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Titolo:
PURIFICATION AND SOME PROPERTIES OF CARBOXYLESTERASE FROM ARTHROBACTER-GLOBIFORMIS - STEREOSELECTIVE HYDROLYSIS OF ETHYL CHRYSANTHEMATE
Autore:
NISHIZAWA M; GOMI H; KISHIMOTO F;
Indirizzi:
SUMITOMO CHEM CO LTD,TAKARAZUKA RES CTR,BIOTECHNOL LAB,4-2-1 TAKATSUKASA TAKARAZUKA HYOGO 665 JAPAN
Titolo Testata:
Bioscience, biotechnology, and biochemistry
fascicolo: 4, volume: 57, anno: 1993,
pagine: 594 - 598
SICI:
0916-8451(1993)57:4<594:PASPOC>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
BACILLUS-SUBTILIS; ESTERASES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
25
Recensione:
Indirizzi per estratti:
Citazione:
M. Nishizawa et al., "PURIFICATION AND SOME PROPERTIES OF CARBOXYLESTERASE FROM ARTHROBACTER-GLOBIFORMIS - STEREOSELECTIVE HYDROLYSIS OF ETHYL CHRYSANTHEMATE", Bioscience, biotechnology, and biochemistry, 57(4), 1993, pp. 594-598

Abstract

An esterase with excellent stereoselectivity for (+)-trans-ethyl chrysanthemate was purified to homogeneity from Arthrobacter globiformis SC-6-98-28. The purified enzyme hydrolyzed a mixture of ethyl chrysanthemate isomers stereoselectively to produce (+)-trans-acid with 100% stereoisomeric purity. The apparent molecular weight of the purified enzyme was 43,000 on SDS-polyacrylamide gel electrophoresis, and 94,000 on gel filtration chromatography. The optimum conditions for the ester hydrolysis were pH 10.0 at 45-degrees-C. The purified esterase hydrolyzed short-chain fatty acid esters, but did not have detectable activity on long-chain water-insoluble fatty acid esters. The enzyme activitywas inhibited by diisopropyl fluorophosphate and phenylmethylsulfonylfluoride.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 05:36:15