Purification and Properties of a Thermostable Esterase of<i>Bacillus stearothermophilus</i>Produced by Recombinant<i>Bacillus brevis</i>
書誌事項
- タイトル別名
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- Purification and Properties of a Thermostable Esterase of Bacillus stearothermophilus Produced by Recombinant Bacillus brevis.
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説明
A thermostable carboxyl esterase of Bacillus stearothermophilus excreted by recombinant B. brevis was purified to homogeneity using column chromatographies on DEAE Bio-Gel A, Sephacryl S-200HR, and Mono Q. The purified enzyme had a molecular weight of 29, 000. The optimum pH at 37°C was 7.5. The esterase had higher activity toward triglycerides with short-chain fatty acids than with long-chain ones. The activity of esterase was completely or significantly inhibited by diisopropyl fluorophosphate, phenylmethylsulfonyl fluoride, iodoacetamide, and p-chloromercuribenzoic acid, while it was slightly stimulated in the presence of 2-mercaptoethanol. This observation suggests that that the enzyme is a serine enzyme having a sulfhydryl group for expressing the enzyme activity. The activation energy for inactivation of the enzyme was estimated to be 131 kcal·mol-1. The kinetic parameters of this enzyme with p-nitrophenyl butyrate were measured : Km was 0.132 mM, and Vmax was 4.8 μmol·(mg protein)-1·min<-1>.
収録刊行物
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- Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ
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Ｂｉｏｓｃｉｅｎｃｅ， Ｂｉｏｔｅｃｈｎｏｌｏｇｙ， ａｎｄ Ｂｉｏｃｈｅｍｉｓｔｒｙ 56 (2), 238-241, 1992
公益社団法人 日本農芸化学会
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詳細情報 詳細情報について
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- CRID
- 1390001206472118784
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- NII論文ID
- 110002680496
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- NII書誌ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- 本文言語コード
- en
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- データソース種別
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- JaLC
- Crossref
- CiNii Articles
- OpenAIRE
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- 抄録ライセンスフラグ
- 使用不可
