CN105887421A - Sequential enzyme delivery system - Google Patents
Sequential enzyme delivery system Download PDFInfo
- Publication number
- CN105887421A CN105887421A CN201610102346.1A CN201610102346A CN105887421A CN 105887421 A CN105887421 A CN 105887421A CN 201610102346 A CN201610102346 A CN 201610102346A CN 105887421 A CN105887421 A CN 105887421A
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- Prior art keywords
- enzyme
- lipase
- bacillus
- protease
- washing
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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
- 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
- 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
- 241000607768 Shigella 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
- QAOWNCQODCNURD-UHFFFAOYSA-L Sulfate Chemical compound [O-]S([O-])(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-L 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
- 241000130764 Tinea Species 0.000 description 1
- 208000002474 Tinea Diseases 0.000 description 1
- 241000223238 Trichophyton Species 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 241000589634 Xanthomonas Species 0.000 description 1
- 241000607734 Yersinia <bacteria> Species 0.000 description 1
- 241000607447 Yersinia enterocolitica Species 0.000 description 1
- 241000588902 Zymomonas mobilis Species 0.000 description 1
- YKTSYUJCYHOUJP-UHFFFAOYSA-N [O--].[Al+3].[Al+3].[O-][Si]([O-])([O-])[O-] Chemical class [O--].[Al+3].[Al+3].[O-][Si]([O-])([O-])[O-] YKTSYUJCYHOUJP-UHFFFAOYSA-N 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 239000013543 active substance Substances 0.000 description 1
- 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
- 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
- 125000003118 aryl group Chemical group 0.000 description 1
- 244000052616 bacterial pathogen Species 0.000 description 1
- 230000008901 benefit Effects 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
- 239000001913 cellulose Substances 0.000 description 1
- 229920002678 cellulose Polymers 0.000 description 1
- 238000012512 characterization method Methods 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 239000004927 clay Substances 0.000 description 1
- 210000003555 cloaca Anatomy 0.000 description 1
- 229910052681 coesite Inorganic materials 0.000 description 1
- 239000002131 composite material Substances 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000007334 copolymerization reaction Methods 0.000 description 1
- 229910052593 corundum Inorganic materials 0.000 description 1
- 229910052906 cristobalite 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
- 230000002478 diastatic effect Effects 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
- 235000013399 edible fruits Nutrition 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
- 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
- 239000003205 fragrance Substances 0.000 description 1
- 230000002538 fungal effect Effects 0.000 description 1
- 150000002337 glycosamines Chemical class 0.000 description 1
- 239000008187 granular material 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
- 230000003301 hydrolyzing effect Effects 0.000 description 1
- 150000002460 imidazoles Chemical class 0.000 description 1
- 238000007654 immersion Methods 0.000 description 1
- 230000006872 improvement Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 230000000968 intestinal effect Effects 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
- 230000007774 longterm Effects 0.000 description 1
- 239000006210 lotion Substances 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
- 239000011572 manganese Substances 0.000 description 1
- 229910052748 manganese Inorganic materials 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
- 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
- 230000000474 nursing effect Effects 0.000 description 1
- 150000002894 organic compounds Chemical class 0.000 description 1
- 239000003960 organic solvent Substances 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
- 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
- 238000006116 polymerization reaction Methods 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
- 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
- 239000000377 silicon dioxide Substances 0.000 description 1
- VYPSYNLAJGMNEJ-UHFFFAOYSA-N silicon dioxide Inorganic materials O=[Si]=O VYPSYNLAJGMNEJ-UHFFFAOYSA-N 0.000 description 1
- 229910001388 sodium aluminate Inorganic materials 0.000 description 1
- 229910000029 sodium carbonate Inorganic materials 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
- 229910052682 stishovite Inorganic materials 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
- 229910052905 tridymite Inorganic materials 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
-
- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- C11D2111/00—Cleaning compositions characterised by the objects to be cleaned; Cleaning compositions characterised by non-standard cleaning or washing processes
- C11D2111/10—Objects to be cleaned
- C11D2111/12—Soft surfaces, e.g. textile
Landscapes
- Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Textile Engineering (AREA)
- Detergent Compositions (AREA)
Abstract
The present invention provides a washing machine which combines a sequential processing device for sequentially treating fabrics with at least a first enzyme and a second enzyme, said device comprising a plurality of separate chambers each containing the first enzyme and the second enzyme. The enzymes are sequentially dispensed from the chamber. The washing machine is characterized in that the first enzyme comprises proteases and the second enzyme comprises one or more kind of lipolytic enzymes.
Description
The application is application number 200880101706.X, 27 days June 2008 applying date, denomination of invention " sequential enzyme delivery
System " the divisional application of Chinese patent application.
Technical field
The present invention relates to enzyme sending successively in washing process pass.
Background technology
The enzymatic mixture used in laundry processes is known.WO2000070006 discloses protease/cellulose group
Close.WO20050089966, EP1664258, US20050059567 and US20060172913 disclose for remove grass and
The enzymatic mixture of the spot on egg.
Summary of the invention
Purpose is to provide the washing/decontamination method relating to enzyme of a kind of improvement.Owing to other components hydrolyze, therefore want
The enzymatic mixture providing a kind of protease to be one of key component is the most extremely difficult.
Therefore, in the first aspect, the present invention provides a kind of fabric cleaning process, different by least two in the method
Enzyme process fabric successively, described method includes step:
1. use one or more Protease Treatment, afterwards
2. process with one or more second enzymes,
It is characterized in that this kind in second step or various second enzyme and the protease in first step are different families
Race.
Preferably described second enzyme includes one or more lipolytic enzymes.
In second aspect, the present invention provides a kind of method removing spot from fabric, and it includes step:
1. use one or more Protease Treatment, afterwards
2. process with one or more second enzymes, it is characterised in that this kind in second step or various second enzyme and first
Protease in step is different families.
The preferred feature of the method for second aspect is also for first aspect.
Between described step or in the step of described step Yu another process, such as may have between rinse step
Time delay.
Preferably, the method for second aspect present invention is the method that grass is dirty that removes from fabric.
In one aspect of the method, the present invention provides a kind of fabric washing and/or decontamination suit, and it includes that at least one contains
First enzyme of first aspect present invention and the packaging of second enzyme, wherein this first enzyme and second enzyme are separated from one another, and described packaging is appointed
Choosing includes for the present invention first and/or the fabric washing of second aspect and/or the operation instruction of fabric decontaminating.
In further, the present invention provides a kind of washing machine, and it is used in and processes the device of fabric successively at least
Combine with the first enzyme according to the present invention and second enzyme, described device include multiple individually, each containing the first enzyme and the
The room of two enzymes, described enzyme is allocated out from this room successively.
Described device preferably includes washing machine drawer (drawer box).
In further, the present invention provides the first enzyme according to a first aspect of the present invention and second enzyme afterwards to depend on
The secondary spot processing fabric that is used in, the purposes in the method that particularly grass is dirty.
Described first enzyme and second enzyme can include the mixture of single enzyme or enzyme.
Minimize surprisingly, above-mentioned setting makes described enzyme be affected by other enzymes when effect.Root is it is contemplated that at first
The protease added may be attacked in addition to other enzymes in washing liquid, thus hinders the place of the nonproteolytic to spot
Reason.But, owing to being sequentially added into, therefore the clean effect of enzyme is greatly improved.
Detailed description of the invention
Suitable protease includes the protease deriving from animal, plant or microbial source.Preferably microbial source.Chemistry changes
Property or in the mutant of protein engineering is also included within.Protease can be serine protease or metalloproteases, preferably
Alkaline microbial protease or trypsin like proteases.The example of alkaline protease is subtilisin, particularly derived from
Those materials of bacillus, such as subtilisin Novo, subtilisin Carlsberg, subtilisin 309, hay bacteriolyze
Element 147 and subtilisin 168 (being described in WO 89/06279).The example of trypsin like proteases is Trypsin
Enzyme (such as, derive from pig or derive from cattle), and the mould egg of reaping hook described in WO 89/06270 and WO 94/25583
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 variant being particularly replaced 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.The most commercially available protease
Including AlcalaseTM、SavinaseTM、PrimaseTM、DuralaseTM、DyrazymTM、EsperaseTM、EverlaseTM、
PolarzymeTMAnd KannaseTM、(Novozymes A/S)、MaxataseTM、MaxacalTM、MaxapemTM、
ProperaseTM、PurafectTM、Purafect OxPTM、FN2TMAnd FN3TM(Genencor International Inc.)。
Suitable lipase includes those lipases deriving from antibacterial or fungus.Chemical modification or protein engineering
Mutant be also included within.The example of available lipase includes the fat deriving from detritus enzyme (with Thermomyces synonym)
Fat enzyme, such as the fat deriving from H.lanuginosa (T.lanuginosus) described in EP 258 068 and EP 305 216
Fat enzyme, or the lipase deriving from special detritus enzyme described in WO 96/13580, Pseudomonas Lipases, such as, originate
In pseudomonas pseudoalcaligenes or pseudomonas pseudoalcaligenes (EP 218 272), pseudomonas cepacia (EP 331 376), this apprentice thatch
Family name pseudomonas (GB 1,372,034), pseudomonas fluorescens, Rhodopseudomonas SD 705 strain (WO 95/06720 and WO 96/
27002), the lipase of P.wisconsinensis (WO 96/12012), bacillus cereus lipase, such as derive from hay bud
Spore bacillus (Dartois et al. (1993), Biochemica et Biophysica Acta, 1131,253-360), stearothermophilus
Bacillus cereus (JP 64/744992) or the lipase of 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 materials described in WO 97/04079 and WO 97/07202.
The most commercially available lipase includes LipolaseTMWith Lipolase UltraTM、LipexTM
(Novozymes A/S)。
It should be understood that within enzyme variants (such as, being prepared by recombinant technique) is also included within the implication of term " enzyme ".This
The example of enzyme variants is at such as EP 251,446 (Genencor), WO 91/00345 (Novo Nordisk), EP 525,610
(Solvay) and WO 94/02618 (Gist-Brocades NV) is disclosed.
The enzyme type that therefore, it can be suitably incorporated in the granule of the present invention includes oxidoreductase (EC
1.-.-.-), transferring enzyme (EC 2.-.-.-), hydrolytic enzyme (EC 3.-.-.-), lyase (EC 4.-.-.-), isomerase (EC
5.-.-.-) with ligase (EC 6.-.-.-).
For other main wash components, can add with independent measure and send the protease and steatolysis passed successively
Enzyme, or it can be measured together with this component addition, but protease is not combined with other enzymes.
The enzyme passed that send successively of the present invention can be together with one or more surfactants and/or other optional compositions
Send and pass, thus at least one in the material being sequentially added into is the laundry cleaning and/or care composition played one's part to the full.
This compositions of the present invention can be drying solid or liquid form.Described compositions can be dilution, water more before use
Close and/or be dissolved in solvent, including the concentrate in water.Described compositions can also be (general (in-use)) easy of use
Compositions.
The present invention is suitable for use in industry or domestic fabric cleaning compositions, fabric-conditioning compositions and washing and fabric is adjusted
In reason dual-purpose composition (so-called general washing care composition).The present invention can be additionally used in industry or domestic non-detergent base
Fabrid care composition, such as in spray composite.
The fabric cleaning composition of the present invention can be any suitable form, such as powder, flakelike powder, liquid or solid
Body detergent bar.
Other expected from composition is discussed below, including surfactant, hydrotrote, preservative, filler, builder,
Compounding ingredient, polymer, stabilizer, spice itself, other detergent compositions, or the combination of one or more.
Described enzyme can exist as the most reactive detergent, or can be combined with other detergents.
As a part for whole washing process, other enzyme can be measured input, condition is initial in the present invention
Add other after process (that is, with enzyme, such as protease and the second or more enzyme, such as lipase treatment afterwards)
Enzyme.
This other (that is, post-dised) enzyme can include above-mentioned further protease and lipase, with
And α-amylase, cellulase, peroxidase/oxidase, pectate lyase and mannase, or its mixture.
Other components are also possible that product at.EC 3.1.1.74 is classified.Use according to the present invention
Product at can be any source.It is microbe-derived for preferably producing at, and especially antibacterial, fungus or yeast comes
Source.
Producing at is the enzyme of cutin of can degrading.In preferred embodiments, at is produced derived from Eurotium
Bacterial strain, especially aspergillus oryzae；Alternaria bacterial strain, especially Caulis et Folium Brassicae capitatae rod method；Fusarium spp, especially fusariun solani, pea
Glycine max (L.) Merr. fusarium, Fusarium roseum culmorum or Fusarium roseum sambucium；Helminthosporium bacterial strain,
The especially compacted spore of Bulbus Allii length；Detritus Pseudomonas bacterial strain, the most special detritus enzyme；Pseudomonas strain, especially Mendoza are false
Zymomonas mobilis or pseudomonas putida；Rhizoctonia bacterial strain, especially Rhizoctonia solani；Streptomyces bacterial strain, especially shot hole
Streptomycete；Or list belongs to bacterial strain every spore, especially all living creatures's thin base lattice spore.In the most preferred embodiment, produce at derived from
Special detritus enzyme bacterial strain, the most special detritus enzyme strain DSM 180.Special detritus enzyme produces in WO 96/13580
Being described, it introduces through quoting.Producing at can be variant, such as described in WO 00/34450 and WO 01/92502
One of variant, it introduces through quoting.Preferably produce what cutinase variants included listing in the embodiment 2 of WO 01/92502
Variant, it introduces through quoting especially with regard to this.
Preferably business product at includes NOVOZYMTM51032 (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 by, term phosphorus lipase is the enzyme active to phospholipid.Phospholipid, such as lecithin or phosphatidylcholine are by outside
(sn-1) by two fatty acid esterifications and the glycerol group that is esterified by phosphoric acid on the 3rd position and on middle part (sn-2) position
Become；In turn, phosphoric acid can be esterified for amino alcohol.Phosphorus lipase is the enzyme participating in phospholipid hydrolysis.Can be to several phospholipid
The activity of fat enzyme makes a distinction, and it includes making a fatty acyl group (laying respectively on sn-1 and sn-2 position) hydrolyze to form haemolysis phosphorus
The phosphorus lipase A of fat1And A2；With lysophosphatide fat enzyme (or the phosphorus lipase that can hydrolyze remaining fatty acyl group in lysophosphatide
B).Phosphorus lipase C and phosphorus lipase D (phosphodiesterase) discharge DG or phosphatidic acid respectively.
Term phosphorus lipase includes the enzyme with phosphorus lipase active, and described activity is such as phospholipid fat enzyme A (A1Or A2)、
Phosphorus lipase B activity, phosphorus lipase C activity or phosphorus lipase D activity.Term used herein " phosphorus lipase A " with this
Bright enzyme combine intention covering there is phosphorus lipase A1And/or phosphorus lipase A2The enzyme of activity.Phosphorus lipase active can also be by
Having the enzyme of other activity, the lipase such as with phosphorus lipase active provides.Phosphorus lipase active can such as derive from
There is the lipase of phosphorus lipase time activity.In other embodiments of the present invention, the enzymatic activity of phosphorus lipase is by substantially
The enzyme only with phosphorus lipase active provides, and the enzymatic activity of wherein said phosphorus lipase is not time activity.
Phosphorus lipase can be any source, such as animal origin (such as, mammal), as derived from pancreas (such as,
Cattle or the pancreas of pig), or derive from the venom of Serpentis or the venom of Apis.Preferably, phosphorus lipase can be microbe-derived, example
As derived from filamentous fungi, yeast or antibacterial, such as aspergillus or kind, such as aspergillus niger；Dictyostelium, such as dictyostelium discoideum；Hair
Mould Pseudomonas, such as mucor javanicus, honeybee Mucor, thin spore Mucor；Neurospora, such as Neurospora；Rhizopus, such as Rhizomucor pusillus；Wine
Aspergillus, such as Rhizopus arrhizus, Japan rhizopus, 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 belongs to, such as citrobacter freundii；Enterobacter, such as clostridium perfringen, cloaca Edward enterobacteria, blunt intestinal 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, general sieve of Ru Sishi becomes to step on this bacterium；Salmonella
Belong to, such as Salmonella typhimurium；Serratia, such as serratia liquefacient, serratia marcesens；Shigella, as Freund will is congratulated
Bacterium；Streptomyces, such as Streptomyces violaceoruber；Yersinia, such as yersinia enterocolitica.Therefore, phosphorus lipase can
Think fungus, such as, derive from fruit capsule bacterium subclass, such as Fusarium, such as machete fusarium strain, different spore fusarium strain, causing root rot disease of Medicago sativa bacterium
Strain, or Fusarium oxysporum strain.Phosphorus lipase can also derive from the filamentous fungi strain belonging to aspergillus, such as bubble and contain inulinase
Strain, smelly aspergillosis strain, aspergillus japonicus strain, Aspergilus niger strain or aspergillus oryzae strain.
Preferably phosphorus lipase is derived from detritus enzyme strain, particularly pubescence detritus enzyme.Phosphorus lipase can be variant, example
One of variant as disclosed in WO 00/32758, the document introduces through quoting.Preferably phosphorus lipase Variant includes WO 00/
Variant listed in the embodiment 5 of 32758, the document introduces through quoting especially with regard to this.Another preferred embodiment party
In case, phosphorus lipase is described in WO 04/111216, variant the most listed.
Preferably, phosphorus lipase is derived from reaping hook bacterial strain, particularly Fusarium oxysporum.Phosphorus lipase can be WO 98/
In 026057 mentioned, derived from of Fusarium oxysporum DSM 2672, or its variant.
Phosphorus lipase is preferably phosphorus lipase A1Or phosphorus lipase A (EC.3.1.1.32)2(EC.3.1.1.4.)。
The example of commercial phosphorus lipase includes LECITASETMAnd LECITASETMULTRA, YIELSMAX or LIPOPAN F
(being purchased from NovozymesA/S, Denmark).
Suitable amylase (α and/or β) includes the amylase deriving from antibacterial or fungus.Chemical modification or protein
In engineered mutants is also included within.Amylase includes that, such as by bacillus, the most special Bacillus licheniformis strain obtains
The α-amylase obtained, GB 1,296, in 839, it is more fully described, or is obtained from WO 95/026397 or WO
The α-amylase of the Bacillus alcalophilus strain disclosed in 00/060060.
Available diastatic example is WO 94/02597, WO 94/18314, WO 96/23873, WO 97/43424,
WO 01/066712, WO 02/010355, (described document is all through quoting for 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 PurastarTM(originate from Genencor
International Inc.)。
Suitable cellulase includes those cellulase deriving from antibacterial or fungus.Chemical modification or protein engineering
In mutant is also included within.Suitable cellulase includes deriving from Bacillus, Rhodopseudomonas, Humicola, reaping hook
Pseudomonas, fusarium globosum shuttle belong to, the cellulase of Acremonium, 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,
Fungal cellulase prepared by Tai Ruisisuo spore shell enzyme, laccase and Fusarium oxysporum.
Especially appropriate cellulase is alkalescence or the neutral cellulase with color nursing benefit.This cellulase
Example EP 0 495 257, EP 0 531 372, WO 96/11262, fibre described in WO 96/29397, WO 98/08940
Dimension element 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)。
Suitable peroxidase/oxidase includes those enzymes of plant, antibacterial or originated from fungus.Chemical modification or albumen
In matter engineered mutants is 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.Commercially available
Peroxidase include GuardzymeTMAnd NovozymTM 51004(Novozymes A/S)。
The example of pectate lyase includes being belonged to by different antibacterials, such as Erwinia, Rhodopseudomonas Cray primary
The pectate lyase that Bordetella and Xanthomonas are cloned and come, and by bacillus subtilis (Nasser et al., (1993) FEBS
Letts.335:319-326) and bacillus cereus YA-14 (Kim et al., (1994) Biosci.Biotech.Biochem.58:
Pectate lyase 947-949) cloned and come.Also describe to that prepared by following bacterium, have in pH scope 8-10
The purification of the pectate lyase of big activity: Bacillus pumilus (Dave and Vaughn (1971) J.Bacteriol.108:
166-174), bacillus polymyxa (Nagel and Vaughn (1961) Arch.Biochem.Biophys.93:344-352), addicted to
Hot 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-independent and/or
Heat-staple pectate lyase may be used for putting into practice the present invention.In preferred embodiments, pectate lyase includes
Heffron et al. exists at (1995) Mol.Plant-Microbe Interact.8:331-334 and Henrissat et al.
(1995) the pectate lyase aminoacid sequence disclosed in Plant Physiol.107:963-976.It is especially contemplated that pectin
Acid lyase is disclosed in WO 99/27083 and WO 99/27084.Other it is especially contemplated that derived from lichenoid form spore
The pectate lyase of bacillus is disclosed in US patent no.6,284,524 (document introduces through quoting).The most pre-
The pectate lyase variant of phase is disclosed in WO 02/006442, specifically WO 02/006442 (document warp
Quote and introduce) embodiment disclosed in variant.
The example of commercially available alkaline pectin hydrochlorate lyase includes BIOPREPTMAnd SCOURZYMETML, it obtains
From Novozymes A/S, Denmark.
The example of mannase (EC 3.2.1.78) includes the mannase deriving from antibacterial and fungus.Special
Embodiment in, mannase belongs to aspergillosis strain, preferably aspergillus niger or aspergillus echinulatus (WO 94/ derived from filamentous fungi
25576).WO 93/24622 discloses the mannase separated from Richter scale wood enzyme.Mannase can also be from
Some antibacterials, separate including in bacillus Organic substance.Such as, Talbot et al. at Appl.Environ.Microbiol., 56
Volume, 11 phases, describes the 'beta '-mannase derived from bacstearothermophilus in 3505-3510 page (1990).Mendoza
Et al. at World J.Microbiol.Biotech., volume 10,5 phases, 551-555 page (1994) describe derived from hay bud
The 'beta '-mannase of spore bacillus.
JP-A-03047076 discloses the 'beta '-mannase derived from Bacillus alcalophilus.JP-A-63056289
In describe the preparation of 'beta '-mannase alkaline, heat-staple.JP-A-63036775 relate to producing 'beta '-mannase and β-
The micro-organisms bacillus of mannosidase.JP-A-08051975 discloses the bacillus cereus AM-001 deriving from basophilic
Alkaline ' beta '-mannase.WO 97/11164 discloses the mannase of the purification deriving from bacillus amyloliquefaciens.
WO 91/18974 describes hemicellulase, such as glucanase, xylanase or Mannanase Activity molecule.Expection
Be derived from the Bacillus agaradhaerens disclosed in WO 99/64619, Bacillus licheniformis, salt tolerant basophilic bud
The mannase of the alkaline family 5 and 26 of spore bacillus, Bacillus clausii, Alkaliphilic bacillus and special detritus enzyme.Special
Be not contemplated that the Bacillus alcalophilus mannase related in the embodiment of WO 99/64619, the document through quoting and
Introduce.
The example of commercially available mannase includes MannawayTM, it is purchased from Novozymes A/S
Denmark。
Can use the stabilizer of routine, such as polyhydric alcohol, 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 is deposited in compositions
Any enzyme carry out static stabilization, and can be according to the description in WO 92/19709 and WO 92/19708 by compositions
Make preparation.
Fabric cleaning composition can comprise the fabric washing material selected from lower group: non-soap anionic surfactant, non-
Ionic surface active agent, soap, amphoteric surfactant, zwitterionic surfactant and mixture thereof.
Be suitable in household or industrial automatic fabric washing machine use composition of detergent usually contain anion without
Soap surfactant or nonionic surfactant, or known to the skilled artisan according to art by both materials
Proper proportion is combined, and optionally mixes with soap.
The compound of many suitable detergent actives be all can obtain and at document, such as " Surface-
Active Agents and Detergents ", I and II volume, Schwartz, Perry&Berch are fully described.
Surfactant existence level in the composition can be 0.1%-60% weight.
Suitable nonionic surfactant is known for art those of skill in the art, and it includes 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；Fatty acid ester sulphonic acid ester
And mixture.Generally preferably sodium salt.If including described material, then based on fabric treatment composition, described combination
Thing usually contains about 1%-about 50%, the anion surfactant of preferably 10wt%-40wt%, such as LABS
Salt, alpha-alkene sulfonate, alkyl sulfate (aliphatic alcohol sulfate), alcohol ethyoxysulfates, secondary alkyl sulfonate, alpha-sulfo fat
Acid methyl ester, alkyl-or alkenyl succinic acid or soap.Preferably surfactant is the alkyl of alkyl ether sulfate and alkoxylate
Nonionic surfactant and alkylsulfonate or the mixture of alkyl ether sulfate.
Preferably alkyl ether sulfate is C8-C15 alkyl and has 2-10 mole to there occurs oxyethylation
(ethoxlation).Preferably alkyl sulfate be alkylbenzenesulfonate, especially alkyl chain length be C8-C15Straight chained alkyl
Phenylsulfate.Counter ion for anion surfactant is usually sodium, it is also possible to use other counter ions, such as
TEA or ammonium.Suitable anionic surface active substances can be purchased from market, its entitled ' Genapol 'TM, originate from Clariant.
Nonionic surfactant is also known for art those of skill in the art, and it includes primary and secondary alcohol second
Oxide, averagely has C 1-20 mole ethylene oxide, ethoxylation in especially every mol of alcohol8-C20Fatty alcohol, more especially
It is the C averagely in every mol of alcohol with 1-10 mole ethylene oxide, ethoxylation10-C15Primary and secondary fatty alcohol.Non-ethoxy
The nonionic surfactant of base includes alkyl polyglycoside, glycerol monoethers and polyhydroxy amides (glucamide).Can also use
The mixture of nonionic surfactant.If including described material, the most described compositions usually contains about 0.2%-about
40%, the nonionic surfactant of preferably 1-20wt%, more preferably 5-15wt%, such as alcohol ethoxylate, nonyl phenol second
Epoxide compound, alkyl polyglycoside, alkyl dimethyl amine oxide, ethoxylated fatty acids single ethanol amide, fatty monoethanol amide,
The polyhydroxy alkyl fatty acid amide of glycosamine or N-acyl N-alkyl derivatives (" glucamides ").
Available nonionic surfactant includes that primary and secondary alcohol b-oxide, particularly average every mol of alcohol have 1-35
Mole ethylene oxide, ethoxylation C8-C20Aliphatic alcohol, more particularly average every mol of alcohol has 1-10 moles
Ethylene, ethoxylation C10-C15Primary and secondary aliphatic alcohol.
Higher levels of surfactant (being up to close to 100%) can be used, but so may make preparation is left for help
The space of lotion and other components is the least, and may produce and need to do the sticky product of special processing.
Compositions can include hydrotrote.Term " hydrotrote " is often referred to improve some slightly soluble organic compound
The dissolubility of thing, the most water miscible compound.The example of hydrotrote includes sodium xylene sulfonate, SCM.
Compositions can comprise solvent, such as water, or organic solvent, such as isopropanol or glycerin ether.Solvent is generally deposited
It is in liquid or gel combination.
Compositions can contain metal-chelator, such as carbonate, bicarbonate and sesquicarbonate.Described metal-chelating
Agent can be bleaching stibilizer (that is, Heavy metal sequestrants).Suitable bleaching stibilizer 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 ester
(DETPMP).Generally, metal-chelator is not present in compositions part, then may damage because if metal ion loses efficacy
Microbial function.
Builder material can be 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 many
Valency chelating agen, such as ethylenediaminetetraacetic acid.
The example of precipitating builder material includes sodium orthophosphate and sodium carbonate.
The example of calcium ion-exchanged builder material includes various types of water-insoluble crystallization or amorphous aluminum silicate
Salt, the most known representative is zeolite, such as Wessalith CS, zeolite B (also referred to zeolite P), zeolite C, X zeolite, zeolite Y
And the type that zeolite P-is as described in EP-A-0,384,070.
Described compositions can also contain builder or compounding ingredient, ethylenediaminetetraacetic acid, the diethyl triamine five of 0-65%
Acetic acid, alkyl-or alkenyl succinic acid, nitrilotriacetic acid(NTA) or another kind of builder referenced below.Many builders for bleaching-
Stabilizer, this is owing to it can the reason of complexed metal ion.
If there is builder, the most described compositions can suitably contain less than 20%wt, preferably less than 10 weight %,
The most preferably in less than detergent builder compound of 10%wt.
Described compositions can be containing the crystalline aluminosilicate as builder, preferred as alkali aluminosilicate, more preferably
Sodium aluminosilicate.It generally exists with the level less than 15%w.Aluminosilicate is the material with following formula:
0.8-1.5M2O·Al2O3·0.8-6SiO2
Wherein M is univalent cation, preferably sodium.These materials contain some and combine water, and have at least 50mg CaO/
The calcium ion exchange capacity of g.In above formula, preferred sodium aluminosilicate contains 1.5-3.5 SiO2Unit.Retouch in detail as in document
Stating ground, it easily can be prepared by the reaction between sodium silicate and sodium aluminate.Surfactant and aluminosilicate are (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 " include diphosphate, triphosphate and phosphonates.The builder of other forms includes silicate, such as soluble silicon
Hydrochlorate, metasilicate, phyllosilicate (such as, originating from the SKS-6 of Hoechst).
In order to reduce preparation cost, carbonate (including bicarbonate and sesquicarbonate) and/or citric acid can be used
Salt is as builder.
Described compositions can comprise one or more polymer.Example is carboxymethyl cellulose, poly-(ethenyl pyrrolidone
Ketone), PEG, poly-(vinyl alcohol), poly-(vinylpyridine-N-oxide), poly-(vinyl imidazole), polycarboxylate, example
Such as polyacrylate, maleic acid/acrylic copolymer and lauryl methyl acrylates/acrylic copolymer.
Composition of detergent now generally uses polymer as so-called " dyestuff-migration inhibitor ".These materials
Prevent the migration of dyestuff, especially during long-term immersion in.Any suitable dyestuff-migration inhibitor all can be according to this
Invention uses.Generally, this dyestuff-migration inhibitor includes that polyvinyl pyrrolidone polymers, polyamine N-oxide are polymerized
Thing, NVP and the copolymer of N-vinyl imidazole, manganese phthalocyanine, peroxidase and mixture thereof.
DTI polymer the most nitrogenous, combination dye.In these materials, preferably cyclic amine, such as vinyl pyrrole
Alkanone and/or the polymer of vinyl imidazole and copolymer.
The polyamine N-oxide pllymers being applicable to the present invention contains the unit with following structural: R-AX-P；Wherein P
For polymerizable unit, N-O group may be coupled on this unit, or described N-O group can form the one of polymerizable unit
Part；A be one of having structure :-NC (O)-,-C (O) O-,-S-,-O-,-N=；X is 0 or 1；R is aliphatic, ethoxyquin fat
Fat race, aromatic series, heterocycle and alicyclic group or a combination thereof, the nitrogen-atoms of N-O group can be connected to it on or described N-
O group is a part for these groups, or described group can be connected on the two unit.Preferably polyamine N-oxide
It is heterocyclic group for wherein R, the such as material of pyridine, pyrroles, imidazoles, pyrrolidine, piperidines and derivant thereof.N-O group is permissible
Representated by general formula: N (O) (R ')0-3Or=N (O) (R ')0-1, little wherein each R ' represents aliphatic, fragrance independently
Race, heterocycle or alicyclic group or a combination thereof；And the nitrogen-atoms of N-O group can be connected on arbitrary above-mentioned group or
Form its a part.The pKa ＜ 10 of the amine oxide unit of polyamine N-oxide, preferably pKa ＜ 7, more preferably pKa ＜ 6.
Can use any main polymer chain, condition is that formed amine oxide is water miscible and has dyestuff and move
Move inhibition activity.The example of suitable polymer main chain is polyethylene, polyalkylene, polyester, polyethers, polyamide, polyimides, gathers
Acrylate and mixture thereof.These polymer include random or block copolymer, and one of them monomer type is amine N-oxygen
Compound, another monomer type is N-oxide.The amine of amine n-oxide polymer and amine n-oxide ratio are usually 10: 1-
1∶1,000,000.But, present in polyamine oxide polymer, the quantity of amine oxide groups can be according to suitable copolymerization
Effect or suitable N-oxide degree and become.The polyamine oxide of substantially any extent of polymerization can be obtained.Generally, averagely
Molecular weight is 500-1,000,000；More preferably 1,000-500,000；Most preferably 5,000-100,000.This preferred material kind
Class is herein referred to as " PVNO ".Preferably polyamine N-oxide is mean molecule quantity about 50,000 and amine and amine n-oxide
Poly-(4-vinylpridine-N-oxide) of ratio about 1: 4.
The further preferably copolymer of NVP and N-vinylimidazole polymers (as a kind, is referred to as
“PVPVI”).Preferably, the mean molecule quantity of described PVPVI is 5,000-1,000,000, more preferably 5,000-200,000, and optimum
Select 10,000-20,000, described molecular weight exists according to Barth et al.Chemical Analysis, volume 113, " Modern
" middle description, is determined Methods of Polymer Characterization by light scattering method.Preferably
PVPVI copolymer is generally of 1: the N-vinyl imidazole of 1-0.2: 1 and NVP mol ratio, and more preferably 0.8:
1-0.3: 1, most preferably 0.6: 1-0.4: 1.These copolymers can be straight chain or side chain.Suitable PVPVI copolymer
Including Sokalan(TM)HP56, it is available commercially from BASF, Ludwigshafen, Germany.
As dye transfer inhibitor, accordingly it is also preferred that mean molecule quantity is about 5,000-about 400,000, preferably from about 5,
The polyvinylpyrrolidonepolymers polymers (" PVP ") of 000-about 2000,000, more preferably from about 5,000-about 50,000.PVP's is upper
State character to have been disclosed in such as EP-A-262,897 and EP-A-256,696.Suitable PVP polymer includes Sokalan(TM)HP50, it is available commercially from BASF.Compositions containing PVP can also be about 500-about 100 containing mean molecule quantity, and 000,
The Polyethylene Glycol (" PEG ") of preferably from about 1,000-about 10,000.Preferably, count based on ppm, cleaning mixture send PEG and PVP passed
Ratio be about 2: 1-about 50: 1, more preferably from about 3: 1-about 10: 1.
As dye transfer inhibitor, equally appropriate is those obtained by modified polyethyleneimine polymers class material
Inhibitor, it is such as situation disclosed in such as WO-A-0005334.These modified polyethyleneimine polymers are water miscible
Or dispersible modified polyamine.Modified polyamine has been made further disclosure: US-A-4,548,744 by following documents；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-2829022；And JP-A-06313271.
Preferably, the dye transfer inhibitor selected from lower group is comprised according to the compositions of the present invention: polyvinylpyridine N-oxygen
Compound (PVNO), polyvinyl pyrrolidone (PVP), polyvinyl imidazol, NVP and N-vinyl imidazole
Copolymer (PVPVI), its copolymer, and mixture.
The amount of the dye transfer inhibitor in the present composition is the 0.01-10% of composition weight, preferably 0.02-
5%, more preferably 0.03-2%.
Described compositions can also contain other detergent compositions, such as fabric conditioner, promotes including clay, foam
Agent, foam inhibitor (anti-infusion), preservative, soil suspender, dirt reprecipitation inhibitor, other dyestuffs, antimicrobial, light
Learn brightening agent, tarnish inhibitor or spice.
The distribution drawer that can use self-action washing machine measures input enzyme successively, such as, uses the metering of pre-chamber wash to throw
Enter protease, and main chamber wash is used for measuring input lipase.
The present invention may be also used in hand operation, and enzyme, without other devices, is added sequentially to by this operation simply
Wash in the cleaning mixture of each article and can complete.
But, hand operation can relate to washing tool, such as scrubbing plant, and can incite somebody to action according to the order of the present invention
Described compositions is directly applied to described instrument, is used for cleaning medicated clothing by described instrument afterwards.
Described instrument or device can also be soaked and/or delivery device can be used as, in order in the present invention
Washing/decontamination (preferably go weeding dirty) method in send and pass described enzyme.
The example of the non-limiting embodiments of the present invention
Embodiment 1
Protease and lipase are gone the washing evaluation (Terg-O-Tometer) that weeding is dirty
Evaluate clean result in the following manner: with protease (Savinase 12TXT) and fat in detergent solution
Enzyme (Lipex 100T and lipolase 100T) washs by grass dirty in the way of single enzyme, combination and (washing 2 times) successively processes
The polyester sample (wfk30A) of dye.
The preparation of the sample polluted by grass: the weeds block on severe friction meadow is to produce all on clean fabric samples
Even bottle green circle spot, thus the manual prepared consumer goods with corresponding spot.
Washing: under mechanical stirring, is placed on dirty for grass sample (7 × 7cm) in Terg-O-Tometer bathtub, makes sample system
The component (table 1) of agent is in 11 and goes to cultivate 30 minutes in mineral water and at 37 DEG C.Stopped stirring when t=15 minute, use
11 go mineral water to rinse all spots, all spots are all transferred in the second bathtub taking turns enzyme.The most continuously stirred 15 points
Clock.In tap water, rinse sample, launch and make it be dried at dark, overnight at room temperature.
Evaluate: use Hunterlab UltraScan VIS reflexivity spectrophotometer color of measuring samples at 410nm
Color reflexivity.Results expression is Δ reflexivity=(RAfter washing-RBefore washing)Enzyme-(RAfter washing-R Before washing)Comparison, wherein R is the reflection at 410nm
Degree, it uses CIE L*a*b* (CIELAB) value generated.
Table 1. preparation forms
Table 2
In Terg-O-Tometer, savinase, savinase and lipase, and savinase and lipase afterwards
Clean result to cotton thread under low FH (FH6).All spots all use surfactant wash.Total concentration=1 μ of zymoprotein
g/ml。
Table shows how metering successively, when throwing in lipase the most again, significantly improve spot if adding protease
Remove.
Embodiment 2
Protease and lipase are gone the washing evaluation (microtitrator) that weeding is dirty
Evaluate clean result in the following manner: with protease (Savinase 12TXT) and fat in detergent solution
Enzyme (Lipex 100T) washs, in the way of single enzyme, combination enzyme and (washing 2 times) successively process, the cotton polluted by grass and tests
Use cloth.
The preparation of the cotton test cloth polluted by grass: use nail brush severe friction on clean bafta to mix
Grass (with the ratio of water 3: 1), carries out pre-flock with polyester textile, thus prepares the consumer goods with corresponding spot by hand.
Washing: under stirring (1150rpm), the test cloth polluted by grass is placed in the plate of microtitrator, makes
The component (table 1) of sample formulation is in 200 μ l and goes to cultivate 30 minutes in ring oscillator in mineral water and at 37 DEG C.This
The secondary situation testing the low water hardness (FH60) and the high water hardness (FH40).Suspended stirring when t=15 minute, go with 200 μ l
Mineral water rinses all spots, and is exposed in the second solution taking turns enzyme.The most continuously stirred 15 minutes.In tap water
Rinsing sample 2 times, by its dark, place at least 3 hours so that it is dried at 45 DEG C.
Evaluate: use platform reflexivity spectrophotometer measurement sample color reflection degree at 410nm.Results expression is
Δ reflexivity=(RAfter washing-RBefore washing)Enzyme-(RAfter washing-RBefore washing)Comparison, wherein R is the reflexivity at 410nm, and it 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 again after Savinase | 20.40 | 21.10 |
Table 3 in the plate of microtitrator, savinase, savinase and lipase, and savinase and afterwards
Lipase clean result to cotton thread under low FH (FH6).All of spot all uses surfactant wash.Zymoprotein total
Concentration=1 or 40 μ g/ml.S-L, savinase, use lipase the most again.
Table 4 in the plate of microtitrator, savinase, savinase and lipase, and lipase and afterwards
Savinase clean result to cotton thread under high FH (FH40).All of spot all uses surfactant wash.Zymoprotein
Total concentration=1 or 40 μ g/ml.S-L, savinase, use lipase the most again.
Of course it is to be understood that be not intended to limit the invention in the details of the embodiment above, these embodiments
It is only be described by way of example.
Claims (2)
1. a washing machine, the processing means successively being used for processing successively fabric is tied mutually by it with at least the first enzyme and second enzyme
Closing, described device includes multiple single, respective containing the first enzyme and the room of second enzyme, and described enzyme is sequentially allocated out from this room
Come, it is characterised in that described first enzyme includes protease, and described second enzyme includes one or more lipolytic enzymes.
2. the washing machine of claim 1, wherein said processing means successively 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 true CN105887421A (en) | 2016-08-24 |
| CN105887421B 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 |
| CN105073971A (en) * | 2013-02-14 | 2015-11-18 | 诺维信公司 | Industrial and institutional laundering using multi-enzyme compositions |
| BE1029579B1 (en) | 2021-06-29 | 2023-02-06 | Christeyns Nv | Method and apparatus for on-site preparation and dosing of an enzyme-containing detergent formulation |
Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US5164100A (en) * | 1990-12-11 | 1992-11-17 | Lever Brothers Company, Division Of Conopco, Inc. | Fabric softener compositions containing a polymeric fluorescent whitening agent |
| 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 |
| US6616705B2 (en) * | 2000-09-08 | 2003-09-09 | Cognis Deutschland Gmbh & Co. Kg | Laundry detergent compositions |
| 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 |
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|---|---|---|---|---|
| US4663278A (en) * | 1982-04-30 | 1987-05-05 | Syva Company | Agglutination dependent enzyme channeling immunoassay |
| 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 |
| US6955067B2 (en) * | 2002-03-28 | 2005-10-18 | The Procter & Gamble Company | Smart dosing device |
| DE60312989T2 (en) * | 2002-06-28 | 2007-12-13 | Reckitt Benckiser N.V. | surfactant |
| 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 |
| EP1907525A1 (en) * | 2005-07-11 | 2008-04-09 | 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 CN CN200880101706A patent/CN101772568A/en active Pending
- 2008-06-27 EP EP08774456A patent/EP2173845B1/en not_active Revoked
- 2008-06-27 CN CN201610102346.1A patent/CN105887421B/en active Active
- 2008-06-27 ES ES08774456T patent/ES2391357T3/en active Active
- 2008-06-27 WO PCT/EP2008/058294 patent/WO2009019075A1/en active Application Filing
- 2008-06-27 BR BRPI0814331A patent/BRPI0814331A2/en not_active Application Discontinuation
-
2010
- 2010-01-12 ZA ZA2010/00215A patent/ZA201000215B/en unknown
Patent Citations (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| 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 |
| US5164100A (en) * | 1990-12-11 | 1992-11-17 | Lever Brothers Company, Division Of Conopco, Inc. | Fabric softener compositions containing a polymeric fluorescent whitening agent |
| US6616705B2 (en) * | 2000-09-08 | 2003-09-09 | Cognis Deutschland Gmbh & Co. Kg | Laundry detergent compositions |
| 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 |
Also Published As
| Publication number | Publication date |
|---|---|
| EP2173845B1 (en) | 2012-07-11 |
| ZA201000215B (en) | 2011-03-30 |
| ES2391357T3 (en) | 2012-11-23 |
| CN105887421B (en) | 2019-04-09 |
| BRPI0814331A2 (en) | 2016-10-04 |
| US20100206013A1 (en) | 2010-08-19 |
| CN101772568A (en) | 2010-07-07 |
| EP2173845A1 (en) | 2010-04-14 |
| WO2009019075A1 (en) | 2009-02-12 |
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