Esterase Activities of Brevibacterium sp. R312 and Brevibacterium linens 62
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概要
- 論文の詳細を見る
Esterase activity of Brevibacterium linens 62 and Brevibacterium sp. R312 was detected. Each strain had esterase activities that hydrolyzed p-nitrophenyl acetate and α-naphthyl acetate. Biosynthesis and optimum pH and temperature of the two esterase activities showed that the latter were caused by different esterases. The influence of the culture medium and the growth substrate on biosynthesis of the esterase systems were studied. Hydrolysis of methylthioacetate and phenethyl acetate by cell extracts of the two strains was done. No enzymatic ester synthesis reaction was observed. However, transfer reactions by cell extracts of the two strains were done.
- 社団法人日本農芸化学会の論文
- 1995-08-23
著者
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Lambrechts C
Chaire De Microbiologie Industrielle Et De Genetique Des Micro-organismes Ecole Nationale Superieure
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Lambrechts Christel
Chaire De Genetique Et Microbiologie Ensa-inra
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GALZY Pierre
Chaire de Genetique et Microbiologie, Ecole Nationale Superieure Agronomique
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Galzy Pierre
Chaire De Genetique Et Microbiologie Ecole Nationale Superieure Agronomique
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Galzy Pierre
Chaire De Microbiologie Industrielle Et De Genetique Des Micro-organismes Ecole Nationale Superieure
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GALZY PIERRE
Chaire de Genetique et Microbiologie , ENSA-INRA
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- Esterase Activities of Brevibacterium sp. R312 and Brevibacterium linens 62