CN103748205A - Enzyme system - Google Patents
Enzyme system Download PDFInfo
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- CN103748205A CN103748205A CN201280040074.7A CN201280040074A CN103748205A CN 103748205 A CN103748205 A CN 103748205A CN 201280040074 A CN201280040074 A CN 201280040074A CN 103748205 A CN103748205 A CN 103748205A
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- amylase
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Classifications
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- C—CHEMISTRY; METALLURGY
- C11—ANIMAL OR VEGETABLE OILS, FATS, FATTY SUBSTANCES OR WAXES; FATTY ACIDS THEREFROM; DETERGENTS; CANDLES
- C11D—DETERGENT COMPOSITIONS; USE OF SINGLE SUBSTANCES AS DETERGENTS; SOAP OR SOAP-MAKING; RESIN SOAPS; RECOVERY OF GLYCEROL
- 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
- 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
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- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Oil, Petroleum & Natural Gas (AREA)
- Wood Science & Technology (AREA)
- Organic Chemistry (AREA)
- Detergent Compositions (AREA)
- Enzymes And Modification Thereof (AREA)
- Chemical Or Physical Treatment Of Fibers (AREA)
Abstract
An enzymatic fabric treatment composition comprising the combination of (i) one or more psychrophilic enzymes, and (ii) one or more mesophilic enzymes and/or one or more thermophilic enzymes.
Description
The present invention relates to enzyme sending in washing process.
It is known in laundry (laundering) process, using enzyme mixture.
Washing/the decontamination method that the object of this invention is to provide improvement, it relates to for having the enzyme of the washings of variable uncontrolled temperature.
A first aspect of the present invention provides enzymatic fabric treatment composition, the combination that it comprises following material:
1. one or more have a liking for cold enzyme (psychrophilic enzyme), and
2. one or more have a liking for warm enzyme (mesophilic enzyme) and/or one or more Zimadzhunt L 340s (thermophilic enzyme).
A second aspect of the present invention provides the method for processing fabric according to the enzymatic fabric treatment composition of described first aspect of using, the wherein temperature of washings variation between low temperature (psychrophilic) and middle temperature (mesophilic) and optional high temperature (thermophilic) in whole single cycles of washing process.
Term used herein " single cycles of washing " means single washing process, and it comprises one or more water washing stages and one or more water rinse stage.Described circulating in after final rinsing finished, and then fabric is prepared to be dried and to re-use.Described circulation can comprise pretreatment stage.
Preferably, described temperature changes in whole single cycles of washing process between low temperature, middle gentle high temperature.
In the situation that the temperature of washings is not controlled by user at least a portion, the present invention is highly favourable.Preferably, described washings temperature is uncontrolled very in large quantities, and the more preferably uncontrolled degree that driven by envrionment conditions to temperature.Described method can comprise hand-washing to be processed or carries out in washing machine, and described washing machine preferably heats without any water.
Adopt the present invention, variation and not all aspect enzyme performance, solved by the combinatorial problem of the washings temperature that (user) control.Washings temperature is usually variation and uncontrolled.The variation of described temperature may occur in single washing process or in whole continuous washing process.For example, in warm weather, for hand washing, washing water can be obtained by the water tap supplying water by underground pipeline, and washing process can start then under warmer envrionment conditions, to be warming up to 20 ℃, 30 ℃, 40 ℃ or higher temperature under low temperature (5 to 15 ℃).The weather condition that change refer to that envrionment temperature changes at least seasonally.Adopt the present invention, these problems are by providing the combination of the enzyme of the function that expectation is provided in different temperature provinces to be solved.Even adopt automatic washing machine, the temperature of washings also may change between the whole usage period of a laundry product.
Term used herein " is had a liking for cold enzyme " and is meant effective enzyme at the temperature of 0 to 25 ℃.
Term used herein " is had a liking for warm enzyme " and is meant effective enzyme at the temperature of 25 to 50 ℃.
Term used herein " Zimadzhunt L 340 " means effective enzyme at the temperature of 50 to 90 ℃.
Term used herein " effectively " means ability or the catalytic capability that enzyme (in given temperature province) can be realized decontamination.
Term used herein " enzyme " comprises enzyme variants (for example preparing by recombinant technology).The example of such enzyme variants is disclosed in for example EP251, and 446 (Genencor), WO91/00345 (Novo Nordisk), EP525, in 610 (Solvay) and WO94/02618 (Gist-Brocades NV).
Preferably, decontamination is measured by alleviating (Remission) unit or alleviating index.Effectively decontamination preferably represents by being equal to or greater than 2 alleviations of alleviating unit.
In the situation of enzymatic fabric treatment composition, term " processing " used preferably means to clean and more preferably mean decontamination herein.
Enzyme can be from bacterium or originated from fungus.Comprise chemically modified or protein engineering mutant.
Preferably, described one or more are had a liking for cold enzyme and/or one or more and are had a liking for the enzyme that warm enzyme and/or one or more Zimadzhunt L 340s comprise common classification.This has the advantage that solves particular type spot under differing temps.In this case, preferably described common classification is proteolytic enzyme or lipase or glycosyl hydrolase or lyase or oxydo-reductase.
Alternatively, the present invention can comprise the enzyme of hybrid category.Preferably, this comprises and has a liking for cold enzyme and have a liking for warm enzyme.The advantage of this combination is the washing that process starts with low temperature, and wherein effectively still now suppressed proteolytic enzyme attacks described lipase to lipase.
have a liking for cold enzyme
Preferably, described one or more are had a liking for cold enzyme and are comprised esterase (ester hydrolase) and more preferably comprise carboxylic ester hydrolase, more preferably comprise for example lipase and/or Phospholipid hydrolase.
Lipase is the highly favourable cold enzyme of having a liking for, because fat and oil-based stains are more difficult to remove at low temperatures.For substantially identical reason, Phospholipid hydrolase is also favourable for low temperature.
Advantageously, alternatively or extraly, described one or more are had a liking for cold enzyme and comprised glycosyl hydrolase (glycosylase), such as cellulase, amylase (comprising α-amylase), zytase etc.
Having a liking for cold fat enzyme comprises from following lipase: No. 6 bacterial strain of acinetobacter (Acinetobacter sp.) (Suzuki etc. (2001) J.Biosci.Bioeng.92:144 – 148; Acinetobacter O16 bacterial strain (Brueuil and Kushner, (1975) Can.J.Microbiol.21:423-433; Separate fat achromobacter (Achromobacter lipolyticum) (Khan etc.; (1967); Biochem.Biophys.Acta.132:68-771967), Aeromonas (Aeromonas sp.) LPB4 bacterial strain (Lee etc. (2003), J.Microbiol.41:22-27, Aeromonas hydrophila (Aeromonas hydrophila) (Pemberton etc. (1997) FEMS Microbiol.Lett.152:1-10); Bacillus sphaericus (Bacillus sphaericus) MTCC7526 (Joseph.PhD Thesis (2006) Allahabad Agricultural Institute, Allahabd, IN); Leaf-head shape microbacterium (Microbacterium phyllosphaerae) MTCC7530, moraxella (Moraxell sp.) (Feller etc. (1990) FEMS Microbiol.Lett.66:239-244; Moraxella (Moraxella sp) TA144 (Feller etc. (1991) Gene.102:111-115; Separate fat luminous bacillus (Photobacterium lipolyticum) M37 (Ryu etc. (2006) Appl.Microbiol.Biotechnol.70:321 – 326); Pseudoalteromonas (Pseudoalteromonas sp.) Wp27 (Zeng etc. (2004) J.Microbiol.Biotechnol.14:952-958); (Giudice etc. (2006) J.Applied Microbiology101:1039-1048, Antarctic psychrophilic bacteria belong to (Pscychrobacter sp.) and Vibrio (Vibrio sp.) to Pseudoalteromonas; Antarctic psychrophilic bacteria belongs to Wp37 (Zeng etc. (2004) J.Microbiol.Biotechnol.14:952-958); Sea of Okhotsk Psychrobacter belongs to (Psychrobacter okhotskensis sp.) (Yumoto etc. (2003) Int.J.Syst.Evol.Microbiol.53:1985 – 1989); Antarctic psychrophilic bacteria belongs to Ant300 (Kulakovaa etc. (2004) Biochemica.Biophysica.Acta.1696:59-65); Motionless Psychrobacter (Psychrobacter immobilis) bacterial strain B10 (Arpigny etc. (1997) J.Mol.Catal.B Enzy.3:29-35.), emplastic serratia (Serratia marcescens) (Abdou, (2003) J.Dairy Sci.86:127 – 132, streptococcus aureus (Staphylococcus aureus) (Alford and Pierce, (1961) J.Food Sci.26:518-524), staphylococcus epidermidis (Staphylococcus epidermidis) (Joseph etc. (2006) J.Gen.Appl.Microbiol.52:315-320).
Have a liking for esterase EstAT1 and EstAT11 that cold esterase preferably includes the descriptions in Mar Biotechnol (2009) 11:307 – 316 such as Jeon.
Have a liking for cold glycosyl hydrolase and preferably include Glycosylase, amylase for example, such as from trip extra large Pseudoalteromonas (Pseudoalteromonas haloplanktis) bacterial strain TAC125, replace Zymomonas mobilis (Alteromonas haloplanktis) A23 (Feller etc. (1998) Journal Biological Chemistry Vol273, No.20 12109-12115 page) and from the α-amylase of Nocardiopsis (Nocardiopsis sp.) 7326 from tetraodotoxin; Cellulase and zytase, from for example Clostridium (Clostridium sp.) PXYL1's (G.Akila, T.S.Chandra (2003) FEMS Microbiol.Letters219,63-67).Have a liking for cold zytase and comprise intestinal bacteria (E.coli) phagemid (2006b such as Lee).
Preferably having a liking for cryoproteins enzyme comprises and is derived from flavobacterium balustinum (Flavobacterium balustinum) P104 (the separated internal organ from salmon, and in February 17 nineteen ninety-five, be preserved in national bio-science and mankind technical institute---industrial science technology Agcy (National Institute of Bioscience and Human-Technology, Agency of Industrial Science and Technology), its preserving number is FERM BP-5006, and be recorded in WO/1996/025489) and be derived from Arthrobacter globiformis (Arthrobacter globiformis) S155 (Poitier etc., (1995) J.Gen.Microbiol.133:2797-2806) those.
Have a liking for cold lyase and preferably include pectin lyase, such as from the extra large Pseudoalteromonas strains A NT/505 of trip (Truong etc. (2001) Extremophiles5:35-44).
have a liking for warm enzyme
Preferably, described one or more are had a liking for warm enzyme and are comprised proteolytic enzyme and/or Glycosylase and/or pectin lyase.
Preferably have a liking for warm proteolytic enzyme and comprise serine protease or metal matrix proteolytic enzyme, preferably, the albumen pancreas of alkaline microbial protease or tryptase (trypsin-like protease).Sumizyme MP comprises subtilisin (subtilisin), especially be derived from those of bacillus (Bacillus), for example subtilisin Novo(subtilisin Novo), subtilisin Carlsberg(subtilisin Carlsberg), subtilisin 309(subtilisin309), subtilisin 147(subtilisin147) and subtilisin 168(subtilisin168).Described tryptase is (can cracking at the peptide bond at Methionin or arginic C-end side place.) such proteolytic enzyme can derive from pig or ox.Also comprise the trypsinase that is derived from sickle-like bacteria (Fusarium).
Commercially available proteolytic enzyme comprises Alcalase
tM, Savinase
tM, Primase
tM, Duralase
tM, Dyrazym
tM, Esperase
tM, Everlase
tM, Polarzyme
tMand Kannase
tM, (Novozymes A/S), Maxatase
tM, Maxacal
tM, Maxapem
tM, Properase
tM, Purafect
tM, Purafect OxP
tM, FN2
tMand FN3
tM(Genencor International Inc.).
Preferably having a liking for warm lipase comprises from Humicola (Humicola) lipase of (also claiming thermophilic fungus to belong to (Thermomyces)), for example, from comb and parallel cotton fibers prior to spinning shape humicola lanuginosa (H.lanuginosa(T.lanuginosus)) or from Humicola insolens (H.insolens); Rhodopseudomonas (Pseudomonas) lipase, for example, from Pseudomonas alcaligenes (P.alcaligenes) or pseudomonas pseudoalcaligenes (P.pseudoalcaligenes), pseudomonas cepacia (P.cepacia), pseudomonas stanieri (P.stutzeri), Pseudomonas fluorescens (P.fluorescens), pseudomonas strain SD705(WO95/06720 and WO96/27002), Wisconsin pseudomonas (P.wisconsinensis); Bacillus lipase, such as from subtilis (B.subtilis) (Dartois etc. (1993), Biochemica et Biophysica Acta, 1131,253-360), bacillus acidocldarius (B.stearothermophilus) (JP64/744992) or bacillus pumilus (B.pumilus) (WO91/16422).
Commercially availablely have a liking for warm lipase and comprise Lipolase
tMwith Lipolase Ultra
tM, Lipex
tM(Novozymes A/S).
Preferably have a liking for the enzyme that warm Phospholipid hydrolase (EC3.1.1.4 and/or EC3.1.1.32) comprises hydrolytic phosphatide.Comprise that a fatty acyl group of hydrolysis (respectively in sn-1 and sn-2 position) is to form the phospholipase A of lysophospholipid
1and A
2; With the lysophospholipase (or phospholipase B) that can be hydrolyzed remaining fatty acyl group in lysophospholipid; But also comprising Phospholipase C and Phospholipase D (phosphodiesterase), it discharges respectively DG or phosphatidic acid.
The relevant term " phospholipase A " of enzyme used herein and of the present invention means to contain has phospholipase A
1and/or phospholipase A
2active enzyme.Phospholipase activity also can for example, provide by also having other active enzymes (lipase with phospholipase activity).
It is described that to have a liking for warm Phospholipid hydrolase can be any source, for example animal source (for example Mammals), for example derive from pancreas (for example ox or pig pancreas) or snake venom or bee venom.Preferably, Phospholipid hydrolase can be microbial source, for example, be derived from filamentous fungus, yeast or bacterium, for example Aspergillus or kind, for example aspergillus niger; Dictyostelium (Dictyostelium), for example dictyostelium discoideum (D.discoideum); Mucor (Mucor), for example mucor javanicus (M.javanicus), mucor mucedo (M.mucedo), thin spore Mucor (M.subtilissimus); Neurospora (Neurospora), for example Neuraspora crassa (N.crassa); Rhizomucor (Rhizomucor), for example Rhizomucor pusillus (R.pusillus); Rhizopus (Rhizopus), for example rhizopus arrhizus (R.arrhizus), routine Japanese head mold (R.japonicus), rhizopus stolonifer (R.stolonifer); Sclerotinia (Sclerotinia), for example soybean sclerotinite (S.libertiana); Hair moss Pseudomonas (Trichophyton), for example red hair moss bacterium (T.rubrum); Vickers Sclerotinia (Whetzelinia), for example W.sclerotiorum; Bacillus, for example bacillus megaterium, subtilis; Citrobacter (Citrobacter), for example citrobacter freundii (C.freundii); Enterobacter (Enterobacter), for example enteroaerogen (E.aerogenes) or enterobacter cloacae (E.cloacae); Edwardsiella (Edwardsiella), blunt tarda (E.tarda); Erwinia (Erwinia), for example grass raw Erwinia (E.herbicola); Escherichia (Escherichia), for example intestinal bacteria; Klebsiella, for example Klebsiella pneumonia (K.pneumoniae); Proteus (Proteus), for example proteus vulgaris (P.vulgaris); Providencia (Providencia), for example providencia stuartii (P.stuartii); Salmonella, for example Salmonella typhimurium (S.typhimurium); Serratia (Serratia), for example liquefied Serratia (S.liquefasciens), serratia marcescens (S.marcescens); Shigella (Shigella), for example shigella flexneri (S.flexneri); Streptomyces, for example Streptomyces violaceoruber (S.violeceoruber); Or Yersinia, for example yersinia entero-colitica (Y.enterocolitica).Therefore Phospholipid hydrolase can come from for example Mycophyta, pyrenomycetes (Pyrenomycetes) class for example, as fusarium (genus Fusarium), the for example bacterial strain of machete sickle spore (F.culmorum), different spore sickle spore (F.heterosporum), fusarium solanae (F.solani), or the bacterial strain of sharp sickle spore (F.oxysporum).Phospholipid hydrolase can also be from the filamentous fungal strains in Aspergillus, for example the bacterial strain of Aspergillus awamori (Aspergillus awamori), smelly aspergillus (Aspergillus foetidus), aspergillus japonicus (Aspergillus japonicus), aspergillus niger or aspergillus oryzae (Aspergillu oryzae).
Preferably having a liking for warm Phospholipid hydrolase is the bacterial strain that is derived from Humicola, especially dredges cotton shape humicola lanuginosa bacterial strain or variant; And be the bacterial strain that is derived from sickle-like bacteria, the bacterial strain of especially sharp sickle spore.Phospholipid hydrolase can be derived from sharp sickle spore DSM2672.
Preferably, have a liking for warm Phospholipid hydrolase and comprise phospholipase A
1or phospholipase A (EC.3.1.1.32)
2(EC.3.1.1.4).
The commercially available example of having a liking for warm Phospholipid hydrolase comprises LECITASE
tMand LECITASE
tMuLTRA, YIELSMAX or LIPOPAN F(can be purchased from Novozymes A/S, Denmark).
Preferably having a liking for warm at (EC3.1.1.74.) is the bacterial strain that is derived from Aspergillus, especially aspergillus oryzae (Aspergillus oryzae); Alternaric bacteria strain, particularly Alternaria brassicicola (Alternaria brassiciola); Fusarium (Fusarium) bacterial strain, particularly Fusaium solani (Fusarium solani), pea root-rot Fusariumsp (Fusarium solani pisi), the pink Fusariumsp of machete (Fusarium roseum culmorum) or the pink Fusariumsp of Williams Elder Twig (Fusarium roseum sambucium); Helminthosporium (Helminthosporum) bacterial strain, the particularly wheat root-rot length spore bacterium (Helminthosporum sativum) that wriggles; Humicola bacterial strain, particularly Humicola insolens; Pseudomonas strain, particularly pseudomonas mendocina (Pseudomonas mendocina), or pseudomonas putida (Pseudomonas putida); Rhizoctonia (Rhizoctonia) bacterial strain, particularly dry thread Pyrenomycetes (Rhizoctonia solani); The sick streptomycete (Streptomyces scabies) of streptomyces (Streptomyces) bacterial strain, particularly scabies; Or thin base lattice spore belongs to (Ulocladium) bacterial strain, particularly all living creatures thin base lattice spores (Ulocladium consortiale).Most preferably, at is derived from Humicola insolens bacterial strain, particularly Humicola insolens DSM1800 bacterial strain.
Commercially available at comprises NOVOZYM
tM51032 (can purchased from Novozymes A/S, Denmark).
Preferably having a liking for warm amylase (α and/or β) for example for example comprises, available from bacillus (bacterial strain NCIB8059, ATCC6634, ATCC6598, ATCC11945, ATCC8480, the ATCC9945a of Bacillus licheniformis (B.licheniformis); Or Bacillus strain DSM12649 (AA560 α-amylase) or bacillus DSM12648 (AA349 α-amylase)) α-amylase.
Commercially availablely have a liking for warm amylase and have Duramyl
tM, Termamyl
tM, Termamyl Ultra
tM, Natalase
tM, Stainzyme
tM, Fungamyl
tMand BAN
tM(Novozymes A/S), Rapidase
tMand Purastar
tM(can purchased from Genencor International Inc.).
Preferably have a liking for warm cellulase and comprise the cellulase from bacillus, Rhodopseudomonas, Humicola, fusarium, Thielavia (Thielavia), Acremonium (Acremonium), for example, the fungal cellulase being produced by Humicola insolens, autochthonal shuttle spore mould (Thielavia terrestris), thermophilic fungus destroyed wire (Myceliophthora thermophila) and Fusarium oxysporum (Fusarium oxysporum).
Especially preferredly have a liking for warm cellulase for thering is alkalescence or the neutral cellulase that protects look (color care) benefit.Commercially available cellulase comprises Celluzyme
tM, Carezyme
tM, Endolase
tM, Renozyme
tM(Novozymes A/S), Clazinase
tMwith Puradax HA
tM(Genencor International Inc.), and KAC-500 (B)
tM(Kao Corporation).
Preferably having a liking for warm pectate lyase comprises and is derived from pectate lyase following or that obtained by following clone: bacterium belongs to such as erwinia, Rhodopseudomonas, Klebsiella and xanthomonas and subtilis (Nasser etc., FEBS Letts.335:319-326) and bacillus YA-14 (Kim etc., (1994) Biosci.Biotech.Biochem.58:947-949) (1993), bacillus pumilus (Bacillus pumilus) (Dave and Vaughn, (1971), J.Bacteriol.108:166-174), bacillus polymyxa (B.Polymyxa) (Nagel and Vaughn, (1961), Arch.Biochem.Biophys.93:344-352), bacillus acidocldarius (B.stearothermophilus) (Karbassi and Vaughn, (1980), Can.J.Microbiol.26:377-384), bacillus (Hasegawa and Nagel, (1966), J.Food Sci.31:838-845) and genus bacillus RK9 (Kelly and Fogarty, (1978), Can.J.Microbiol.24:1164-1172).Can use non-divalent cation dependent form and/or heat-staple pectin lyase.
Commercially available obtain that the alkaline example of having a liking for warm pectate lyase comprises can be purchased from Novozymes A/S, the BIOPREP of Denmark
tMand SCOURZYME
tMl.
Preferably having a liking for warm mannase (EC3.2.1.78) comprises and is derived from following mannase: Aspergillus filamentous fungus belongs to (filamentous fungus genus Aspergillus) bacterial strain, preferably aspergillus niger (Aspergillus niger) or microorganism Aspergillus aculeatus (Aspergillus aculeatus) or Trichodermareesei (Trichoderma reesei); Or micro-organisms bacillus FERM P-8856, it produces 'beta '-mannase and beta-Mannosidase; Or Alkaliphilic bacillus AM-001; Or bacillus amyloliquefaciens.Described mannase can comprise the mannase of the alkalescence 5 He26 families that are derived from Bacillus agaradhaeren, Bacillus licheniformis, Alkaliphilic bacillus, Bacillus clausii, bacillus and Humicola insolens.
The commercially available example that obtains mannase comprises can be purchased from Novozymes A/S, the Mannaway of Denmark
tM.
Preferably have a liking for warm peroxidase/oxydase and comprise and be derived from Coprinus (Coprinus), for example peroxidase and the variant thereof of Coprinus cinereus (C.cinereus).Commercially available peroxidase comprises Guardzyme
tMand Novozym
tM(Novozymes A/S).
zimadzhunt L 340
Thermophilic protease comprises being derived to be had a liking for
heatbacillus strain HS08 (African Journal of Biotechnology Vol.5 (24), 2433-2438 page, on December 18th, 2006) and bacstearothermophilus (B.Stearothermophilius) 1503; Thermos caldophilus GK24; Thermus aquaticus (T.Aquaticus) T351; The proteolytic enzyme of thermus aquaticus YT1Aq.I and Aq.II.
Have a liking for
heatlipase comprises that those and the preferred source that are derived from bacstearothermophilus (Bacillus thermocatenulatus) BTL1 are from BTL2 (Schimdt-Dannert etc., Biochim.Biophys.Acta (1994) 1214,114 pages of the 43rd 5 pages of – and Biochim.Biophys.Acta the (1996) 1301, the 105th –) those.
Have a liking for
heatglycosyl hydrolase comprises and is derived from thermophilic chain gemma bacillus Donk, bacterial strain BS-1 (Journal Biochemistry, Vol67,1:65-75) and the α-amylase that is derived from bacillus ANT-6 (Process Biochemistry (May2003) Vol38,10:1397-1403).Have a liking for
heatlyase comprises the pectin lyase that is derived from Italian thermophilic anaerobic Bacillaceae (Thermoanaerobacter italicus sp.) nov. strains A b9 (Kozianowski etc., (1997) Extremophiles Vol1,4:171-182).
Once selected each suitable enzyme according to the present invention, separatedly to those skilled in the art can produce the suitable microorganism of this enzyme and implement as known in the art for the preparation of in for example powder or liquid composition and/or be relatively easy in the inferior optimization step with the enzyme of required stability/performance of some wash conditions.
Fabric treatment composition can comprise laundry/clean fabric/care composition and can comprise one or more tensio-active agents and/or other optional composition.
This composition of the present invention can be drying solid form, for example powdered, particle or plate or liquid or gel form.It can be also the form of solid cleaning agent rod.Described composition can be enriched material, and it is diluted before use, rehydrated and/or be dissolved in solvent (comprising water).Described composition can be also to use (in use) composition.
The present invention is suitable for industry or domestic fabric cleaning composition, fabric-conditioning compositions and for the composition (so-called by washing conditioner composition) of laundering of textile fabrics and conditioning fabric.The present invention also can be applied to the non-detergent based Fabrid care composition of industry or family expenses, for example, directly use for example to roll and smear (roll-on) or spray composition, and described composition can be as for example part of pretreating fabrics before " master " washes.
Enzyme can be with the 0-5 % by weight of composition, preferably 2-4 % by weight and most preferably 2.5-3.5 % by weight (wherein wt % means the per-cent of composition total weight) existence.
In washings, (total size of enzyme of the present invention) total protein concentration is preferably 0.01 to 10.0mg/L and more preferably 2 to 5mg/L.
The total protein concentration of composition and % by weight will comprise respectively the cold enzyme of having a liking for of each level/have a liking for warm enzyme and optional Zimadzhunt L 340; And within this combination, described level can be when for example each enzyme be used separately half of level used.This is possible, because realized at a temperature, when peak value may seem to provide very large validity in that temperature range, and outside this scope, exists in the uncontrolled washing process of temperature therein minimum or there is no an activity.Adopt the present invention, it is in the whole uncontrolled temperature range of Actual laundering that realizes validity, to have the enzyme of validity and this for example, lower than (half) combination of level separately, this means and temperature sensitive enzymatic performance composition can be provided and the cost of said composition be maintained to reasonable level (because total enzyme content is not higher and even may be lower) simultaneously.
Enzyme can be unique fabric-treating agent, or also can be incorporated to other stain remover.
Other detergent ingredients that can comprise comprises tensio-active agent, washing assistant (builder), sequestrant, hydrotropic solvent, sanitas, complexing agent, polymkeric substance, stablizer, spices, white dyes, or other composition for example fabric conditioner (comprises clay, profoamer, suds suppressor (defoamer), anticorrosive agent, dirt suspension agent, anti-stain deposition agent, biocide, stain inhibitor (tarnish inhibitor) again, and its one or both combination, prerequisite is that these compositions are compatible with described enzyme.
Fabric cleaning composition can comprise fabric washing agent material, and it is selected from non-soap anionic surfactant, nonionogenic tenside, soap, amphoterics and zwitterionics and its mixture.The exist level of tensio-active agent in composition can be 0.1 % by weight to 60 % by weight.
Any enzyme being present in composition can adopt conventional stablizer to stablize, for example for example aromatic boric acid ester or phenyl-boron dihydroxide derivative (for example 4-formyl radical phenyl-boron dihydroxide) of polyvalent alcohol (for example propylene glycol or glycerine), sugar or sugar alcohol, lactic acid, boric acid or boric acid derivatives.
the embodiment of non-limiting embodiments of the present invention
Now with reference to the following drawings, various non-limiting embodiments of the present invention are done to describe more specifically, wherein:
Accompanying drawing 1-3 corresponds respectively to table 1-3a, b, and has shown that enzyme AHA is used and use together with both separately efficacy data under various conditions with Stainzyme.
Clone, preparation and purifying (from the extra large Pseudoalteromonas bacterial strain TAB23's of trip) are had a liking for cold diastatic illustrative methods:
Clone is from the method for having a liking for cold enzyme of the obtainable geneseq database of the public
That in embodiments of the invention, from the document through the peer review, determines that α-amylase (hereinafter referred to as AHA) has an expectation has a liking for cold property (Feller, G. etc., 1992; J.Biol.Chem.267 (8), 5217-5221).From the obtainable database of the public (http://www.ncbi.nlm.nih.gov/nuccore/2467084), (Fig. 1) obtain and comprise described diastatic gene order (GenBank accession number: X58627.1), and it is modified can be beneficial to the mode of the expression of recombinant protein and be incorporated to intestinal bacteria consistency plasmid carrier pUC19 via computer simulation (in silico).Fig. 2 shows for prepare the modified sequence of protein intestinal bacteria, and Fig. 3 is once the sequence that is incorporated to the AHA of pUC19 carrier.As the service of Eurogentec Ltd (Southampton, UK), the sequence shown in Fig. 2 that adopted they self proprietary method chemosynthesis is also inserted into pUC19 plasmid (shown in Fig. 3).
The method of cold α-amylase AHA is had a liking in preparation
The pUC19 plasmid that 10ng is contained to AHA-coding DNA is transformed into chemically active coli strain HB101, and tiling, to containing on the LB agar of 100 μ g/ml Pyocianils (carbenicillin), is cultivated and spent the night at 37 ℃.Then the LB substratum that the volume that single bacterium colony is contained to 100 μ g/ml Pyocianils for inoculating (2L shaking flask) is 0.5L.Bottle is hatched to 24-36 hour in 18 ℃ with 120rpm on orbital shaker, now cell is separated from substratum to (centrifugal, 10,000g, 15 minutes, 4 ℃).Substratum containing restructuring AHA is stored until while needing at 4 ℃.
Diastatic composition is produced to adopt by Roche Diagnostics and is confirmed as follows in the microtiter plate of 96-hole with the reagent of test kit (products catalogue numbers 11876473316) form supply: each sample to be evaluated (or its dilution) of 10 μ l is joined in the hole of described microtiter plate (in duplicate).Add 75 μ l reagent 1, then add 15 μ l reagent 2.Blank testing comprises described additive, containing the growth medium of AHA, uses without the LB using and replaces.Plate, the lower hatching of assigned temperature (being generally 20 ℃) 30 minutes, then on being set as the FluoStar Optima microplate reader at 405nm place, absorbance detection is evaluated to the release (due to amylase activity) of nitrophenols.
The method of purification of Recombinant AHA
First 1-2L is once diluted with the ratio of 1:2 with sterile distilled water containing the LB growth medium of AHA, then made to be concentrated to the following methods between 300ml to 500ml: using and adopting nominal molecular weight cut-off is the tangential cross flow filter of 30,000 daltonian regenerated cellulose filter for installations.Then (containing AHA's) concentrated LB is carried out to purifying in the following manner: by ion-exchange chromatography (using the Macro-Prep High Q ion-exchange Zai Ti – BioRad of 100ml), then by adopting 1.5cm x60cm S200 chromatographic column (GE Healthcare) to carry out gel-filtration.Use above-mentioned amylase test to determine the fraction containing AHA, and analyze and use coomassie method albumen spot (Imperial stain – ThermoPierce) assess proteins 49000 daltonian existence (and purity) of expection by SDS-PAGE.
enzyme combination A, B, C, D, E are as follows.
In each combination A-D, described combination comprises one or more and has a liking for cold enzyme and have a liking for warm enzyme and/or Zimadzhunt L 340.
tested enzyme validity in following composition
Example explanation improves the method for the catalytic activity of α-amylase composition solution in wide temperature range, and wherein said temperature range comprises low temperature, middle gentle high temperature (term as defined herein).
Employing is determined AHA, Stainzyme and AHA and the Stainzyme alpha-amylase activity between the temperature of 20 ℃ to 50 ℃ together by Roche Diagnostics with the reagent of test kit (products catalogue numbering 11876473316) form supply.
The stock solution of each enzyme (AHA of 1mg/ml, the Stainzyme of 0.5mg/ml) is preparation in buffer A (100mM Hepes, 100mM NaCl, 1mM CaCl, pH7.0).Described enzyme stock solution ratio with 1:125 in buffer A is further diluted and is mixed in following each reaction mixture on ice:
1) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted Stainzyme of 0.3ml
2) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted AHA of 0.3ml
3) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2,0.3ml buffer A (negative control)
4) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted Stainzyme of 0.15ml, the diluted AHA of 0.15ml
The aliquots containig of 100 μ l is transferred to immediately to 0.2ml thin-walled 96-hole PCR plate (every kind of reaction mixture 2 permutation holes provide the reading of two repetitions for the temperature of each evaluation) and can in the PCR instrument (Techne TC-500) of operating temperature gradient, so cultivating:
Described instrument is set and makes to move the thermograde between 20 ℃ and 50 ℃.The sample being distributed in the PCR plate of 96-hole is hatched just in time 30 minutes under these conditions, now PCR plate is cooled to rapidly to 4 ℃.During this cooling step, the 1M tris.base of 50 μ l (without what cushion) is joined to each hole so that reaction stops (preventing from further discharging nitrophenols reaction product).After fully mixing, each reaction mixture of 100 μ l is transferred in clean flat-bottom microtiter plates and use Fluostar Optima microplate reader to evaluate the absorbancy at 405nm place.Blank value under each probe temperature is deducted from the result obtaining containing enzyme mixture.The results are shown in Fig. 1.
In the modification of described test, the stock solution of each enzyme (AHA of 1mg/ml, the Stainzyme of 0.5mg/ml) is preparation in buffer A (100mM Hepes, 100mM NaCl, 1mM CaCl, pH7.0).Described enzyme stock solution is further diluted and is mixed in following each reaction mixture on ice with the ratio of 1:250 by buffer A:
1) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2,0.15ml buffer A, the diluted Stainzyme of 0.15ml
2) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2,0.15ml buffer A, the diluted AHA of 0.15ml
3) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2,0.3ml buffer A (negative control)
4) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted Stainzyme of 0.15ml, the diluted AHA of 0.15ml
The aliquots containig of 100 μ l is transferred to immediately to 0.2ml thin-walled 96-hole PCR plate (every kind of reaction mixture 2 permutation holes provide the reading of two repetitions for the temperature of each evaluation) and can in the PCR instrument (Techne TC-500) of operating temperature gradient, so cultivating:
Described instrument is set and makes to move the thermograde between 20 ℃ and 50 ℃.By the sample being distributed in the PCR plate of 96-hole, hatching is just in time 30 minutes under these conditions, now PCR plate is cooled to rapidly to 4 ℃.During this cooling step, the 1M tris.base of 50 μ l (without what cushion) is joined to each hole so that reaction stops (preventing from further discharging nitrophenols reaction product).After fully mixing, each reaction mixture of 100 μ l is transferred in clean flat-bottom microtiter plates and use Fluostar Optima microplate reader to evaluate the absorbancy at 405nm place.Blank value under each probe temperature is deducted from the result obtaining containing enzyme mixture.The results are shown in Fig. 2.
In another modification of described test, the stock solution of each enzyme (AHA of 1mg/ml, the Stainzyme of 0.5mg/ml) is preparation in buffer A (100mM Hepes, 100mM NaCl, 1mM CaCl, pH7.0).Described enzyme stock solution is further diluted and is mixed in following each reaction mixture on ice with the ratio of 1:415 by buffer A:
1) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted Stainzyme of 0.3ml
2) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted AHA of 0.3ml
3) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2,0.3ml buffer A (negative control)
4) 2.25ml amylase detection reagent 1,0.45ml detection reagent 2, the diluted Stainzyme of 0.15ml, the diluted AHA of 0.15ml
The aliquots containig of 100 μ l is transferred to immediately to 0.2ml thin-walled 96-hole PCR plate (every kind of reaction mixture 2 permutation holes provide the reading of two repetitions for the temperature of each evaluation) and can in the PCR instrument (Techne TC-500) of operating temperature gradient, so cultivating:
Described instrument is set and makes to move the thermograde between 20 ℃ and 50 ℃.By the sample being distributed in the PCR plate of 96-hole, hatching is just in time 30 minutes under these conditions, now PCR plate is cooled to rapidly to 4 ℃.During this cooling step, the 1M tris.base of 50 μ l (without what cushion) is joined to each hole so that reaction stops (preventing from further discharging nitrophenols reaction product).After fully mixing, each reaction mixture of 100 μ l is transferred in clean flat-bottom microtiter plates and use Fluostar Optima microplate reader to evaluate the absorbancy at 405nm place.Blank value under each probe temperature is deducted from the result obtaining containing enzyme mixture.The results are shown in Fig. 3.
The activity data of table 1a together with 1b:AHA, Stainzyme and two kinds of enzymes, wherein take the stock solution of each enzyme the dilution proportion of 1:125 for (data value is for being used the Fluostar Optima microplate reader that is set to 405nm place at the absorbance reading with the acquisition after the thermograde between 20 ℃ and 50 ℃ is hatched 30 minutes of test substrate) in test.With diagrammatic form, be shown in Fig. 5.
Table 1a temperature 22.533.8 (℃)
Table 1b temperature 35.7-47.5 (℃)
Table 2a, 2b:AHA, Stainzyme and two kinds of enzymes activity data together, wherein take the stock solution of each enzyme the dilution proportion of 1:250 for (data value is for being used the Fluostar Optima microplate reader that is set to 405nm place at the absorbance reading with the acquisition after the thermograde between 20 ℃ and 50 ℃ is hatched 30 minutes of test substrate) in test.With diagrammatic form, be shown in Fig. 2.
Table 2a temperature 22.5-33.8 (℃)
Table 2b temperature 35.7-47.5 (℃)
Table 3:AHA, Stainzyme and two kinds of enzymes activity data together, wherein take the stock solution of each enzyme the dilution proportion of 1:417 for (data value is for being used the Fluostar Optima microplate reader that is set to 405nm place at the absorbance reading with the acquisition after the thermograde between 20 ℃ and 50 ℃ is hatched 30 minutes of test substrate) in test.With diagrammatic form, be shown in Fig. 3.
Table 3a temperature 22.5-33.8 (℃)
Table 3b temperature 35.7-47.5 (℃)
The concentration of table in 1a, 1b is: AHA separately=0.8mg/L, Stainzyme separately=0.4mg/L, two kinds of enzymes together=0.4mg/L AHA and 0.2mg/L Stainzyme (gross protein=0.6mg/L)
The concentration of table in 2a, 2b is: AHA separately=0.2mg/L, Stainzyme separately=0.1mg/L, two kinds of enzymes together=0.2mg/L AHA and 0.1mg/L Stainzyme (gross protein=0.3mg/L)
The concentration of table in 3a, 3b is: AHA separately=0.24mg/L, Stainzyme separately=0.12mg/L, two kinds of enzymes together=0.12mg/L AHA and 0.06mg/L Stainzyme (gross protein=0.18mg/L)
Result in table 1a, 1b & 3a, 3b also illustrates to use together two kinds of enzymes to provide the active more balance in wide temperature range than single enzyme contrast lower concentration is low.
The result of table in 2a, 2b also illustrate with single enzyme contrast use together with the same concentrations of being used two kinds of enzymes to provide the high reactivity in temperature range.
Example explanation is had a liking for combination cold and that have a liking for warm α-amylase by uses and from fabric, is removed the method for the spot based on starch
By 96-hole microtiter plate (by CFT, Vlaardingen, NL supply) the micro-sample of fabric that the 4mmC-S-27 yam starch in hole stains is used the 100mM HEPES damping fluid of pH7 to add 100mM sodium-chlor and 5 minutes (200 every holes of μ l of 1mM calcium chloride pre-wash, 1000rpm on orbital shaker, and at the temperature of carrying out in decontamination test).Discard pre-wash solution.
Use the 100mM HEPES damping fluid of pH7 to add that 100mM sodium-chlor and 1mM calcium chloride are diluted to suitable concentration (as indicated) AHA and Stainzyme α-amylase.
The diluted enzyme of 200 μ l is joined in triplicate sample.The microtiter plate that comprises sample and enzyme solution is hatched 1 hour at 10 ℃, 20 ℃ or 60 ℃, with 1000rpm, shake.
After hatching, will from micro titer plate well, shift out and by treated samples with water rinsing, change 5 water (hatch 5 minutes at every turn, in the identical temperature of the temperature adopting with washing step, shake with 1000rpm) containing enzyme solution.Then make at room temperature dried overnight of treated sample.Once dry, the removal of at 410nm place, the micro-sample analysis of fabric being measured to spot with flat reflective spectrophotometer.Result is with SRI unit representation, and it uses the Δ alleviation value producing to produce.The SRI value obtaining after the AHA that the micro-sample of C-S-27 fabric is used alone or in combination in employing and Stainzyme decontamination is shown in Table 8.
In table institute's column data clearly example illustrated that Stainzyme provides most cleaning benefit at high temperature.At low temperature, Stainzyme performance reduces and AHA has improved decontamination situation.
Table 4 example shows AHA and the data of Stainzyme to the decontamination feelings of the fabric of C-S-27 yam starch contamination alone or in combination.Wash temperature is 10 ℃, 20 ℃ and 60 ℃ (being respectively top, centre and bottom group).Data are with the expression of SRI, and repetition values provides together with standard deviation (1SD) with arithmetical av.
The limiting examples of below describing laundry enzymatic fabric treatment composition, wherein following examples enzyme is combined as:
a. lipase combination
Have a liking for cold fat enzyme: from Pseudoalteromonas W27.
Have a liking for warm lipase: Lipex100T (Novozymes A/A)
Thermophilic lipase: from bacstearothermophilus (Bacillus thermocatenlatus) BTL2
b. proteinase combination
Have a liking for cryoproteins enzyme: from flavobacterium balustinum P104
Have a liking for warm proteolytic enzyme: Savinase
tM24.0GTT (12.0 or 24.0T) Novozymes
Thermophilic protease: from having a liking for high temperature Bacillus strain HS08
c. amylase combination
Have a liking for cold amylase: from the extra large Pseudoalteromonas bacterial strain TAC125 of trip and/or swim the α-amylase of extra large Pseudoalteromonas bacterial strain TAB23 (as above)
Have a liking for warm amylase: Stainzyme
tM2.0T (Novozymes)
Have a liking for cold amylase: from the α-amylase of bacstearothermophilus Donk BS-1
d. lyase combination
Have a liking for cold pectin lyase: from the extra large Pseudoalteromonas ANT/505 of trip
Have a liking for warm pectin lyase: Bioprep
tMnovozymes
Thermophilic pectin lyase: from Italian thermophilic anaerobic Bacillaceae Nov.AB9.
e. the combination mixing
Have a liking for cold fat enzyme: from Pseudoalteromonas W27, and
Have a liking for warm proteolytic enzyme: 24.0GTT (12.0 or 24.0T) Novozymes, and/or
Thermophilic amylase: from the α-amylase of bacstearothermophilus Donk BS-1
The example of the short fabric treatment composition of liquid enzymes that comprises above enzyme combination:
Except as otherwise noted, all proportions all provides with the weight percent of any total composition weight.
Certainly, be to be understood that the present invention is not intended to be limited to the details of above-mentioned embodiment, they are just described as an example.
Claims (9)
1. an enzymatic fabric treatment composition, it comprises following combination:
I. one or more have a liking for cold enzyme, and
Ii. one or more have a liking for warm enzyme and/or one or more Zimadzhunt L 340s.
2. according to the enzymatic fabric treatment composition of any one in aforementioned claim, wherein saidly have a liking for cold enzyme, have a liking for warm enzyme and preferably Zimadzhunt L 340 all comprise the enzyme of common classification.
3. according to the enzymatic fabric treatment composition of claim 2, wherein said common classification is proteolytic enzyme or lipase or glycosyl hydrolase or lyase.
4. according to the enzymatic fabric treatment composition of any one in aforementioned claim, wherein said one or more are had a liking for cold enzyme and are comprised esterase.
5. according to the enzymatic fabric treatment composition of claim 4, wherein said one or more are had a liking for cold enzyme and are comprised lipase.
6. use the method for processing fabric according to the enzymatic fabric treatment composition of any one in aforementioned claim, wherein the temperature of washings changes in whole single cycles of washing process between low temperature and middle temperature.
7. according to the method for claim 6, wherein said temperature changes in whole single cycles of washing process between low temperature, middle gentle high temperature.
8. according to the method for the processing fabric of claim 6 or 7, wherein said method comprises hand washing processing and/or processes with washing machine.
9. according to the method for the processing fabric of any one in claim 4-8, wherein the temperature of washings is not controlled by user at least a portion.
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| EP11178002 | 2011-08-18 | ||
| EP11178002.9 | 2011-08-18 | ||
| PCT/EP2012/066050 WO2013024143A1 (en) | 2011-08-18 | 2012-08-16 | Enzyme system |
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| EP (1) | EP2744882A1 (en) |
| CN (1) | CN103748205A (en) |
| AR (1) | AR087586A1 (en) |
| CL (1) | CL2014000379A1 (en) |
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| CN107922889A (en) * | 2015-08-28 | 2018-04-17 | 荷兰联合利华有限公司 | Improved cleaning compositions |
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| CN112322547B (en) * | 2020-11-23 | 2021-10-08 | 江苏海洋大学 | Pseudoalteromonas from sea HL9 and method for producing phospholipase B by using same |
| WO2024194190A1 (en) * | 2023-03-17 | 2024-09-26 | Unilever Ip Holdings B.V. | Composition |
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- 2012-08-16 WO PCT/EP2012/066050 patent/WO2013024143A1/en active Application Filing
- 2012-08-16 EP EP12751483.4A patent/EP2744882A1/en not_active Withdrawn
- 2012-08-16 CN CN201280040074.7A patent/CN103748205A/en active Pending
- 2012-08-17 AR ARP120103032A patent/AR087586A1/en unknown
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- 2014-02-14 CL CL2014000379A patent/CL2014000379A1/en unknown
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| WO1997024428A1 (en) * | 1995-12-29 | 1997-07-10 | The Procter & Gamble Company | Detergent compositions comprising psychrophilic/psychrotrophic enzymes |
| US5769900A (en) * | 1996-01-29 | 1998-06-23 | Bayer Aktiengesellschaft | Enzyme mixtures and processes for desizing textiles sized with starch |
| CN1225120A (en) * | 1996-05-15 | 1999-08-04 | 普罗格特-甘布尔公司 | Detergent compositions comprising improved amylases, cellulase and cationic surfactant |
| WO2002061026A1 (en) * | 2001-02-01 | 2002-08-08 | Ecolab Inc. | Stable solid enzyme compositions and methods employing them |
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| EP2744882A1 (en) | 2014-06-25 |
| ZA201400850B (en) | 2015-10-28 |
| WO2013024143A1 (en) | 2013-02-21 |
| AR087586A1 (en) | 2014-04-03 |
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