NO843661L - L-aminosyre-oksydase fra gjaer av slekten cryptococcus, dens fremstilling og anvendelse - Google Patents
L-aminosyre-oksydase fra gjaer av slekten cryptococcus, dens fremstilling og anvendelseInfo
- Publication number
- NO843661L NO843661L NO843661A NO843661A NO843661L NO 843661 L NO843661 L NO 843661L NO 843661 A NO843661 A NO 843661A NO 843661 A NO843661 A NO 843661A NO 843661 L NO843661 L NO 843661L
- Authority
- NO
- Norway
- Prior art keywords
- amino acid
- generation
- cryptococcus
- production
- laurentii
- Prior art date
Links
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Classifications
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- C—CHEMISTRY; METALLURGY
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- C—CHEMISTRY; METALLURGY
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Abstract
Gjær av slekten Cryptococcus, fortrinnsvis. av arten C. laurentii, danner i nærvær av aminosyrer en L-aminosyre-oksydase, som stereospesifikt omdanner L-aminosyrer og deres derivater i de tilsvarende a-ketosyrene. For denne omdannelse som også kan tjene til racematadskillelse, anvendes fortrinnsvis de fikserte celler.
Description
Oppfinnelsen vedrører en ny L-aminosyre-oksydase med bredt substratspektrum, dens utvinnelse ved fermentering av gjær av slekten Cryptococcus og dens anvendelse til fremstilling av a-ketosyrer, deres estere og etere fra de tilsvarende L-a-aminosyrer resp. deres derivater. L-aminosyre-oksydase, i det følgende LAO, er for gjær av slekten Cryptococcus et induserbart enzym. For dens fremstilling fermenterer man derfor gjæren under tilsetning av en aminosyre eller et aminosyre frigjørende stoff som induk-tor. Foretrukkede utforminger av oppfinnelsen forklares nærmere i det følgende.
Foretrukket fra slekten Cryptococcus er arten C. laurentii, eksempelvis stammen Cryptococcus laurentii var. magnus CBS 569 samt arten C. albidus..
Spesielt foretrukket er stammen C. laurentii DSM 2762. Utgangsmaterial for denne stamme var en jordprøve fra Bobodiovlassio (Øvre Volta), som ble inkubert over flere passasjer i et mineralmedium med D-glutaminsyre som eneste nitrogenkilde ved 28°C for resp. 2-3 dager. Disse væske-kulturer ble utplattert på medier som inneholdt D-a-aminoadipinsyre-etylamid som eneste N-kilde. Etter ytterligere overpodninger ble det bl.a. isolert stammen DSM 2762 som renkultur.
Ved denne stammen dreier det seg om en encellet oval gjær
som hverken danner mycel eller pseudomycelin. Formeringen fullfører seg ved mangsidig knoppskyting, et nærvær av Asko- resp. Ballistosporer kunne ikke påvises. De konvekse, hvitaktige kolonier er rue og har en glatt kant. En pig-mentdannelse i form av karotinoider finner ikke sted. Påvisning av gjærstivelse lykkes med jod-jodkålium, nemlig
så vel i koloniene som også i væskekulturene. Fysiolog-
iske undersøkelser viste at glukose, sakkarose, maltose, raffinose, galaktose, laktose, stivelse, ramnose, melibiose,
dekstrin og inosit assimileres som karbonkilde, en forgjæring av sukkeret finner ikke sted. En utnyttelse av ammoniumsulfat, a-aminoadipinsyre, glutaminsyre, alanin, leucin, serin, trypto-fan, tyrosin og fenylalanin som nitrogenkilde kunne påvises.
En vekst med natriumnitrat ble derimot ikke iakttatt.
Det ble funnet at LAO dannes parallelt i veksten og dens høyeste aktivitet oppnås mot slutten av den logaritmiske fase. Foretrukne induktorer er D-aminosyrer, spesielt D-Leu, D-ct-aminoadipinsyre (DaAAA) samt D-Ala. En oversikt over funnede LAO-aktiviteter viser tabell 1: Foretrukne C-kilder er oppløselig stivelse og spesielt laktose og sakkarose.
I motsetning til de kjente mikrobielle L-aminosyre-oksydaser har LAO ifølge oppfinnelsen et bredt substratspektrum: Ved siden av de fleste naturlige aminosyrer omdannes også andre aminosyrer som L-a-aminoadipinsyre og L-cefalosporin C til de tilsvarende a-ketosyrer. Dertil omsettes imidlertid også derivater av aminosyrene, nemlig deres estere, spesielt lavere alkylester og benzylester, samt etere og nemlig så vel etere av alkoholgruppen av serinen som også den fenoliske hydroksygruppe av tryrosin og tioeter av-cystein. Også herved er de lavere alkyl- og benzyletere resp. -tioetere foretrukket. Den naturlige tioeter L-metionin omsettes likeledes.
Alle omsetninger er strengt stereospesifikke: Det omdannes L-formene i de tilsvarende ketosyrer resp. ketosyrederivater. Ifølge oppfinnelsen kan således også racemater oppdeles,
idet L-formen omformes til ketoderivat, mens D-formen for-blir uendret.
Omsetningen av L-aminosyrene foregår fordelaktig i et pH-område på 6,5-8,5, fortrinnsvis 7-8-, spesielt 7,5. Egnede puffere er derfor kaliumfosfat- og -ris-HCl-puffer.
Fordelaktige omsetningstemperaturer ligger ved ca. 30-60, fortrinnsvis 40-55, spesielt 50°C.
LAO har for L-a-AAA en Km-verdi på 0,25 mM og et Vmax.
på 2-mM.
LAO ifølge oppfinnelsen utmerker seg ved en høy lagrings-stabilitet. Den.er anvendbar ved 4°C flere dager og ved
-18°C flere måneder uten aktivitetsfall.
LAO ifølge oppfinnelsen er lokalisert på den ytre cyto plasma-membran. Enzymaktiviteten er derfor i ikke-permeabili-sert, intakte celler likeså høy som i med cetyl-trimetyl-ammoniumbromid-behandlede celler. Innfrysing og opptining av cellene bevirker en aktivitetsøkning rundt 30-40%.
LAO ifølge oppfinnelsen kan anvendes som konsentrat fra cytoplasma-membran. Spesielt fordelaktig er imidlertid anvend-elsen i form av fikserte celler. Da - som nevnt ovenfor - enzymet er lokalisert på den ytre cytoplasma-membran, er det ikke nødvendig ved fikseringen av cellene å overholde ikke-toksiske betingelser.
Ved siden av de kjente fordeler for enzymfiksering -
høyere stabilitet og forbedret håndtering - bortfaller ved innleiring av de hele celler, isoleringen og rensingen av enzymet.
Immobiliseringen av enzymet resp. cellene kan foregå på
kjent måte med naturlige eller syntetiske polymere
(Nachr. Chem. Tech. Lab. 29 (1981) 850, tyske Offenlegungs-skrifter 2 252 815, 2 343 633, 2 414 128, 2 420 102 og 2 805 607).
I de følgende eksempler forklares spesielt foretrukne utførelser av oppfinnelsen nærmere:
Eksemp_el_l
Gjæren Cryptococcus albidus holdes på følgende faste næringsbunn:
Mediet fordeles på reagensglass og steriliseres 30 minutter ved 121°C, avkjøles deretter, podes med kulturen og inkuberes 3-4 dager ved 2 5°C. Den voksende kultur oppsvømmes med 10 ml steril koksaltoppløsning og haes i et kulturmedium av følgende sammensetning:
500 ml av dette mediet haes i 2 1-Erlenmeyerkolber og steriliseres 30 minutter ved 121°C.
De med 10 ml inokulum podede kolber inkuberes deretter ved 28°C og 190 Opm på en rotasjonsryster. Etter 72 timer høstes den voksende kultur, vaskes og opptas i en kaliumfosfatpuffer (pH 7,5, 50 mM). LAO-aktiviteten av de intakte celler ble bestemt med L-ct-AAA som substrat i en o-fenylendiamin-peroksydase-avhengig prøve med 1,34/g celler.
Eksemp_el_2
Cryptococcus laurentii DSM 2762 ble ifølge eksempel 1 dyrket
i 500 ml næringsoppløsning og overpodet etter 3 dager i en 12 1-fermenterer med 9 1 av samme medium som imidlertid inneholdt D-leucin i stedet for D-a-AAA, og inkubert ved 28°C, 400 Opm og en luftningsgrad på 400 1 luft pr. time.
Etter 4 dager ble det målt en LAO-aktivitet på 3,5 U/g celler.
Eksemp_el_3
En 6&-ig oppløsning av x^Carrageenan (Marine Colloids, Rockland, Maine, USA) oppløses ved 75°C og avkjøles til
40°C og blandes med en 4%-ig cellesuspensjon av Cryptococcus-celler i fysiologisk koksaltoppløsning i forhold 1:1. Denne suspensjon trykkes gjennom en kanyle inn i et fellebad (10 mM CaCl2, 300 mM KC1), slik at det oppstår kuler. Etter en times etteromrøring vaskes tre ganger med 0,3 M KC1. Carrageenan-kulene oppbevares ved 4°C
i 0,13 M kaliumfosfatpuffer (pH 7,5) som inneholder 0,02% natriumacid. Disse kulers aktivitet utgjør ca.
80 mU/g katalysatorfuktigmasse.
Eksemp_el_4_
10 ml 10 mM L-fenylalanin oppløses i 0,1 M kaliumfosfat-puf f er (pH 8,0), omsettes med 4 g ifølge eksempel 3
fikserte Cryptococcus laurentii DSM 2762-celler under luftbegassing ved 37°C. En tilsetning av 10 \ il teknisk katalase (Boehringer, Mannheim) bevirker ødeleggelse av det dannede hydrogenperoksyd og unngår en påvirkning av produktkvaliteten. Forsvinningen av substratet og dannelsen av produktet kan følges ved tynnsjiktkromatografi. Påvisning av produktet kan foregå ved besprøyting av tynnsjiktkromatogrammet med 2,4-dintrofenylhydrazin. Likeledes kan dannelsen av ammoniumioner følges med nitroprussid-metoden.
Etter 5 timer er utgangsmaterialet omsatt kvantitativt.
De i de følgnende tabeller 2 og 3 oppførte resultater ble oppnådd ifølge eksempel 4. Substratkonsentrasjonen var 4 mM, hvis intet er angitt.
Claims (10)
1. L-aminosyre-oksydase fra gjær av slekten Cryptococcus.
2. L-aminosyre-oksydase fra gjær av arten C. laurentii.
3. L-aminosyre-oksydase fra Ci laurentii DSM 2762.
4. Fremgangsmåte til fremstilling av L-aminosyre-oksydase ifølge krav 1-3, karakterisert ved at de nevnte gjærtyper fermenteres under tilsetning av en aminosyre eller et aminosyrefrigjørende stoff.
5. Fremgangsmåte ifølge krav 4, karakterisert ved at det anvendes en D-aminosyre.
6. Fremgangsmåte ifølge krav 5, karakterisert ved at det anvendes D-Leu. D-Ala. D-a-aminoadipinsyre eller D-a-aminoadipinsyre-6-semietylamid.
7. Fremgangsmåte ifølge et eller flere av kravene 4-6, karakterisert ved at det som karbonkilde tjener laktose eller sakkarose.
8. Anvendelse av L-aminosyre-oksydase ifølge krav 1-3 resp. de ifølge krav 4-7 oppnåelige produkter til fremstilling av ct-ketosyrer og deres estere og etere fra de tilsvarende L-a-aminosyrer resp. -derivater.
9. Anvendelse ifølge krav 8, idet L-aminosyre-oksydasen anvendes som konsentrat av cytoplasma-membranen eller i form av fikserte celler.
10. Cryptococcus laurentii DSM 2762.
Applications Claiming Priority (1)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
DE19833333453 DE3333453A1 (de) | 1983-09-16 | 1983-09-16 | L-aminosaeure-oxidase aus hefen der gattung cryptococcus, ihre herstellung und verwendung |
Publications (1)
Publication Number | Publication Date |
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NO843661L true NO843661L (no) | 1985-03-18 |
Family
ID=6209234
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
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NO843661A NO843661L (no) | 1983-09-16 | 1984-09-14 | L-aminosyre-oksydase fra gjaer av slekten cryptococcus, dens fremstilling og anvendelse |
Country Status (18)
Country | Link |
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US (1) | US4783404A (no) |
EP (1) | EP0138040B1 (no) |
JP (2) | JPS6087786A (no) |
AT (1) | ATE57957T1 (no) |
AU (1) | AU3306984A (no) |
BR (1) | BR8404594A (no) |
CA (1) | CA1232560A (no) |
DD (1) | DD222629A5 (no) |
DE (2) | DE3333453A1 (no) |
DK (1) | DK440984A (no) |
ES (2) | ES8506083A1 (no) |
FI (1) | FI843592L (no) |
GR (1) | GR80367B (no) |
HU (1) | HUT36176A (no) |
IL (1) | IL72944A0 (no) |
NO (1) | NO843661L (no) |
PT (1) | PT79204B (no) |
ZA (1) | ZA847260B (no) |
Families Citing this family (4)
Publication number | Priority date | Publication date | Assignee | Title |
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DE3447023A1 (de) * | 1984-12-22 | 1986-06-26 | Hoechst Ag, 6230 Frankfurt | Neue d-aminosaeure-transaminase und ihre verwendung |
US5422255A (en) * | 1987-02-13 | 1995-06-06 | Toray Industries, Inc. | Method for producing D-alanine |
FR2614038B1 (fr) * | 1987-04-17 | 1989-08-04 | Centre Nat Rech Scient | Procede electroenzymatique de production de composes de purete enantiomerique controlee |
FR2918876B1 (fr) * | 2007-07-16 | 2012-10-05 | Oreal | Utilisation de lumiere verte pour activer la l-amino acide oxydase |
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JPS5617073B2 (no) * | 1971-10-28 | 1981-04-20 | ||
JPS5247038B2 (no) * | 1973-03-24 | 1977-11-29 | ||
JPS5247036B2 (no) * | 1973-04-25 | 1977-11-29 | ||
US4070348A (en) * | 1973-07-25 | 1978-01-24 | Rohm Gmbh | Water-swellable, bead copolymer |
GB2015532B (en) * | 1978-02-27 | 1982-06-16 | Yamasa Shoyu Kk | -lysine -oxidase |
JPS56154990A (en) * | 1980-04-30 | 1981-11-30 | Toyo Jozo Co Ltd | Preparation of l-aminoacid oxidase |
JPS58149677A (ja) * | 1982-03-02 | 1983-09-06 | Toyo Jozo Co Ltd | L−グルタミン酸オキシダ−ゼ(h↓2o↓2・ジエネレイテイング)およびその製造法、ならびに分析方法 |
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1983
- 1983-09-16 DE DE19833333453 patent/DE3333453A1/de not_active Withdrawn
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1984
- 1984-09-07 AT AT84110666T patent/ATE57957T1/de not_active IP Right Cessation
- 1984-09-07 EP EP84110666A patent/EP0138040B1/de not_active Expired - Lifetime
- 1984-09-07 DE DE8484110666T patent/DE3483509D1/de not_active Expired - Fee Related
- 1984-09-10 HU HU843414A patent/HUT36176A/hu unknown
- 1984-09-13 CA CA000463070A patent/CA1232560A/en not_active Expired
- 1984-09-13 JP JP59190726A patent/JPS6087786A/ja active Granted
- 1984-09-13 FI FI843592A patent/FI843592L/fi not_active Application Discontinuation
- 1984-09-14 DD DD84267295A patent/DD222629A5/de unknown
- 1984-09-14 AU AU33069/84A patent/AU3306984A/en not_active Abandoned
- 1984-09-14 IL IL72944A patent/IL72944A0/xx unknown
- 1984-09-14 ES ES535920A patent/ES8506083A1/es not_active Expired
- 1984-09-14 GR GR80367A patent/GR80367B/el unknown
- 1984-09-14 ZA ZA847260A patent/ZA847260B/xx unknown
- 1984-09-14 DK DK440984A patent/DK440984A/da not_active Application Discontinuation
- 1984-09-14 PT PT79204A patent/PT79204B/pt unknown
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- 1984-09-14 BR BR8404594A patent/BR8404594A/pt unknown
- 1984-09-14 NO NO843661A patent/NO843661L/no unknown
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1991
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Also Published As
Publication number | Publication date |
---|---|
DE3483509D1 (de) | 1990-12-06 |
US4783404A (en) | 1988-11-08 |
DK440984A (da) | 1985-03-17 |
FI843592A0 (fi) | 1984-09-13 |
GR80367B (en) | 1985-01-15 |
JPH04365473A (ja) | 1992-12-17 |
BR8404594A (pt) | 1985-08-06 |
PT79204A (de) | 1984-10-01 |
JPH0561909B2 (no) | 1993-09-07 |
EP0138040B1 (de) | 1990-10-31 |
ZA847260B (en) | 1985-05-29 |
ES8602113A1 (es) | 1985-11-16 |
EP0138040A2 (de) | 1985-04-24 |
DE3333453A1 (de) | 1985-04-11 |
FI843592L (fi) | 1985-03-17 |
IL72944A0 (en) | 1984-12-31 |
AU3306984A (en) | 1985-03-21 |
CA1232560A (en) | 1988-02-09 |
DK440984D0 (da) | 1984-09-14 |
HUT36176A (en) | 1985-08-28 |
PT79204B (de) | 1986-09-10 |
ES535920A0 (es) | 1985-06-16 |
EP0138040A3 (en) | 1987-08-05 |
ES539085A0 (es) | 1985-11-16 |
JPH0646939B2 (ja) | 1994-06-22 |
ATE57957T1 (de) | 1990-11-15 |
JPS6087786A (ja) | 1985-05-17 |
DD222629A5 (de) | 1985-05-22 |
ES8506083A1 (es) | 1985-06-16 |
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