DK163434B - Enzymatisk detergentadditiv og detergentkomposition indeholdende dette - Google Patents
Enzymatisk detergentadditiv og detergentkomposition indeholdende dette Download PDFInfo
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- DK163434B DK163434B DK144990A DK144990A DK163434B DK 163434 B DK163434 B DK 163434B DK 144990 A DK144990 A DK 144990A DK 144990 A DK144990 A DK 144990A DK 163434 B DK163434 B DK 163434B
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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
- C11D3/38609—Protease or amylase in solid compositions only
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- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/58—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from fungi
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Description
DK 163434B
Nærværende opfindelse angår en proteaseholdigt detergentkomposition og et proteolytisk detergentadditiv til anvendelse heri.
Proteaser anvendes i stor udstrækning som ingredien-5 ser i kommercielle detergenter til forbedring af vaskevirkningen overfor proteinholdig besmudsning. Yderligere oplysninger om dette kan fås i artiklen "How Enzymes got into Detergents", bind 12, Developments in Industrial Microbiology, en publikation af The Society for Industrial Microbio-10 logy, American Institute of Biological Sciences, Washington, D.C. 1971, af Claus Dambmann, Poul Holm, Villy Jensen og Mogens Hilmer Nielsen, og i P.N. Christensen, K. Thomsen og S. Branner: "Development of Detergent Enzymes”, foredrag holdt d. 9. oktober 1986 ved 2nd World Conference on Deter-15 gents, der blev afholdt i Montreaux, Schweiz.
Som angivet i ovennævnte henvisning blev trypsinpræ-parater tidligere anvendt i detergenter, men siden I960'erne er næsten udelukkende alkaliske Bacillus proteaser blevet anvendt til dette formål, og i denne periode er der gjort 20 store anstrengelser for at udvikle mikrobielle proteaser med forbedret vaskevirkning. Detergenter omfattende alkaliske Bacillus proteaser er beskrevet f.eks. i britisk patent nr. 1,243,784 og 1,356,130.
Det er kendt, at hvor ren trypsin er meget specifik, 25 idet den kun hydrolyserer nogle få peptidbindinger i enhvert givet protein, har den almindeligt anvendte Bacillus protease en bred specificitet og hydrolyserer derved mange bindinger i et givet substrat.
I forsøget på at finde forbedrede proteaser har man 30 gået ud fra, at en sådan protease skulle have den bredest mulige substratspecificitet, d.v.s. den skulle være i stand til at hydrolysere så mange bindinger som muligt i proteinbe-smudsningen.
Således skriver M. Minagawa, Osaka Shiritsu Daigaku 35 Seikatsu kagaku-bu Kiyo, bind 23, s. 65-74 (1975) på side 68: "Typen af protease, der er tilpasset til anvendelse ved fjernelse af proteinholdige pletter, må have et bredt spek- 2
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trum af substratspecificitet, der er i stand til uden begrænsning at nedbryde peptidbindingen."
Det har nu overraskende vist sig, at aminosyre-specifikke proteaser udviser udmærket vaskevirkning, og at 5 tilstedeværelsen af uspecifik protease nedsætter vaskeevnen.
Der ses således en stadig bedre vaskevirkning, efterhånden som præparater indeholdende blandinger af proteaser oprenses til kun at indeholde specifikke proteaser. Vi har endog fundet, at specifikke proteaser er bedre end de 10 uspecikke proteaser, der anvendes i detergenter idag.
Kommercielle præparater af den specifikke protease trypsin, som indeholder varierende mængder af andre proteaser, har været anvendt i detergenter, men anvendelsen af i det væsentlige rent trypsin i detergenter er hidtil ukendt.
15 Mikrobielle specifikke proteaser, der i det væsentlige er frie for andre proteaser er også kendte, men anvendelsen af disse i detergenter er hidtil ukendt.
Arbejdshypotesen er, at den forbedrede vaskevirkning skyldes, at store peptidfragmenter fjernes mere effektivt ved 20 vaskebetingelser. Dette kan endvidere forklare, hvorfor kommercielle trypsinpræparater, som indeholder varierende mængder af andre proteaser, aldrig er blevet anset som værende overlegne overfor de uspecifikke Bacillus proteaser, der anvendes i detergenter idag.
25 Det første aspekt af opfindelsen tilvejebringer følgelig et detergentadditiv omfattende protease i form af et ikke-støvende granulat, en stabiliseret væske eller et beskyttet enzym der er kendetegnet ved, at proteasen er en endoprotease med trypsin-lignende specificitet, der hydroly-30 serer proteiner ved at spalte peptidbindinger ved to aminosyrer, og ved at være fri for andre proteaser, der kan påvirke vaskevirkningen.
Et andet aspekt af opfindelsen tilvejebringer en detergentkomposition indeholdende det nævnte detergentad-35 ditiv.
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Aminosvre-specifik protease
De proteaser, der kan anvendes i nærværende opfindelse er de endoproteaser med trypsin-lignende specificitet, der hydrolyserer proteiner ved at spalte peptidbindinger ved 5 to aminosyrer, hvorved man får store peptidfragmenter. En række af sådanne proteaser er kendte, især de af animalsk og mikrobiel oprindelse. Se K. Morihara: "Comparative Specificity of Microbial Proteinases", adv. Enzymol. Relat. Areas Mol. Biol., 41, 179-243 (1974).
10 Proteasen har trypsin-lignende specificitet, og den kan være trypsin eller en mikrobiel, trypsin-lignende protease.
Proteasen kan være af serin-, thiol-, metal- eller aspartattype.
15 Rekombinant DNA teknologi kan anvendes til at til vejebringe en mikroorganisme indeholdende et gen, der koder for og udtrykker og fortrinsvis også udskiller den specifikke protease. Denne organisme kan dyrkes til at danne protease til anvendelse i denne opfindelse.
20 Foretrukne specifikke proteaser til anvendelse i denne opfindelse er aktive i pH-området 6-12, især 7 -10,5, og mest fortrinsvis med pH-optimum i et af disse pH-områder.
Detergentadditivet ifølge opfindelsen er fri for 25 andre proteaser, der kan påvirke vaskevirkningen.
Sædvanligvis tilvejebringes den specifikke protease-aktivitet i det væsentlige af en enkelt specifik protease.
Men en blanding af to (eller flere) specifikke proteaser kan anvendes, forudsat at blandingen udviser den angivne specifi-30 citet, f.eks. en blanding af proteaser med den samme specificitet.
En specielt foretrukken protease er den Fusarium protease, der er beskrevet nedenfor.
Denne protease blev isoleret fra en mikrobiel stam-35 me, som blev deponeret hos Deutsche Sammlung von Mikroorganismen, Gottingen, Vesttyskland den 6. juni 1983 under Budapesttraktatens betingelser med deponeringsnr. DSM 2672.
Den blev klassificeret som tilhørende Fusarium oxvsporum.
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Gæringsvæske indeholdende proteasen kan opnås ved dyrkning af nævnte stamme i henhold til de i teknikken kendte retningslinier, f.eks. som angivet i US patent nr. 3,652,399 (Takeda) eller et eksempel i denne beskrivelse.
5 Kulturvæsken indeholder mindst to proteaser (I og II, hvor II kan anvendes i detergentadditivet ifølge opfindelsen) samt andre proteiner. Separation kan udføres ved affinitetschromatografi på en bacitracin-sepharose-søjle, men det har vist sig, at en søjle med sojabønnetrypsininhibitor-10 sepharose (STI-sepharose) har bedre kapacitet.
Ved anvendelsen af 0,05 M borsyre, pH 6,5 som puffer, bindes protease I og II mens andre proteiner elueres.
Den uønskede protease I kan dernæst elueres med 0,25 M NaCl i den samme puffer, med 0,1 M NaCl eller med 0,05 M borsyre ved 15 pH 4-5 eller derunder. Protease II kan slutteligt elueres med 0,05 M eddikesyre, pH 2,8.
SDS-PAGE og isoelektrisk fokusering (IEF) i tilstedeværelsen af markør-proteiner er egnede metoder til bestemmelse af henholdsvis molekylvægt (MW) og isoelektrisk 20 punkt (pi). I henhold til disse metoder har protease MW på ca. 27 kD og pi på ca. 9-10. Protease I (beskrevet ovenfor) har MW på ca. 30 kD og pi 9-10, og kendt Fusarium protease, der er fremstillet ved dyrkning af stamme S-19-5 i henhold til US patent nr. 3,652,399, indeholder en enkelt komponent· 25 med MW på ca. 32 kD ved ovenfor angivne metode.
pH- og temperatur-afhængigheden af aktiviteten af protease II fremgår af fig. 2 og 3, hvor protease I også er vist til sammenligning. Kurverne er baseret på CPU-metoden (beskrevet nedenfor), bortset fra at temperatur og pH er 30 varieret. Som vist i figurerne har protease II, der kan anvendes i detergentadditivet ifølge opfindelsen, temperaturoptimum omkring 45'C (30 minutters reaktion ved pH 9,5), og pH-optimum ved 8,5 - ll,0 (30 minutters reaktion ved 25'C) med næsten konstant aktivitet i dette pH-område.
35 pH- og temperaturkurverne blev endvidere målt i opløsninger af et flydende detergent med builder samt af et pulverdetergent med perborat og TAED (blegeaktivator) . Disse 5
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kurver var næsten identiske med dem uden detergent, som er vist i fig. 2 og 3.
Proteasen hæmmes af inhibitorer, der er karakter- ·»- istiske for serin-proteaser, såsom PMSF.
5 For at illustrere specificiteten blev oxideret okseinsulin-B-kæde hydrolyseret med protease (1,38 CPU/1, 15 minutter), og hydrolyseprodukterne blev analyseret ved omvendt-fase væskechromatografi (5 μη silica overtrukket med C-18 kulbrinte, gradient eluering). Fig. 4 viser resultatet med 10 protease II, der kan anvendes i detergentadditivet ifølge opfindelsen, fig. 5 med komponent I fra DSM 2672, og fig. 6-7 med kendte Fusarium proteaser i henhold til US patent nr. 3,652,399 (henholdsvis Fusarium sp. S-19-5 og I\_ oxvsporum f. batatas IFO 4468).
15 Chromatogrammerne viser en slående forskel. Chroma- togrammet for protease II, der kan anvendes i detergentadditivet ifølge opfindelsen, har kun to store toppe, og synes at ligne chromatogrammet for trypsin, som er kendt for at hydrolysere to peptidbindinger (Arg(22)-Gly(23) og Lys(29)-20 Ala(30)). I modsætning hertil hydrolyserer de andre Fusarium proteaser talrige bindinger i dette substrat, hvorved der opnås mere end 10 toppe af samme størrelsesorden.
Substratspecificiteten illustreres endvidere ved virkningen på to syntetiske substrater. Protease II, der kan 25 anvendes i detergentadditivet ifølge opfindelsen, hydrolyserer Bz-Arg-pNA men ikke Suc-AAPF-pNA. Protease I derimod hydrolyserer kun sidstnævnte.
Monospecifikke antisera mod oprenset protease kan rejses f.eks. ved at immunisere kaniner i henhold til for-30 skrifterne i "A Manual of Quantitative Immunoelectrophoresis", Blackwell Scientific Publications, 1973, kapitel 23 af N. Axelsen et al. Oprensede immunoglobuliner kan opnås fra antiseraene, f.eks. ved fældning med salt ((NH4)2S04) efterfulgt af dialyse og ionbytterchromatografi, f.eks. på 35 DEAE-Sephadex.
Immunokemisk karakterisering af proteiner kan udføres enten ved Ouchterlony's dobbelt diffusionsanalyse (O. Ouchterlony i: "Handbook of Experimental Immunology (D.M.
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Weir, Ed.)/ Blackwell Scientific Publications, 1967, s. 655-706), ved krydset iiranunoelektrophorese (N. Axelsen et al., supra, kapitel 3 og 4) eller ved raket immunoelektrophorese (N. Axelsen et al., supra, kapitel 2).
5 Protease II, der kan anvendes i detergentadditivet ifølge opfindelsen, viser immunokemisk ikke-identitet med protease I fra DSM 2672 og med den kendte S-19-5 Fusarium protease.
Detergentkompositionerne ifølge opfindelsen omfatter 10 overfladeaktivt stof, som kan. være af den anioniske, non-ioniske, cationiske, amphoteri'ské eller zwitterioniske type, eller en blanding af disse. Typiske eksempler på anioniske overfladeaktive stoffer er lineær alkylbenzensulfonat (LAS), alpha-olefinsulfonat (AOS), alkoholethoxysulfat (AES) og 15 alkalimetalsæber.
Detergentkompositionerne ifølge opfindelsen kan indeholde andre kendte detergentbestanddele, såsom buildere, blegemidler, blegeaktivatorer, antikorrosionsmidler, sek-vestreringsmidler, antiredepositionsmidler, parfume, stabili-20 seringsmidler til enzymer og blegemidler o.s.v.
Detergentkompositionerne ifølge opfindelsen kan formuleres i enhver hensigtsmæssig form, f.eks. som pulvere, væsker o.s.v. Proteasen kan stabiliseres i et flydende detergent ved inkludering af enzymstabiliseringsmidler, f.eks.
25 nedennævnte.
Detergent har sædvanligvis et pH i opløsning på 7 -12, især 8 - 10,5. Specifik protease med aktivitet ved dette pH foretrækkes.
Detergentkompositionen ifølge opfindelsen kan in-30 deholde et eller flere andre detergentenzymer udover protease. Eksempler er lipase, amylase og cellulase. Det er kendt, at når en protease kombineres med et andet enzym i et detergent, er det andet enzym tilbøjeligt til at blive nedbrudt og. deaktiveret af proteasen i detergentopløsningen (se f.eks.
35 europæisk patentskrift nr. 205,208 (Unilever). I denne forbindelse gør den høje substratspecificitet af proteasen, der anvendes i detergentadditivet ifølge opfindelsen, den mere
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7 kompatibel med andre enzymer. De to (eller flere) enzymer kan tilsættes separat eller i form af et kombineret additiv.
Detergentadditivet ifølge opfindelsen er i form af et ikke-støvende granulat, en stabiliseret væske eller et 5 beskyttet enzym.
Ikke-støvende grnaulater kan fremstilles f.eks. i henhold til hollandsk patentskrift nr. 167,1993 (Novo Nordisk), US patent nr. 4,106,991 (Novo Nordisk) eller US patent nr 4,661,452 (Novo Nordisk) og kan om ønsket overtræk-10 kes i henhold til de i teknikken kendte retningslinier.
Et flydende proteasepræparat kan stabiliseres, f.eks. ved tilsætning af propylenglycol, andre polyoler, sukkerarter, sukkeralkohol, mælkesyre, borsyre. Andre stabiliseringsmidler til enzymer er kendte.
15 Beskyttet enzym kan fremstillet i henhold til euro pæisk patentskrift nr. 238,216 (Novo Nordisk, Albright & Wilson).
• Detergentadditivet ifølge opfindelsen kan indeholde en eller flere andre detergentenzymer, f.eks. lipase, cellu-20 lase eller amylase. I de tilfælde, hvor det drejer sig om et granulat kan enzymerne blandes før eller efter granuleringen.
Proteaseaktivitet (CPU)
Proteolytisk aktivitet bestemmes med casein som substrat. En casein-proteaseenhed (CPU) defineres som mængden 25 af enzym, der frigør 1 millimol primære aminogrupper (bestemt ved sammenligning med en serinstandard) pr. minut under standardbetingelser, d.v.s. inkubation i 30 minutter ved 25'C og pH 9,5.
En 2% (w/w) opløsning af casein (Hammersten, solgt 30 af Merck A.G., Vesttyskland) fremstilles med "Universal Buffer", som er beskrevet af Britton og Robinson (Journ. Chem.Soc., 1931, s. 1451), indstillet til pH 9,5.
To ml substratopløsning forinkuberes i et vandbad i 10 minutter ved 25*C. 1 ml enzymopløsning indeholdende b g/ml 35 enzympræparat, svarende til ca. 0,2 - 0,3 CPU/ml Britton-Robinson puffer (pH 9,5) tilsættes. Efter 30 minutters inkubation ved 25 ‘ C stoppes reaktionen ved tilsætning af et 8
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stopreagens (5 ral af en opløsning indeholdende trichloro-eddikesyre (17,9 g), natriumacetat (29,9 g) og eddikesyre (19,8 g), der er fyldt op med af ioniseret vand til 500 ml).
En blindprøve fremstilles på samme måde som prøveopløsningen, 5 med den undtagelse, at stopreagenset tilsættes før enzymopløsningen.
Reaktionsblandingerne henstår i 20 minutter i vandbad, hvorefter de filtreres gennem Whatman® 42 papirfiltre.
Primære aminogrupper bestemmes ved deres farveudvik-10 ling med o-phthaldialdehyd (OPA).
Dinatriumtetraboratdecahydrat (7,62 g) og natrium-dodecylsulfat (2,0 g) opløses i 150 ml vand. OPA (160 mg), der er opløst i 4 ml methanol' tilsættes derefter sammen med 400 μΐ beta-mercaptoethanol, hvorefter opløsningen fyldes med 15 vand til 200 ml.
Til OPA-reagenset (3 ml) tilsættes 400 μΐ af ovennævnte filtrater under omrøring. OD-værdien ved 340 nm måles efter ca. 5 minutter.
OPA-testen udføres endvidere med en serinstandard 20 indeholdende 10 mg serin i 100 ml Britton-Robinson puffer (pH 9,5). Pufferen anvendes til blindforsøg.
Proteaseaktiviteten beregnes udfra målingerne af OD-værdien ved hjælp af nedenstående formel.
(0Dt - ODjj x cser x Q
25 CPU/ml enzymopløsning = --
(0Dser " odb) x ^ser x H
CPU/g enzympræparat = CPU/ml: b hvori ODt, ODtø, ODser og ODB er OD-værdien for henholdsvis testopløsningen, blindprøven, serinstandarden og pufferen, 30 Cser koncentrationen af serin i ml/ml i standarden, MWser molekylvægten af serin. Q er fortyndingsfaktoren (i dette tilfælde lig med 8) for enzymopløsningen og tj_ er inkubationstiden i minutter.
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Kort beskrivelse af tegningerne
Fig. 1 viser elueringschromatogrammet for kulturvæsken fra stamme DSM 2672 på en STI-Sepharosesøjle. Detaljer fremgår af eksempel 2.
5 Fig. 2 og 3 viser kurverne for henholdsvis pH-ak- tiviteten og temperaturaktiviteten for de to proteaser fra DSM 2672, nemlig protease II (proteasen, der kan anvendes i detergentadditivet ifølge opfindelsen) og protease I til sammenligning.
10 Fig. 4-7 viser omvendt-fase-chromatogrammer af hydrolyseproduktet af oxideret okseinsulin-B-kæde med Fusa rium proteaser.' Fig. 4 viser hydrolyse med protease II, fig. 5 med protease I fra DSM 2672, fig. 6 med protease fra S-19-5 og fig. 7 med protease fra F\. oxysporum f. batatas 15 (IFO 4468), hvor de to sidstnævnte fremstilles i henhold til US patent nr. 3,652,399.
Fig. 8-13 viser resultatet af vaskeforsøgene fra eksemplerne 3-8.
Fig. 14 viser resultatet af vaskeforsøgene i ek-20 sempel 10.
EKSEMPEL 1 Gæring af F. oxvsporum DSM 2672
En podegæringstank med nedenfor angivne medium blev podet med DSM 2672 og gærede i 30-35 timer under beluftning.
25 Derefter blev det anvendt til at pode en 10 gange større hovedgæringstank med samme medium og gærede i 114 timer under beluftning og med kontinuert tilsætning af yderligere substrater.
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Sammensætning af medium (w/v%):
Sojamel 5,0 glucose 5,0 KH2P04 2,0 5 K2HP04 2,0
CaCl2*2H20 0,02 '
MgS04-7H20 0,02 sojaolie 0,5
Pluronic® (ml/1) 0,033 10 Doseret substrat: 45% w/v glucose
Doseringshastighed: 0,28% volumina/volumina/tirae
Proteaseaktiviteten af væsken var 2,84 AU/1 (AU angiver proteaseaktivitet i Ansori-ériheder, se US patent nr. 3,723,250, spalte 8).
15 Rå protease blev udvundet fra kulturvæsken ved tilsætning af ammoniumsulfat (udsaltning), filtrering, opløsning af filterkagen igen, oprensning ved ionbytter efter- fulgt af bentonit og endelig tørring.
EKSEMPEL 2 20 Separation af oroteaser Rå protease fremkommet som i eksempel 1 (aktivitet 15 CPU/g) blev opløst i puffer (0,0514 borsyre, pH 6,5). Efter affarvning ved adsorption på DEAE-Sephadex var OD-værdien 1,2 ved 280 nm. 15 ml af denne opløsning med et totalt protein-25 indhold på 18 mg (beregnet ud fra OD, 280 nm) blev separeret ved affinitetschromatografi.
Gelen var sojabønnetrypsin inhibitoragarose (STI- , agarose), volumenet af lejet var 10 ml, og søjlediameteren var 2,5 cm. Ovennævnte puffer blev anvendt med en flowhastig-30 hed af 0,5 ml/min, og fraktioner af 4,5 ml hver blev opsamlet. Til hver fraktion blev OD 280 nm målt, så vel som aktivitet overfor Bz-DL-Arg-pNA og Suc-AAPF-pNA. Elueringschroma- 11
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togrammet fremgår af fig. 1. Eluenten, der blev anvendt på hvert stade, angives også i tegningen.
Som vist i fig. 1 blev uadsorberet materiale først elueret med puffer, dernæst blev en proteasetop (benævnt I) 5 elueret ved 0,25H NaCl i puffer. Som vist blev der ikke elueret yderligere materiale ved forøgelse til 0,5M NaCl og anvendelse af 0,1M acetat, pH 4,0. En anden proteasetop (benævnt II) blev elueret ved 0,05M eddikesyre, pH 2,8.
Fordeling af protein: 10 Indsprøjtet 18 mg
Elueret
Ikke adsorberet 7,45 mg (41%)
Komponent I 6,55 mg (36%)
Komponent II 4,03 mg (22%) 15 Total 18 mg
Ca. 64% af proteinet blev tilbage i opløsning efter initial oprensing ved DEAE, hvorfor udvindingen af protein i forhold til proteasekoncentratet var som følger:
Komponent I 23% af protein (62% af protease) 20 Komponent II 14% af protein (38% af protease) EKSEMPEL 3-8
Vaskeforsøq
Nedenstående detergentopløsninger (i g/1) blev anvendt. Numrene I-III repræsenterer pulverdetergenter og nr.
25 IV et flydende detergent med builder.
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I II III
LAS 0,4 0,4 0,4 AE 0,15 0,15 0,15 Sæbe 0,15 0,15 0,15 5 Natriumtripolyphosphat 1,75 - 1,75
Natriumsilicat 0,4 0,4 0,4
Carboxymethylcellulose 0,05 0,05 0,05 EDTA 0,01 0,01 0,01
Natriumsulfat 2,1 2,1 2,1 10 Natriumperborat - - 1,0 TAED - - 0,1
Zeolite A 1,25 ΝΤΑ - 0,5
Natriumcarbonat - 0,5 15 NaOH til pH: 9,5 10,0 9,5
IV
AES 0,23 AE 0,23
Oliesyre 0,075 20 Triethanolamin 0,15
Ethanol 0,03
Propylenglycol 0,15 DTPA 0,008
Dinatriumcitrat, 2H20 0,17 25 CaCl2, 2H20 0,015
NaOH til pH: 8,0 LAS er lineær alkylbenzensulfonat (Nansa 80S, produkt fra Albright & Wilson, UK) , AE er alkoholethoxylat (Berol 065, produkt fra Berol Kemi AB, Sverige) , EDTA er 30 ethylendiamintetra-eddikesyre, TAED er Ν,Ν,Ν,Ν-tetraacetyl- ethylendiamin, NTA er nitrilotri-eddikesyre, AES er alkohol- ethoxysulfat (Dobanol 25-3S, produkt fra Shell Chemicals), DTPA er diethylentriaminpenta-eddikesyre trinatriummonocal-ciumsalt.
13
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Besmudsede spinatlapper blev fremstillet på en Mathis' Vaske- og tørreenhed (Werner Mathis AG, Schweitz) i kontinuert drift, ved hvilken bomuldsstoffet passerer gennem spinatsaft, presses mellem to ruller og dernæst blæsetørres i 5 30*C varm luft (termostateret). Lapperne blev ældet i 3 uger ved 20eC og henstod ved -18°C, til de skulle anvendes.
Lapper med blandet besmudsning blev fremstillet ved at nedsænke bomuld i nedenstående blanding; presning mellem ruller; tørring og ældning i 2 dage i luft ved 20°C.
10 Olivenolie 14,4 vægt-%
Stearinsyre 1,8 -
Monoglycerid 1,8 -
Gelatine 0,9 -
Afioniseret vand 79,3 - 15 Kønrøg 0,2 -
Kaolin 1,4 -
Tusch 0,2 -
Vaskeforsøg blev udført i et Terg-O-Tometer (Jay c. Harris; Detergency Evaluation and Testing, Interscience 20 Publishers Ltd. (1954), s. 60-61) med 7 lapper (7x7 cm) og 700 ml detergentopløsning i hvert bæger. Betingelser var 25’C, 10 minutter, 100 rpm. Efter vask og tørring blev re- flektionsværdien (R) af lapperne målt. Vaskevirkningen udtrykkes som Δ R = R-RQ, hvor RQ er målingen uden enzym.
25 Protease II, der anvendes i detergentadditivet ifølge opfindelsen (fremstillet som i eksempel 2), blev sammenlignet med komponent I (fremstillet som i eksempel 2) og med Savinase® (en alkalisk Bacillus protease, produkt fra Novo Nordisk A/S, Danmark).
30 Resultater angives som R0 og Δ R overfor proteasety- pe og dosering (i CPU/1). Nedenfor anførte resultater fremgår endvidere af figurerne som angivet:
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EKSEMPEL 3 (fig. 8) 14
Detergent I, besmudsning med spinat CPU/1 5 ----—-
Protease 0 0,025 0,05 0,075 0,1
R0 .AR .AR AR AR
10 Opfindelse 8,3 11,2 13,5 15,3
Sammenligning I 42,2 2,6 7,0 10,3 11,5
Savinase® 2,5 5,1 8,3 11,3'' 15 EKSEMPEL 4 (fig. 9)
Detergent II, besmudsning med spinat CPU/1 20 Protease 0 0,025 0,05 0,075 0,1 0,2
R0 AR AR ARARAR
Opfindelse 7,9 10,7 12,8 15,5 20,3 25
Sammenligning I 43,4 3,7 8,6 11,7 12,6 17,6 EKSEMPEL 5 (fig. 10)
Detergent IV, besmudsning med spinat 30 CPU/1
Protease o 0,025 0,05 .0,2
R0 A R Δ R Δ R
35
Opfindelse 3,5 4,0 7,0
Sammenligning I 37,7 1,8 2,8 4,7 EKSEMPEL 6 (fig. 11) 15
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Detergent I. blandet besmudsninq CPU/1 5 ----
Protease 0 0,025 0,05 0,1
R0 ÅR ÅR ÅR
10 Opfindelse 8,2 11,0 12,8
Sammenligning I 21,0 2,3 4,7 8,5 EKSEMPEL 7 (fig. 12)
Detergent III. besmudsninq med spinat 15 CPU/1
Protease 0 0,025 0,05 0,075 0,1
R0 ÅR ÅR. ÅR ÅR
20-------
Opfindelse 6,4 10,2 13,5 13,2
Sammenligning I 40,5 3,6 6,4 8,5 10,9 25
Savinase® 2,2 3,6 9,7 EKSEMPEL 8 (fig. 13)
Detergent II., blandetbesmudsning 30 CPU/1
Protease 0 0,022 0,044 0,066 0,088
Rq ÅR ÅR ÅR ÅR
35
Opfindelse 18,5 20,7 23,1 26,6
Sammenligning I 21,5 5,2 8,8 11,0 13,9 16
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De testede detergentformuleringer ligger i pH området 8-10 med forskellige buildere (phosphat og ikke-phosphat) med og uden perborat og med anionisk og non-ionisk overfladeaktivt middel. Således er et stort antal af typiske 5 formuleringer til detergenter i flydende form eller som pulver omfattet. Ved alle disse betingelser udviste proteasen II en overlegen vaskevirkning på basis af CPU aktivitet.
EKSEMPEL 9
Vaskeforsøq med proteaseblandinoer 10 Detergent nr. Ii eksemplerne 3-8 blev anvendt.
Lapper og vaskebetingelser var som beskrevet i eksempel 3 -8. Proteasen II, komponent I og forskellige blandinger af disse blev tilsat i totale mængder op til 0,10 CPU/1.
15 Mængdeforhold i- CPU/1 mellem proteaserne
Opfindelse : 0 0,01 0,05 0,10
sammenligning I RQ ÅR ÅR AR
20 -*----- 0 : 100 45,1 1,8 7,1 9,7 50 : 50 44,7 1,7 9,1 11,5 25 75 : 25 44,7 2,1 8,8 11,2 90 : 10 45,1 2,0 9,1 11,2 99 : 1 45,1 2,2 9,5 12,2 30 100 : 0 44,7 2,2 11,0 14,3
Det ses, at en forøget renhed af den specifikke protease giver forbedret vaskevirkning.
EKSEMPEL 10 17
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Vaskeforsøg med Asp-N specifik protease
Nedenstående detergentformulering blev anvendt: LAS 0,40 g/1 5 AE 0,15 - Sæbe 0,15 - Ν32^0^ 2,00 *
De samme kemikalier, som beskrevet i eksemplerne 3 -8, blev anvendt.
10 Detergentet blev opløst i 10 mM NH4HC03 fremstillet af 9* GH vand, og pH var indstillet til 8,0.
Besmudsede spinatlapper blev fremstillet analogt med eksemplerne 3-8.
Vaskeforsøg blev udført i 150 ml glasbægere i et 15 termostat-vandbad med magnetisk omrøring med 6 lapper (2,2 x 2,2 cm hver) og 60 ml detergentopløsning i hvert bæger. Betingelser var 35'C, 90 minutter.
Som et andet eksempel på specifikke proteaser sammenlignes den specifikke protease Asp-N endoproteinase, der 20 er et kommercielt produkt fra Boehringer (cat. nr. 1054 589), med den uspecifikke Alcalase· og Subtilisin Novo (der begge er Bacillus proteaser og produkter fra Novo Nordisk A/S, Danmark).
Proteaserne doseres i lige store mængder enzympro-25 tein, 0,6 og 1,2 mg/1.
Efter vask og tørring blev. reflektionsværdien (% R) af lapperne målt i henhold til eksemplerne 3-8.
Resultater angives som Δ R overfor proteasetype og dosering i fig. 14.
30 EKSEMPEL 11
Dette eksempel viser, hvordan adsorption på bomuld af hydrolyseprodukter af hæmoglobin varierer alt efter hvilken type protease, der anvendes til at hydrolysere hæmoglobi- 18
DK 163434 B
net. Det fremgår, at hydrolyseprodukter, der er dannet ved en specifik protease (Trypsin), adsorberes i mindre grad end de hydrolyseprodukter, der opnås med en uspecifik protease (Subtilisin Carlsberg).
5 Fremgangsmåden er som følger:
En 0,05% (w/v) opløsning af hæmoglobin i Britton-Robinson I puffer, pH 9,0 hydrolyseres ved 0,3 CPU/1 af en protease. Efter 30 minutter ved 25eC placeres en bomuldslap (rund, 5 cm i diameter) i reaktionsblandingen, og den koges i 10 10 minutter. Dernæst fjernes lappen, vaskes under rindende vand, opblødes i afioniseret vand' i 30 minutter og vaskes igen under rindende vand. Efter lufttørring måles reflektionsværdien (R) af lapperne ved 460 nm. Graden af adsorption udtrykkes som Δ R = R-R0, hvor RQ er remiss ionen, der er 15 opnået uden enzym, d.v.s med uhydrolyseret hæmoglobin.
Den specifikke protease Trypsin og den uspecifikke protease Subtilisin Carlsberg blev testet både separat og sammen. Resultaterne fremgår af nedenstående tabel:
Total aktivitet 0,3 CPU/1 20 --
% Trypsin % Carlsberg A R
0 ' · 100 . · · -6,8 25 ‘ 100 0 -0,1 90 10 -3,8 30 50 50 -5,0
En større negativ værdi af A R indikerer en mørkere lap, d.v.s. at der adsorberes flere nedbrydningsprodukter .
Resultaterne viser, at den uspecifikke protease har 35 en negativ effekt, d.v.s. frembringer nedbrydningsprodukter, der adsorberes lettere, hvorimod den specifikke protease praktisk taget ikke har en sådan virkning. Det fremgår også, at inkorporeringen af sdlv en lille mængde af den uspecifikke protease frembringer et væsentligt større adsorptionresultat 40 end den rene specifikke protease.
Claims (5)
1. Detergentadditiv omfattende protease i form af et ikke-støvende granulat, en stabiliseret væske eller et beskyttet enzym, kendetegnet ved, at proteasen er en endoprote- 5 ase med trypsin-lignende specificitet, der hydrolyserer proteiner ved at spalte peptidbindinger ved to aminosyrer, og ved at være fri for andre proteaser, der kan påvirke vaskevirkningen.
2. Detergentadditiv ifølge krav 1, hvori proteasen er 10 en animalsk eller mikrobiel protease eller er fremstillet ved dyrkning af en transformeret værtsorganisme indeholdende et gen, der koder for og udtrykker en animalsk eller mikrobiel protease.
3. Detergentadditiv ifølge krav 1, hvori proteasen er 15 trypsin.
4. Detergentadditiv ifølge krav 1 kendetegnet ved, at proteasen a) er en serin-protease b) har evnen til at hydrolysere den oxiderede oksein- 20 sulin-B-kæde, således at et chromatogram kun udviser to hoved-hydrolyseprodukter. c) udviser immunokemisk identitet med den trypsin-lignende protease II, der opnås ved dyrkning af Fusarium so. DSM 2672 25 d) har et isoelektrisk punkt på ca. 9-10 e) har evnen til at hydrolysere Bz-Arg, pNA f) i det væsentlige ikke hydrolyserer Suc-AAPF-pNA g) i det væsentlige har samme aktivitet overfor casein ved pH 9 og pH 11.
5. Detergentkomposition kendetegnet ved, at den in deholder et detergentadditiv ifølge krav 1.
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DK6388 | 1988-01-07 | ||
DK6288A DK6288D0 (da) | 1988-01-07 | 1988-01-07 | Enzymatisk detergent |
DK6388A DK6388D0 (da) | 1988-01-07 | 1988-01-07 | Enzymatisk detergent |
DK6288 | 1988-01-07 | ||
DK8900001 | 1989-01-06 | ||
PCT/DK1989/000001 WO1989006270A1 (en) | 1988-01-07 | 1989-01-06 | Enzymatic detergent |
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DK163434B true DK163434B (da) | 1992-03-02 |
DK163434C DK163434C (da) | 1992-07-20 |
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DK144990A DK163434C (da) | 1988-01-07 | 1990-06-14 | Enzymatisk detergentadditiv og detergentkomposition indeholdende dette |
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JP (2) | JP2624859B2 (da) |
AT (1) | ATE129523T1 (da) |
DE (1) | DE68924654T2 (da) |
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US365399A (en) * | 1887-06-28 | Temperature-alarm | ||
US3655570A (en) * | 1968-02-08 | 1972-04-11 | Takeda Chemical Industries Ltd | Detergent containing alkali protease |
US3652399A (en) * | 1969-04-30 | 1972-03-28 | Takeda Chemical Industries Ltd | Alkali protease |
GB1349650A (en) * | 1970-11-27 | 1974-04-10 | Pegg S & Son Ltd | Textile processing |
US4264738A (en) * | 1979-08-01 | 1981-04-28 | Stepanov Valentin M | Process for purification of proteolytic enzymes |
ATE77648T1 (de) * | 1985-04-15 | 1992-07-15 | Procter & Gamble | Fluessige reinigungsmittel mit einer anionischen oberflaechenaktiven verbindung, einem verstaerker und einem proteolytischen enzym. |
-
1989
- 1989-01-06 DE DE68924654T patent/DE68924654T2/de not_active Expired - Fee Related
- 1989-01-06 JP JP1501510A patent/JP2624859B2/ja not_active Expired - Lifetime
- 1989-01-06 WO PCT/DK1989/000001 patent/WO1989006270A1/en active IP Right Grant
- 1989-01-06 EP EP91113109A patent/EP0471265B1/en not_active Expired - Lifetime
- 1989-01-06 AT AT91113109T patent/ATE129523T1/de not_active IP Right Cessation
- 1989-01-06 EP EP89901710A patent/EP0394352B1/en not_active Expired
-
1990
- 1990-06-14 DK DK144990A patent/DK163434C/da not_active IP Right Cessation
-
1996
- 1996-01-04 JP JP8000074A patent/JP2693141B2/ja not_active Expired - Lifetime
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DK144990A (da) | 1990-06-14 |
EP0471265B1 (en) | 1995-10-25 |
WO1989006270A1 (en) | 1989-07-13 |
JPH08308566A (ja) | 1996-11-26 |
EP0471265A1 (en) | 1992-02-19 |
EP0394352A1 (en) | 1990-10-31 |
EP0394352B1 (en) | 1992-03-11 |
DE68924654T2 (de) | 1996-04-04 |
ATE129523T1 (de) | 1995-11-15 |
JPH03502203A (ja) | 1991-05-23 |
DK163434C (da) | 1992-07-20 |
JP2624859B2 (ja) | 1997-06-25 |
DK144990D0 (da) | 1990-06-14 |
DE68924654D1 (de) | 1995-11-30 |
JP2693141B2 (ja) | 1997-12-24 |
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