059442 hemicellulase Drugs 0.000 description 1
- 108010002430 hemicellulase Proteins 0.000 description 1
- 230000008588 hemolysis Effects 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 150000002460 imidazoles Chemical class 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 229910052500 inorganic mineral Inorganic materials 0.000 description 1
- 210000000936 intestine Anatomy 0.000 description 1
- 108010090785 inulinase Proteins 0.000 description 1
- 238000005342 ion exchange Methods 0.000 description 1
- SUMDYPCJJOFFON-UHFFFAOYSA-N isethionic acid Chemical compound OCCS(O)(=O)=O SUMDYPCJJOFFON-UHFFFAOYSA-N 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000000787 lecithin Substances 0.000 description 1
- 235000010445 lecithin Nutrition 0.000 description 1
- 229940067606 lecithin Drugs 0.000 description 1
- 230000004130 lipolysis Effects 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 230000014759 maintenance of location Effects 0.000 description 1
- VZCYOOQTPOCHFL-UPHRSURJSA-N maleic acid Chemical compound OC(=O)\C=C/C(O)=O VZCYOOQTPOCHFL-UPHRSURJSA-N 0.000 description 1
- 239000011976 maleic acid Substances 0.000 description 1
- 229910052748 manganese Inorganic materials 0.000 description 1
- 239000011572 manganese Substances 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 238000010907 mechanical stirring Methods 0.000 description 1
- 150000004702 methyl esters Chemical class 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 230000005012 migration Effects 0.000 description 1
- 235000013336 milk Nutrition 0.000 description 1
- 239000008267 milk Substances 0.000 description 1
- 210000004080 milk Anatomy 0.000 description 1
- 239000011707 mineral Substances 0.000 description 1
- 230000007935 neutral effect Effects 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- QJGQUHMNIGDVPM-UHFFFAOYSA-N nitrogen group Chemical group [N] QJGQUHMNIGDVPM-UHFFFAOYSA-N 0.000 description 1
- SNQQPOLDUKLAAF-UHFFFAOYSA-N nonylphenol Chemical compound CCCCCCCCCC1=CC=CC=C1O SNQQPOLDUKLAAF-UHFFFAOYSA-N 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 239000005416 organic matter Substances 0.000 description 1
- 239000003960 organic solvent Substances 0.000 description 1
- 229910052760 oxygen Inorganic materials 0.000 description 1
- 239000001301 oxygen Substances 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 239000001814 pectin Substances 0.000 description 1
- 235000010987 pectin Nutrition 0.000 description 1
- 229920001277 pectin Polymers 0.000 description 1
- HXITXNWTGFUOAU-UHFFFAOYSA-N phenylboronic acid Chemical class OB(O)C1=CC=CC=C1 HXITXNWTGFUOAU-UHFFFAOYSA-N 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate 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
- 150000003904 phospholipids Chemical class 0.000 description 1
- IEQIEDJGQAUEQZ-UHFFFAOYSA-N phthalocyanine Chemical compound N1C(N=C2C3=CC=CC=C3C(N=C3C4=CC=CC=C4C(=N4)N3)=N2)=C(C=CC=C2)C2=C1N=C1C2=CC=CC=C2C4=N1 IEQIEDJGQAUEQZ-UHFFFAOYSA-N 0.000 description 1
- 229910052615 phyllosilicate Inorganic materials 0.000 description 1
- 150000003053 piperidines Chemical class 0.000 description 1
- 229920000058 polyacrylate Polymers 0.000 description 1
- 229920001281 polyalkylene Polymers 0.000 description 1
- 229920002647 polyamide Polymers 0.000 description 1
- 229920005646 polycarboxylate Polymers 0.000 description 1
- 229920000570 polyether Polymers 0.000 description 1
- 229920000573 polyethylene Polymers 0.000 description 1
- 229920001721 polyimide Polymers 0.000 description 1
- 239000001205 polyphosphate Substances 0.000 description 1
- 235000011176 polyphosphates Nutrition 0.000 description 1
- 229920002451 polyvinyl alcohol Polymers 0.000 description 1
- 229920002717 polyvinylpyridine Polymers 0.000 description 1
- 230000001376 precipitating effect Effects 0.000 description 1
- 229940007042 proteus vulgaris Drugs 0.000 description 1
- UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 1
- 150000003233 pyrroles Chemical class 0.000 description 1
- 150000003235 pyrrolidines Chemical class 0.000 description 1
- 229920005604 random copolymer Polymers 0.000 description 1
- 238000010188 recombinant method Methods 0.000 description 1
- 238000001226 reprecipitation Methods 0.000 description 1
- 229940071089 sarcosinate Drugs 0.000 description 1
- 238000005201 scrubbing Methods 0.000 description 1
- 229910052710 silicon Inorganic materials 0.000 description 1
- 239000010703 silicon Substances 0.000 description 1
- 229910001388 sodium aluminate Inorganic materials 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 0.000 description 1
- 235000019795 sodium metasilicate Nutrition 0.000 description 1
- 159000000000 sodium salts Chemical class 0.000 description 1
- NTHWMYGWWRZVTN-UHFFFAOYSA-N sodium silicate Chemical compound [Na+].[Na+].[O-][Si]([O-])=O NTHWMYGWWRZVTN-UHFFFAOYSA-N 0.000 description 1
- 229910052911 sodium silicate Inorganic materials 0.000 description 1
- 235000019832 sodium triphosphate Nutrition 0.000 description 1
- 229940048842 sodium xylenesulfonate Drugs 0.000 description 1
- ZUFONQSOSYEWCN-UHFFFAOYSA-M sodium;2-(methylamino)acetate Chemical compound [Na+].CNCC([O-])=O ZUFONQSOSYEWCN-UHFFFAOYSA-M 0.000 description 1
- QUCDWLYKDRVKMI-UHFFFAOYSA-M sodium;3,4-dimethylbenzenesulfonate Chemical compound [Na+].CC1=CC=C(S([O-])(=O)=O)C=C1C QUCDWLYKDRVKMI-UHFFFAOYSA-M 0.000 description 1
- 239000002689 soil Substances 0.000 description 1
- 239000007921 spray Substances 0.000 description 1
- 230000006641 stabilisation Effects 0.000 description 1
- 238000011105 stabilization Methods 0.000 description 1
- 230000003068 static effect Effects 0.000 description 1
- 239000001384 succinic acid Substances 0.000 description 1
- 108010075550 termamyl Proteins 0.000 description 1
- 239000004753 textile Substances 0.000 description 1
- 239000004577 thatch Substances 0.000 description 1
- VZCYOOQTPOCHFL-UHFFFAOYSA-N trans-butenedioic acid Natural products OC(=O)C=CC(O)=O VZCYOOQTPOCHFL-UHFFFAOYSA-N 0.000 description 1
- 239000001226 triphosphate Substances 0.000 description 1
- 235000011178 triphosphate Nutrition 0.000 description 1
- UNXRWKVEANCORM-UHFFFAOYSA-N triphosphoric acid Chemical compound OP(O)(=O)OP(O)(=O)OP(O)(O)=O UNXRWKVEANCORM-UHFFFAOYSA-N 0.000 description 1
- RYFMWSXOAZQYPI-UHFFFAOYSA-K trisodium phosphate Chemical compound [Na+].[Na+].[Na+].[O-]P([O-])([O-])=O RYFMWSXOAZQYPI-UHFFFAOYSA-K 0.000 description 1
- 229920002554 vinyl polymer Polymers 0.000 description 1
- 239000002023 wood Substances 0.000 description 1
- 229940071104 xylenesulfonate Drugs 0.000 description 1
- 229940098232 yersinia enterocolitica Drugs 0.000 description 1
- 229910001845 yogo sapphire Inorganic materials 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
- D06F—LAUNDERING, DRYING, IRONING, PRESSING OR FOLDING TEXTILE ARTICLES
- D06F39/00—Details of washing machines not specific to a single type of machines covered by groups D06F9/00 - D06F27/00
- D06F39/02—Devices for adding soap or other washing agents
-
- 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
- C11D3/38627—Preparations containing enzymes, e.g. protease or amylase containing lipase
-
- C11D2111/12—
Abstract
The present invention provides a kind of washing machine, it combines the successively processing unit for being used to successively handle fabric at least the first enzyme and second enzyme, described device includes multiple individual, rooms respectively containing the first enzyme and second enzyme, the enzyme is sequentially allocated out from the room, it is characterized in that first enzyme includes protease, and the second enzyme includes one or more lipolytic enzymes.
Description
The application is application number 200880101706.X, 27 days June 2008 applying date, denomination of invention " sequential enzyme delivery
System " Chinese patent application divisional application.
Technical field
The present invention relates to enzymes, and successively sending in washing process is passed.
Background technique
Enzymatic mixture used in laundry processes is known.Protease/cellulose group is disclosed in WO2000070006
It closes.Disclosed in WO20050089966, EP1664258, US20050059567 and US20060172913 for except burring with
And the enzymatic mixture of the spot on egg.
Summary of the invention
Purpose, which is to provide, a kind of improved is related to washing/decontamination method of enzyme.Since other components hydrolyze,
It is still extremely difficult for the enzymatic mixture of one of main component to provide a kind of protease.
Therefore, in the first aspect, the present invention provides a kind of fabric cleaning process, in the method at least two differences
Enzyme successively handle fabric, the method includes the steps:
1. with one or more Protease Treatments, later
2. with one or more second enzymatic treatments,
It is characterized in that this kind or various second enzymes in second step are different families from the protease in first step
Race.
It is preferred that the second enzyme includes one or more lipolytic enzymes.
In second aspect, the present invention provides a kind of method that spot is removed from fabric comprising step:
1. with one or more Protease Treatments, later
2. with one or more second enzymatic treatments, it is characterised in that this kind or various second enzymes and first in second step
Protease in step is different families.
The preferred feature of the method for second aspect is also for first aspect.
Between the step or the step of the step is with another process, such as may have between rinse step
Time delay.
It is preferred that the method for second aspect of the present invention is the method for removing burring dirt from fabric.
In another aspect, the present invention provides a kind of fabric washing and/or decontamination suit comprising at least one contains
First enzyme of first aspect present invention and the packaging of second enzyme, wherein first enzyme and second enzyme are separated from each other, and the packaging is appointed
Choosing includes the operation instruction of the fabric washing and/or fabric decontaminating for the present invention first and/or second aspect.
In further, the present invention provides a kind of washing machine, is used in and successively handles the device of fabric at least
Combined with the first enzyme according to the present invention and second enzyme, described device include it is multiple individually, respectively containing the first enzyme and the
The room of two enzymes, the enzyme are successively allocated out from the room.
Described device preferably includes washing machine drawer (drawer box).
In further, the present invention provide the first enzyme according to a first aspect of the present invention and second enzyme later according to
Purposes in the secondary spot for being used in processing fabric, the especially dirty method of grass.
First enzyme and second enzyme may include the mixture of individual enzyme or enzyme.
Surprisingly, above-mentioned setting makes the enzyme be influenced to minimize by other enzymes in effect.Root is it is contemplated that at first
The protease of addition may be invaded in addition to other enzymes in washing lotion, to hinder the place to the nonproteolytic of spot
Reason.However, the clean effect of enzyme is greatly improved due to sequentially adding.
Specific embodiment
Protease appropriate includes the protease from animal, plant or microbial source.Preferably microbial source.Chemistry changes
Property or protein engineering mutant be also included in.Protease can be serine protease or metalloproteinases, preferably
Alkaline microbial protease or trypsin like proteases.The example of alkali protease is subtilisin, is especially derived from
Those of bacillus substance, such as subtilisin Novo, subtilisin Carlsberg, subtilisin 309, withered grass bacteriolyze
Element 147 and subtilisin 168 (being described in WO 89/06279).The example of trypsin like proteases is tryptose
Enzyme (for example, from pig or it is from ox) and WO 89/06270 and WO 94/25583 described in the mould egg of reaping hook
White enzyme.
The example of available protease is WO 92/19729, WO 98/20115, WO 98/20116 and WO 98/34946
Described in variant, the substituted variant especially on following one or more positions: 27,36,57,76,87,97,
101,104,120,123,167,170,194,206,218,222,224,235 and 274.Preferred commercially available albumen
Enzyme includes AlcalaseTM、SavinaseTM、PrimaseTM、DuralaseTM、DyrazymTM、 EsperaseTM、EverlaseTM、
PolarzymeTMAnd KannaseTM、(Novozymes A/S)、 MaxataseTM、MaxacalTM、MaxapemTM、
ProperaseTM、PurafectTM、Purafect OxPTM、FN2TMAnd FN3TM(Genencor International Inc.)。
Lipase appropriate includes deriving from those of bacterium or fungi lipase.Chemical modification or protein engineering
Mutant be also included in.The example of available lipase includes the rouge from detritus enzyme (synonymous with Thermomyces)
Fat enzyme, such as the rouge of H.lanuginosa (T.lanuginosus) is derived from described in EP 258 068 and EP 305 216
The lipase of special detritus enzyme, Pseudomonas Lipases, such as source are derived from described in fat enzyme or WO 96/13580
Alkali vacation unit cell mattress or pseudomonas pseudoalcaligenes (EP 218 272), pseudomonas cepacia (EP 331 376), this empty thatch are produced in class
Family name pseudomonad (GB 1,372,034), Pseudomonas fluorescens, 705 plants of pseudomonas SD (WO 95/06720 and WO 96/
27002), the lipase of P.wisconsinensis (WO 96/12012), bacillus lipase, such as from withered grass bud
Spore bacillus (Dartois et al. (1993), Biochemica et Biophysica Acta, 1131,253-360), thermophilic rouge
The lipase of fat bacillus (JP 64/744992) or bacillus pumilus (WO 91/16422).
Other examples are lipase Variant, such as WO 92/05249, WO 94/01541, EP 407 225, EP 260
105、WO 95/35381、WO 96/00292、WO 95/30744、WO 94/25578、WO 95/14783、WO 95/22615、
Those substances described in WO 97/04079 and WO 97/07202.
Preferred commercially available lipase includes LipolaseTMWith Lipolase UltraTM、 LipexTM
(Novozymes A/S)。
It should be understood that enzyme variants (for example, being made by recombinant technique) are also included within the meaning of term " enzyme ".It is this
The example of enzyme variants is in such as EP 251,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610
(Solvay) and in WO 94/02618 (Gist-Brocades NV) it is disclosed.
Therefore, the enzyme type that can be suitably incorporated in particle of the invention includes oxidoreducing enzyme (EC
1.-.-.-), transferase (EC 2.-.-.-), hydrolase (EC 3.-.-.-), lyase (EC 4.-.-.-), isomerase (EC
5.-.-.-) and ligase (EC 6.-.-.-).
For other main wash components, it can be added with independent measure and successively send the protease passed and lipolysis
Enzyme, or can by its together with this component it is metered, it is preferred that not by protease in conjunction with other enzymes.
Of the invention successively send the enzyme passed can be together with one or more surfactants and/or other optional compositions
It send and passs, so that at least one of substance sequentially added is the laundry cleaning to play one's part to the full and/or care composition.
This composition of the invention can be drying solid or liquid form.The composition can be using preceding dilution, again water
Solvent is closed and/or is dissolved in, including the concentrate in water.The composition can also be (general (in-use)) easy to use
Composition.
The present invention is suitable for use in industry or domestic fabric cleaning compositions, fabric-conditioning compositions and washing and fabric tune
It manages in dual-purpose composition (so-called general washing conditioning composition).The present invention can also be used in industry or the non-detergent base of household
Fabrid care composition, such as in spray composite.
Fabric cleaning composition of the invention can be any form appropriate, such as powder, flakelike powder, liquid or solid
Body detergent bar.
Be discussed below other expected compositions, including surfactant, hydrotrote, preservative, filler, builder,
The combination of compounding agent, polymer, stabilizer, fragrance itself, other detergent compositions or one or more.
The enzyme, which can be used as individually reactive detergent, to be existed, or can be combined with other detergents.
Investment can be measured using other enzyme as a part of whole washing process, condition is of the invention initial
It is added after process (that is, with enzyme, such as protease and second or more enzyme later, such as lipase treatment) other
Enzyme.
This other (that is, post-dised) enzyme may include above-mentioned further protease and lipase, with
Or mixtures thereof and alpha-amylase, cellulase, peroxidase/oxidizing ferment, pectate lyase and mannase,.
Other components are also possible that production cutinase.It is classified in EC 3.1.1.74.It uses according to the present invention
Production cutinase can be any source.Preferably production cutinase is microbe-derived, and especially bacterium, fungi or yeast come
Source.
Producing cutinase is the enzyme of cutin of capable of degrading.In preferred embodiments, it produces cutinase and is derived from Eurotium
Bacterial strain, especially aspergillus oryzae；Alternaria bacterial strain, especially wild cabbage rod method；Fusarium spp, especially fusariun solani, pea
Skin of soya-bean milk fusarium, Fusarium roseum culmorum or Fusarium roseum sambucium；Helminthosporium bacterial strain,
The especially long compacted spore of garlic；Detritus Pseudomonas bacterial strain, especially special detritus enzyme；Pseudomonas strain, especially Mendoza are false
Monad or pseudomonas putida；Rhizoctonia bacterial strain, especially Rhizoctonia solani；Streptomyces bacterial strain, especially shot hole
Streptomycete；Or it is single every the thin base lattice spore of spore category bacterial strain, especially all living creatures.In the most preferred embodiment, produces cutinase and be derived from
Special detritus enzyme bacterial strain, especially special detritus enzyme strain DSM 1800.Special detritus enzyme produces cutinase in WO 96/13580
It is described, is introduced through reference.Producing cutinase can be to describe in variant, such as WO 00/34450 and WO 01/92502
One of variant, introduced through reference.Preferred produce is listed in the embodiment 2 that cutinase variants include WO 01/92502
Variant is particularly introduced through reference with regard to this.
It includes NOVOZYM that preferred business, which produces cutinase,TM51032 (being purchased from Novozymes A/S, Denmark).
Other components can also include the phosphorus lipase classified such as EC 3.1.1.4 and/or EC 3.1.1.32.As herein
Used in, term phosphorus lipase is the enzyme active to phosphatide.Phosphatide, such as lecithin or phosphatidyl choline are by outside
(sn-1) and on the position middle part (sn-2) glycerol group fatty acid esterification and be esterified on third position by phosphoric acid by two
At；In turn, phosphoric acid can be esterified as amino alcohol.Phosphorus lipase is the enzyme for participating in phospholipid hydrolysis.It can be to several phosphatide
The activity of fat enzyme distinguishes comprising fatty acyl group (being located on the position sn-1 and sn-2) is made to hydrolyze to form haemolysis
The phosphorus lipase A of phosphatide1And A2；With lysophosphatide fat enzyme (or the phosphatide fat that can hydrolyze remaining fatty acyl group in lysophosphatide
Enzyme B).Phosphorus lipase C and phosphorus lipase D (phosphodiesterase) discharges diacylglycerol or phosphatidic acid respectively.
Term phosphorus lipase includes the enzyme with phosphorus lipase active, and the activity is such as phosphatide fat enzyme A (A1Or A2)、
Phosphorus lipase B activity, phosphorus lipase C activity or phosphorus lipase D activity.Term " phosphorus lipase A " used herein and this hair
Bright enzyme, which combines intention covering, has phosphorus lipase A1And/or phosphorus lipase A2Active enzyme.Phosphorus lipase active can also be by
Lipase with other active enzymes, such as with phosphorus lipase active provides.Phosphorus lipase active can for example from
With the active lipase of phosphorus lipase time.In other embodiments of the present invention, the enzymatic activity of phosphorus lipase is by substantially
Only the enzyme with phosphorus lipase active provides, and wherein the enzymatic activity of the phosphatide fat enzyme is not time activity.
Phosphorus lipase can be any source, such as animal origin (for example, mammal), such as from pancreas (for example,
The pancreas of ox or pig), or from the venom of snake or the venom of honeybee.It is preferred that phosphorus lipase can be microbe-derived, example
Such as derive from filamentous fungi, yeast or bacterium, such as aspergillus or kind, such as aspergillus niger；Dictyostelium, such as dictyostelium discoideum；Hair
Mould category, such as mucor javanicus, bee Mucor, thin spore Mucor；Neurospora, such as Neurospora；Rhizopus, such as Rhizomucor pusillus；Wine
Aspergillus, such as Rhizopus arrhizus, Japanese head mold, Rhizopus stolonifer；Sclerotinia, such as Sclerotinia sclerotiorum；Trichophyton, such as red hair
Tinea bacterium；Vickers Sclerotinia, such as W. sclerotiorum；Bacillus, such as bacillus megaterium, bacillus subtilis；Lemon
Lemon acidfast bacilli category, such as citrobacter freundii；Enterobacter, such as clostridium perfringen, cloaca Edward enterobacteria, blunt intestines bar
Bacterium；Erwinia, such as glacial epoch activated bacterial；Escherichia, such as Escherichia coli；Klebsiella, such as Cray primary
Family name's pulmonitis strain；Proteus, such as proteus vulgaris；Providencia, the general sieve Cheng Dengsi bacterium of Ru Sishi；Salmonella
Belong to, such as salmonella typhimurium；Serratia, such as serratia liquefacient, serratia marcesens；Shiga's mattress category, as Freund will is congratulated
Bacterium；Streptomyces, such as Streptomyces violaceoruber；Yersinia, such as yersinia enterocolitica.Therefore, phosphorus lipase can
Think fungi, such as from fruit capsule bacterium subclass, such as Fusarium, such as the strain of machete fusarium, different spore fusarium strain, causing root rot disease of Medicago sativa bacterium
Strain or Fusarium oxysporum strain.Phosphorus lipase can also contain inulinase from the filamentous fungi strain for belonging to aspergillus, such as bubble
Strain, smelly aspergillus strain, aspergillus japonicus strain, Aspergilus niger strain or aspergillus oryzae strain.
Preferred phosphorus lipase is derived from the strain of detritus enzyme, especially pubescence detritus enzyme.Phosphorus lipase can be variant, such as
One of variant disclosed in WO 00/32758, the document is introduced through reference.Preferred phosphorus lipase Variant includes WO 00/
Listed variant, the document are particularly introduced through reference with regard to this in 32758 embodiment 5.In another preferred embodiment party
In case, phosphorus lipase is one described in WO 04/111216, especially listed variant in embodiment 1.
It is preferred that phosphorus lipase is derived from reaping hook bacterial strain, especially Fusarium oxysporum.Phosphorus lipase can be WO 98/
One or its variant mentioned in 026057, derived from Fusarium oxysporum DSM 2672.
Phosphorus lipase is preferably phosphorus lipase A1(EC.3.1.1.32) or phosphorus lipase A2 (EC.3.1.1.4.)。
The example of commercial phosphorus lipase includes LECITASETMAnd LECITASETMULTRA, YIELSMAX or LIPOPAN
F (is purchased from Novozymes A/S, Denmark).
Amylase (α and/or β) appropriate includes the amylase from bacterium or fungi.Chemical modification or protein
In engineered mutants are also included within.Amylase includes for example being obtained by bacillus, such as special Bacillus licheniformis strain
Alpha-amylase, it is more fully described in GB 1,296,839, or be obtained from WO 95/026397 or WO
The alpha-amylase of Bacillus alcalophilus strain disclosed in 00/060060.
The example of available amylase be WO 94/02597, WO 94/18314, WO 96/23873, WO 97/43424,
(document is all through quoting by WO 01/066712, WO 02/010355, WO 02/031124 and PCT/DK2005/000469
And introduce) described in variant.
Commercially available amylase is DuramylTM、TermamylTM、Termamyl UltraTM、 NatalaseTM、
StainzymeTM、FungamylTMAnd BANTM(Novozymes A/S)、 RapidaseTMAnd PurastarTMIt (originates from
Genencor International Inc.)。
Cellulase appropriate includes deriving from those of bacterium or fungi cellulase.Chemical modification or protein engineering
In mutant is also included within.Cellulase appropriate includes deriving from Bacillus, pseudomonas, Humicola, reaping hook
Pseudomonas, fusarium globosum shuttle category, Acremonium cellulase, such as US 4,435,307, US 5,648,263, US 5,691,
178, disclosed in US 5,776,757, WO 89/09259, WO 96/029397 and WO 98/012307 by special humic enzyme,
The fungal cellulase of tai Ruisisuo spore shell enzyme, laccase and Fusarium oxysporum preparation.
Especially appropriate cellulase is the alkalinity or neutral cellulase that benefit is nursed with color.This cellulase
Example EP 0 495 257, EP 0 531 372, WO 96/11262, WO 96/29397, fibre described in WO 98/08940
Tie up plain enzyme.Other examples are cellulase variants, such as WO 94/07998, EP 0 531 315, US 5,457,046, US 5,
686,593, those variants described in US 5,763,254, WO 95/24471, WO 98/12307 and PCT/DK98/00299.
Commercially available cellulase includes CelluzymeTM、CarezymeTM、EndolaseTM、 RenozymeTM
(Novozymes A/S)、ClazinaseTMWith Puradax HATM(Genencor International Inc.) and KAC-
500(B)TM(Kao Corporation)。
Peroxidase/oxidizing ferment appropriate includes those of plant, bacterium or originated from fungus enzyme.Chemical modification or albumen
In matter engineered mutants are also included within.The example of available peroxidase includes deriving from Coprinus, such as the mistake of Coprinus cinereus
Oxide enzyme, and its variant as described in WO 93/24618, WO 95/10602 and WO 98/15257.It is commercially available
Peroxidase include GuardzymeTMAnd NovozymTM 51004(Novozymes A/S)。
The example of pectate lyase includes by different bacterium categories, such as Erwinia, pseudomonas Cray primary
The pectate lyase of Bordetella and Xanthomonas clone, and by hay bacillus (Nasser et al., (1993) FEBS
) and bacillus YA-14 (Kim et al., (1994) Biosci.Biotech Letts.335:319-326.Biochem.58:
947-949) the pectate lyase cloned.Also describe to it is being prepared by following bacterium, in pH range 8-10 have most
The purifying of big active pectate lyase: bacillus pumilus (Dave and Vaughn (1971) J.
Bacteriol.108:166-174), bacillus polymyxa (Nagel and Vaughn (1961) Arch.
Biochem.Biophys.93:344-352), bacillus stearothermophilus (Karbassi and Vaughn (1980)
Can.J.Microbiol.26:377-384), Alkaliphilic bacillus (Hasegawa and Nagel (1966) J.Food Sci.31:
838-845) and Alkaliphilic bacillus RK9 (Kelly and Fogarty (1978) Can.J.Microbiol.24:1164-1172).
Above-mentioned any one and bivalent cation-is independent and/or heat-staple pectate lyase can be used for practicing this hair
It is bright.In preferred embodiments, pectate lyase includes Heffron et al. in (1995) Mol. Plant-Microbe
Interact.8:331-334 and Henrissat et al. the fruit disclosed in (1995) Plant Physiol. 107:963-976
Glue acid lyase amino acid sequence.Especially expected pectate lyase carries out in WO 99/27083 and WO 99/27084
It is open.Other especially expected pectate lyases derived from Bacillus licheniformis (should in US patent no.6,284,524
Document is introduced into through reference) in disclosed.Especially expected pectate lyase variant carries out in WO 02/006442
It is open, specifically variant disclosed in the embodiment of WO 02/006442 (document is introduced through reference).
The example of commercially available alkaline pectin hydrochlorate lyase includes BIOPREPTMAnd SCOURZYMETML is obtained
From Novozymes A/S, Denmark.
The example of mannase (EC 3.2.1.78) includes the mannase from bacterium and fungi.Special
Embodiment in, mannase be derived from the aspergillus strain of filamentous fungi category, preferably aspergillus niger or aspergillus echinulatus (WO 94/
25576).The mannase separated from Richter scale wood enzyme is disclosed in WO 93/24622.Mannase can also be from
It is separated in several bacteriums, including bacillus organic matter.For example, Talbot et al. is in Appl.Environ.Microbiol., 56
Volume, 11 phases describe the 'beta '-mannase derived from bacillus stearothermophilus in 3505-3510 pages (1990).
Mendoza et al. is in World J.Microbiol.Biotech., and volume 10,5 phases described derivative in 551-555 pages (1994)
From the 'beta '-mannase of bacillus subtilis.
The 'beta '-mannase derived from Bacillus alcalophilus is disclosed in JP-A-03047076. JP-A-
The preparation of alkalinity, heat-staple 'beta '-mannase is described in 63056289.JP-A-63036775 is related to generating β-sweet dew
The micro-organisms bacillus of dextranase and beta-Mannosidase.The gemma bar from basophilic is disclosed in JP-A-08051975
Alkaline β-mannase of bacterium AM-001.The purifying from bacillus amyloliquefaciens is disclosed in WO 97/11164
Mannase.Hemicellulase, such as dextranase, zytase or mannosan enzyme activity are described in WO 91/18974
Property molecule.It is contemplated that derived from Bacillus agaradhaerens, lichenoid form gemma bar disclosed in WO 99/64619
Bacterium, salt tolerant Alkaliphilic bacillus, Bacillus clausii, Alkaliphilic bacillus and special detritus enzyme alkaline family 5 and 26
Mannase.Particularly expected that Bacillus alcalophilus mannase involved in the embodiment of WO 99/64619, should
Document is introduced through reference.
The example of commercially available mannase includes MannawayTM, it is purchased from Novozymes A/S
Denmark。
Conventional stabilizer, such as polyalcohol can be used, such as propylene glycol or glycerol, sugar or sugar alcohol, lactic acid, boric acid or boron
Acid derivative, such as aromatic boric acid ester or phenyl boronic acid derivative, such as 4- formyl phenylboronic acid in composition to depositing
Any enzyme carry out static stabilization, and can be according to the description in WO 92/19709 and WO 92/19708 by composition
Preparation is made.
Fabric cleaning composition may include fabric washing substance selected from the group below: non-soap anionic surfactant, non-
Ionic surface active agent, soap, amphoteric surfactant, zwitterionic surfactant and its mixture.
Be suitble to the detergent composition used in household or industrial automatic fabric washing machine usually contain anion without
Soap surfactant or nonionic surfactant, or it is known to the skilled artisan according to fields by both substances
Proper proportion is combined, and is optionally mixed with soap.
The compound of many detergent actives appropriate be all can obtain and in document, such as " Surface-
It is fully described in Active Agents and Detergents ", I and II volumes, Schwartz, Perry&Berch.
Surfactant in the composition can be 0.1%-60% weight there are level.
Nonionic surfactant appropriate is well known for fields those of skill in the art comprising alkylbenzene
Sulfonate, primary and secondary alkyl sulfate, especially C8-C15Primary alkyl sulphates；Alkyl ether sulfate；Alkene sulfonate；Alkyl
Xylenesulfonate, dialkyl sulfosuccinates；Ether carboxylate；Isethionate；Sarcosinate；Aliphatic ester sulphonic acid ester
And its mixture.Generally preferable sodium salt.If being based on fabric treatment composition, the combination including the substance
Object usually contains about 1%- about 50%, the preferably anionic surfactant of 10wt%-40wt%, such as linear alkyl benzene sulfonic acid
Salt, alpha-alkene sulfonate, alkyl sulfate (aliphatic alcohol sulfate), alcohol ethyoxysulfates, secondary alkyl sulfonate, alpha-sulfo fat
Sour methyl esters, alkyl-or alkenyl succinic acid or soap.Preferred surfactant is alkyl ether sulfate and alkoxylated alkyl
The mixture of nonionic surfactant and alkylsulfonate or alkyl ether sulfate.
Preferred alkyl ether sulfate is C8-C15 alkyl and has 2-10 moles oxyethylation has occurred
(ethoxlation).It is C that preferred alkyl sulfate, which is alkylbenzene sulfonate, especially alkyl chain length,8-C15Straight chained alkyl
Phenylsulfate.Counter ion for anionic surfactant is usually sodium, it is also possible to use other counter ions, such as
TEA or ammonium.Anionic surface active substances appropriate can be purchased from market, entitled ' Genapol 'TM, originate from Clariant.
Nonionic surfactant is also well known for fields those of skill in the art comprising primary and secondary alcohol second
Oxide averagely has 1-20 mole ethylene oxide, ethoxylation C in especially every mol of alcohol8-C20Fatty alcohol, more especially
It is the averagely C with 1-10 mole ethylene oxide, ethoxylation in every mol of alcohol10-C15Primary and secondary fatty alcohol.Non- ethoxy
The nonionic surfactant of base includes alkyl polyglycoside, glycerol monoethers and polyhydroxy amides (glucamide).It can also use
The mixture of nonionic surfactant.If the composition usually contains about 0.2%- about including the substance
40%, preferably 1-20wt%, the nonionic surfactant of more preferable 5-15wt%, such as alcohol ethoxylate, nonyl phenol second
Oxygroup compound, alkyl polyglycoside, alkyl dimethyl amine oxide, ethoxylated fatty acids single ethanol amide, fatty monoethanol amide,
The polyhydroxy alkyl fatty acid amide or N- acyl N-alkyl derivatives (" glucamides ") of aminoglucose.
Available nonionic surfactant includes primary and secondary alcohol b-oxide, and especially average every mol of alcohol has 1-35
Mole ethylene oxide, ethoxylation C8-C20Aliphatic alcohol, more particularly average every mol of alcohol have 1-10 moles
Ethylene, ethoxylation C10-C15Primary and secondary aliphatic alcohol.
Higher levels of surfactant (up to intimate 100%), but may make to leave in preparation in this way to help can be used
The space very little of lotion and other components, and there may be the sticky products for needing to do special processing.
It may include hydrotrote in composition.Term " hydrotrote " is often referred to can be improved certain slightly soluble organic compounds
The solubility of object, preferably water-soluble compound.The example of hydrotrote includes sodium xylene sulfonate, SCM.
Composition may include solvent, such as water or organic solvent, such as isopropanol or glycerin ether.Solvent is usually deposited
It is in liquid or gel combination.
Composition can contain metal-chelator, such as carbonate, bicarbonate and sesquicarbonate.The metal-chelating
Agent can be bleaching stibilizer (that is, Heavy metal sequestrants).Bleaching stibilizer appropriate includes edetate
(EDTA), diethyl pentetic acid salt (DTPA), ethylenediamine disuccinate (EDDS) and polyphosphonate, such as
Dequests (Trade Mark), ethylenediamine tetramethylene phosphonic acid ester (EDTMP) and diethyl triamine pentamethylene phosphate
(DETPMP).In general, metal-chelator is not present in composition part, because if metal ion failure then may damage
Microbial function.
Builder material can selected from 1) calcium sequestering agent material, 2) deposited material, 3) calcium ion-exchanged material and 4)
Its mixture.
The example of calcium multivalence sequestering builder material includes alkali metal polyphosphates, such as sodium tripolyphosphate and organic more
Valence chelating agent, such as ethylenediamine tetra-acetic acid.
The example of precipitating builder material includes sodium orthophosphate and sodium carbonate.
The example of calcium ion-exchanged builder material include various types of water-insolubles crystallization or amorphous manosil AS
Salt, wherein most known representative is zeolite, such as Wessalith CS, zeolite B (also referred to zeolite P), zeolite C, X zeolite, zeolite Y
And zeolite P- type as described in EP-A-0,384,070.
The composition can also builder or compounding agent containing 0-65%, ethylenediamine tetra-acetic acid, diethyl triamine five
Acetic acid, alkyl-or alkenyl succinic acid, nitrilotriacetic acid or another builder referenced below.Many builders are bleaching-
Stabilizer, this is because its can complexed metal ion the reason of.
If there is builder, then the composition, which can suitably contain, is less than 20%wt, preferably less than 10 weight %,
The most preferably in less than detergent builder compound of 10%wt.
The composition can be containing the crystalline aluminosilicate as builder, preferred as alkali aluminosilicate, more preferably
Sodium aluminosilicate.It less than the horizontal of 15%w usually to exist.Aluminosilicate is the substance with the following general formula:
0.8-1.5M2O·Al2O3·0.8-6SiO2
Wherein M is univalent cation, preferably sodium.These substances contain some combination water, and have at least 50mg CaO/
The calcium ion exchange capacity of g.Preferred sodium aluminosilicate contains 1.5-3.5 SiO in above formula2Unit.As retouched in detail in document
Ground is stated, can easily be prepared by reacting between sodium metasilicate and sodium aluminate.Surfactant is with aluminosilicate (if deposited
) between ratio be preferably greater than 5: 2, more preferably greater than 3: 1.
Phosphate builder can also be used to replace or be additional to aluminosilicate builder.In this field, term " phosphorus
Hydrochlorate " includes diphosphate, triphosphate and phosphonates.The builder of other forms includes silicate, such as soluble silicon
Hydrochlorate, metasilicate, phyllosilicate (for example, the SKS-6 for originating from Hoechst).
In order to reduce preparation cost, carbonate (including bicarbonate and sesquicarbonate) and/or citric acid can be used
Salt is as builder.
The composition may include one or more polymer.Example is carboxymethyl cellulose, poly- (vinyl pyrrole
Alkanone), poly(ethylene glycol), poly- (vinyl alcohol), poly- (vinylpyridine-N-oxide), poly- (vinyl imidazole), polycarboxylate,
Such as polyacrylate, maleic acid/acrylic copolymer and lauryl methyl acrylates/acrylic copolymer.
Detergent composition now generallys use polymer as so-called " dyestuff-migration inhibitor ".These substances
The migration of dyestuff is prevented, especially during long-term immersion.Any dyestuff-migration inhibitor appropriate can be according to this
Invention is to use.In general, this dyestuff-migration inhibitor includes polyvinyl pyrrolidone polymers, polyamine N-oxide polymerization
Object, the copolymer of n-vinyl pyrrolidone and N- vinyl imidazole, manganese phthalocyanine, peroxidase and its mixture.
It is preferred that nitrogenous, combination dye DTI polymer.In these substances, preferably cyclic amine, such as vinyl pyrrole
The polymer and copolymer of alkanone and/or vinyl imidazole.
It is suitable for the invention polyamine N-oxide pllymers and contains the unit with following structural: R-AX-P；Wherein
P is polymerizable unit, and N-O group may be coupled on the unit or the N-O group can form the one of polymerizable unit
Part；A is one of having structure :-NC (O)-,-C (O) O- ,-S- ,-O- ,-N=；X is 0 or 1；R is aliphatic, ethoxyquin rouge
Fat race, aromatic series, heterocycle and alicyclic group or combinations thereof, the nitrogen-atoms of N-O group can connect on it or the N-O
Group is that a part of these groups or the group can connect on the two units.Preferred polyamine N-oxide
Be heterocyclic group for wherein R, for example, pyridine, pyrroles, imidazoles, pyrrolidines, piperidines and its derivative substance.N-O group can be with
As representated by general formula: N (O) (R ')0-3Or=N (O) (R ')0-1, wherein each R ' independently represent aliphatic, aromatic series,
Heterocycle or alicyclic group or combinations thereof；And the nitrogen-atoms of N-O group can connect on arbitrary above-mentioned group or shape
At its a part.The pKa < 10 of the amine oxide unit of polyamine N-oxide, preferably pKa < 7, more preferable pKa < 6.
Any main polymer chain can be used, condition is to be formed by amine oxide to be water-soluble and move with dyestuff
Move inhibition activity.The example of polymer main chain appropriate is polyethylene, polyalkylene, polyester, polyethers, polyamide, polyimides, gathers
Acrylate and its mixture.These polymer include random or block copolymer, and one of monomer type is amine N- oxygen
Compound, another monomer type are N- oxide.The amine and amine n-oxide ratio of amine n-oxide polymer are usually 10:
1-1:1,000,000.But the quantity of amine oxide groups present in polyamine oxide polymer can be according to appropriate total
Gather effect or N- oxide degree appropriate and becomes.The polyamine oxide of available substantially any extent of polymerization.In general, flat
Average molecular weight is 500-1,000,000；More preferable 1,000-500,000；Most preferably 5,000-100,000.The preferred substance
Type is herein referred to as " PVNO ".Preferred polyamine N-oxide is average molecular weight about 50,000 and amine and amine N- oxygen
Poly- (4-vinylpridine-N- oxide) of the ratio between compound about 1:4.
Further preferably the copolymer of n-vinyl pyrrolidone and N- vinylimidazole polymers is (as a kind of classification, referred to as
"PVPVI").It is preferred that the average molecular weight of the PVPVI is 5,000-1,000,000, more preferable 5,000-200,000, it is optimal
10,000-20,000 are selected, the molecular weight exists according to Barth et al.Chemical Analysis, volume 113, " Modern
Made description in Methods of Polymer Characterization ", is determined by light scattering method.Preferably
PVPVI copolymer usually have 1: 1-0.2: 1 N- vinyl imidazole and n-vinyl pyrrolidone molar ratio, more preferable 0.8:
1-0.3: 1, most preferably 0.6: 1-0.4: 1.These copolymers can be straight chain or branch.PVPVI copolymer appropriate
Including Sokalan(TM)HP56, available commercially from BASF, Ludwigshafen, Germany.
As dye transfer inhibitor, accordingly it is also preferred that average molecular weight is about 5,000- about 400,000, preferably from about
The polyvinylpyrrolidonepolymers polymers (" PVP ") of 5,000- about 2000,000, more preferably from about 5,000- about 50,000.PVP's
Above-mentioned property is had been disclosed in such as EP-A-262,897 and EP-A-256,696.PVP polymer appropriate includes
Sokalan(TM)HP50, available commercially from BASF.Composition containing PVP can also containing average molecular weight be about 500- about
The polyethylene glycol (" PEG ") of 100,000, preferably from about 1,000- about 10,000.It is preferred that based on ppm, send and pass in cleaning solution
The ratio of PEG and PVP is about 2: 1- about 50: 1, more preferably from about 3: 1- about 10: 1.
As dye transfer inhibitor, equally appropriate is by those of modified polyethyleneimine polymers substance acquisition
Inhibitor, the case where as disclosed in such as WO-A-0005334.These modified polyethyleneimine polymers are water-soluble
Or dispersible modified polyamine.Following documents have made further disclosure: US-A-4,548,744 to modified polyamine；US-A-
4,597,898； US-A-4,877,896；US-A-4,891,160；US-A-4,976,879；US-A-5,415,807； GB-A-
1,537,288；GB-A-1,498,520；DE-A-28 29022；And JP-A-06313271.
It is preferred that composition according to the present invention includes dye transfer inhibitor selected from the group below: polyvinylpyridine N- oxygen
Compound (PVNO), polyvinylpyrrolidone (PVP), polyvinyl imidazol, n-vinyl pyrrolidone and N- vinyl imidazole
Copolymer (PVPVI), copolymer and its mixture.
The amount of dye transfer inhibitor in the present composition is the 0.01-10%, preferably 0.02- of composition weight
5%, more preferable 0.03-2%.
The composition can also contain other detergent compositions, such as fabric conditioner, including clay, foam promote
Agent, foam inhibitor (anti-infusion), preservative, soil suspender, dirt reprecipitation inhibitor, other dyestuffs, antimicrobial, light
Learn brightening agent, tarnish inhibitor or fragrance.
The distribution drawer of self-action washing machine can be used successively to measure investment enzyme, thrown for example, being measured using pre- chamber wash
Enter protease, and main chamber wash is for measuring investment lipase.
The present invention may be also used in hand operation, and this operation is not necessarily to other devices, simply be added sequentially to enzyme
Washing can be completed in the cleaning solution of each article.
But hand operation can be related to washing tool, such as scrubbing plant, and can sequence general according to the invention
The composition is directly applied to the tool, is used for the tool to clean clothing later.
The tool or device can also be carried out impregnating and/or delivery device can be used as, in the present invention
Washing/decontamination (preferably go weeding dirty) method in send and pass the enzyme.
The example of non-limiting embodiments of the invention
Embodiment 1
The washing of weeding dirt is gone to evaluate (Terg-O-Tometer) in protease and lipase
Washing effect is evaluated in the following manner: with protease (Savinase 12TXT) and fat in detergent solution
Enzyme (Lipex 100T and lipolase 100T) washs in a manner of (washing 2 times) processing by careless dirty by single enzyme, combination and successively
The polyester sample (wfk30A) of dye.
By the preparation of the sample of grass pollution: the weeds block on severe friction meadow is on clean fabric samples to generate
Even bottle green circle spot, so that the consumer goods with corresponding spot be made by hand.
Washing: under mechanical stirring, careless dirty sample (7 × 7cm) is placed in Terg-O-Tometer bathtub, sample system is made
The component (table 1) of agent is in 1l demineralized water and cultivates 30 minutes at 37 DEG C.Stopped stirring at t=15 minutes, uses
11 demineralized waters rinse all spots, all spots are all transferred in the bathtub of the second wheel enzyme.15 points are persistently stirred again
Clock.Sample is rinsed in tap water, is unfolded and is dried overnight it in dark, at room temperature.
Evaluation: the color of sample is measured at 410nm using Hunterlab UltraScan VIS reflectance spectrophotometer
Color reflectance.Results expression is Δ reflectance=(RAfter washing-RBefore washing)Enzyme-(RAfter washing-R Before washing)Control, wherein R is the reflection at 410nm
Degree uses CIE L*a*b* (CIELAB) value generated.
1. preparation of table composition
Table 2
In Terg-O-Tometer, savinase, savinase and lipase and savinase and lipase later
To the washing effect of cotton thread at low FH (FH6).All spots all use surfactant wash.The total concentration of zymoprotein=1 μ
g/ml。
Successively metered protease is shown in table, when launching lipase again later, how to significantly improve spot
Removal.
Embodiment 2
The washing of weeding dirt is gone to evaluate (microtitrator) in protease and lipase
Washing effect is evaluated in the following manner: with protease (Savinase 12TXT) and fat in detergent solution
Enzyme (Lipex 100T) washs in a manner of (washing 2 times) processing by the cotton test of grass pollution by single enzyme, group synthase and successively
Use cloth.
By the preparation of the cotton test cloth of grass pollution: severe friction mixes on clean cotton fabric using nail brush
Careless (ratio with water 3: 1), carries out pre-flock with polyester textile, so that the consumer goods with corresponding spot be made by hand.
Washing: at stirring (1150rpm), it will be placed in the plate of microtitrator, made with cloth by the test of grass pollution
The component (table 1) of sample formulation is in 200 μ l demineralized waters and cultivates 30 minutes in ring oscillator at 37 DEG C.This
Secondary the case where testing the low water hardness (FH60) and the high water hardness (FH40).Suspended stirring at t=15 minutes, is gone with 200 μ l
Mineral water rinses all spots, and is exposed in the solution of the second wheel enzyme.It persistently stirs 15 minutes again.In tap water
It is placed at least 3 hours at dark, 45 DEG C to make it dry by rinsing sample 2 times.
Evaluation: color reflection degree of the platform reflectance spectrophotometer measurement sample at 410nm is used.Results expression is
Δ reflectance=(RAfter washing-RBefore washing)Enzyme-(RAfter washing-RBefore washing)Control, wherein R is the reflectance at 410nm, uses the CIE generated
L*a*b* (CIELAB) value (table 3 and 4).
| Savinase | 15.39 | 16.12 |
| Savinase+ lipase | 14.17 | 17.95 |
| Lipase is used after Savinase again | 20.40 | 21.10 |
Table 3 is in the plate of microtitrator, savinase, savinase and lipase and savinase and later
Lipase is at low FH (FH6) to the washing effect of cotton thread.All spots all use surfactant wash.Zymoprotein it is total
Concentration=1 or 40 μ g/ml.S-L, savinase use lipase again later.
Table 4 is in the plate of microtitrator, savinase, savinase and lipase and lipase and later
Savinase is at high FH (FH40) to the washing effect of cotton thread.All spots all use surfactant wash.Zymoprotein
Total concentration=1 or 40 μ g/ml.S-L, savinase use lipase again later.
Of course it is to be understood that being not intended to limit the invention in the details of the embodiment above, these embodiments
Only it is described by way of example.
Claims (2)
1. a kind of washing machine mutually ties the successively processing unit for being used to successively handle fabric and at least the first enzyme and second enzyme
It closes, described device includes multiple individual, rooms respectively containing the first enzyme and second enzyme, and the enzyme is in washing process from the room
In be sequentially allocated out, it is characterised in that first enzyme includes protease, and the second enzyme includes staying in the application egg
The one or more lipolytic enzymes applied after white enzyme.
2. the washing machine of claim 1, wherein the successively processing unit includes washing machine drawer.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP07113806 | 2007-08-03 | ||
| EP07113806.9 | 2007-08-03 | ||
| CN200880101706A CN101772568A (en) | 2007-08-03 | 2008-06-27 | Sequential enzyme delivery system |
Related Parent Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200880101706A Division CN101772568A (en) | 2007-08-03 | 2008-06-27 | Sequential enzyme delivery system |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| CN105887421A CN105887421A (en) | 2016-08-24 |
| CN105887421B true CN105887421B (en) | 2019-04-09 |
Family
ID=38973008
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200880101706A Pending CN101772568A (en) | 2007-08-03 | 2008-06-27 | Sequential enzyme delivery system |
| CN201610102346.1A Active CN105887421B (en) | 2007-08-03 | 2008-06-27 | The system of sequential enzyme delivery |
Family Applications Before (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CN200880101706A Pending CN101772568A (en) | 2007-08-03 | 2008-06-27 | Sequential enzyme delivery system |
Country Status (7)
| Country | Link |
|---|---|
| US (1) | US20100206013A1 (en) |
| EP (1) | EP2173845B1 (en) |
| CN (2) | CN101772568A (en) |
| BR (1) | BRPI0814331A2 (en) |
| ES (1) | ES2391357T3 (en) |
| WO (1) | WO2009019075A1 (en) |
| ZA (1) | ZA201000215B (en) |
Families Citing this family (5)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| GB0915572D0 (en) | 2009-09-07 | 2009-10-07 | Reckitt Benckiser Nv | Detergent composition |
| US20110174340A1 (en) * | 2010-01-20 | 2011-07-21 | Ecolab USA | Low and high temperature enzymatic system |
| EP2537918A1 (en) | 2011-06-20 | 2012-12-26 | The Procter & Gamble Company | Consumer products with lipase comprising coated particles |
| US20150376554A1 (en) * | 2013-02-14 | 2015-12-31 | Novozymes A/S | Industrial and Institutional Laundering Using Multi-Enzyme Compositions |
| WO2023275192A1 (en) | 2021-06-29 | 2023-01-05 | Christeyns | Method and apparatus for on-site preparation and dosing of an enzyme-containing detergent formulation |
Family Cites Families (18)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4663278A (en) * | 1982-04-30 | 1987-05-05 | Syva Company | Agglutination dependent enzyme channeling immunoassay |
| US5733763A (en) * | 1988-08-19 | 1998-03-31 | Novo Nordisk A/S | Enzyme granulate formed of an enzyme-containing core and an enzyme-containing shell |
| US5082578A (en) * | 1990-12-11 | 1992-01-21 | Lever Brothers Company, Division Of Conopco, Inc. | Fabric care compositions containing a polymeric fluorescent whitening agent |
| US5272893A (en) * | 1992-09-11 | 1993-12-28 | White Consolidated Industries, Inc. | Enzyme bath maintenance system |
| DE4329463A1 (en) * | 1993-09-01 | 1995-03-02 | Cognis Bio Umwelt | More enzyme granules |
| CN2306243Y (en) * | 1997-07-03 | 1999-02-03 | 海尔集团公司 | Automatic detergent feeding device for washer |
| US6551981B1 (en) * | 1998-07-17 | 2003-04-22 | Patrizio Ricci | Detergent tablet |
| US6812199B2 (en) * | 2000-04-28 | 2004-11-02 | The Procter & Gamble Company | Method for treating stained materials |
| US20030104969A1 (en) * | 2000-05-11 | 2003-06-05 | Caswell Debra Sue | Laundry system having unitized dosing |
| DE10044471A1 (en) * | 2000-09-08 | 2002-03-21 | Cognis Deutschland Gmbh | Fabric-conditioning detergent composition comprising an anionic surfactant, a nonionic and amphoteric surfactant, a cationic polymer and a phosphate |
| US6955067B2 (en) * | 2002-03-28 | 2005-10-18 | The Procter & Gamble Company | Smart dosing device |
| US20050245418A1 (en) * | 2002-06-28 | 2005-11-03 | Reckitt Benckiser N.V. | Detergent composition |
| GB0229806D0 (en) * | 2002-12-20 | 2003-01-29 | Unilever Plc | Fabric care composition |
| US20050059567A1 (en) * | 2003-09-11 | 2005-03-17 | The Procter & Gamble Company | Methods of formulating enzyme cocktails, enzyme cocktails for the removal of egg-based and grass-based stains and/or soils, compositions and products comprising same |
| FR2866252B1 (en) * | 2004-02-18 | 2006-04-21 | Solystic | METHOD FOR SORTING POSTAL SHIPMENTS IN MULTIPLE SORT PASSES |
| CN1779017A (en) * | 2004-11-19 | 2006-05-31 | 乐金电子(天津)电器有限公司 | Water-supply control of washer |
| US20100120651A1 (en) * | 2005-07-11 | 2010-05-13 | Genencor International, Inc. | Enzyme fabric care tablets for consumers and methods |
| GB0613069D0 (en) * | 2006-06-30 | 2006-08-09 | Unilever Plc | Laundry articles |
-
2008
- 2008-06-27 US US12/670,671 patent/US20100206013A1/en not_active Abandoned
- 2008-06-27 BR BRPI0814331A patent/BRPI0814331A2/en not_active Application Discontinuation
- 2008-06-27 EP EP08774456A patent/EP2173845B1/en not_active Revoked
- 2008-06-27 WO PCT/EP2008/058294 patent/WO2009019075A1/en active Application Filing
- 2008-06-27 CN CN200880101706A patent/CN101772568A/en active Pending
- 2008-06-27 CN CN201610102346.1A patent/CN105887421B/en active Active
- 2008-06-27 ES ES08774456T patent/ES2391357T3/en active Active
-
2010
- 2010-01-12 ZA ZA2010/00215A patent/ZA201000215B/en unknown
Also Published As
| Publication number | Publication date |
|---|---|
| CN105887421A (en) | 2016-08-24 |
| ES2391357T3 (en) | 2012-11-23 |
| US20100206013A1 (en) | 2010-08-19 |
| BRPI0814331A2 (en) | 2016-10-04 |
| CN101772568A (en) | 2010-07-07 |
| EP2173845B1 (en) | 2012-07-11 |
| ZA201000215B (en) | 2011-03-30 |
| EP2173845A1 (en) | 2010-04-14 |
| WO2009019075A1 (en) | 2009-02-12 |
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