Catalytic activity of Teflon particle-immobilized protease in aqueous solution

被引：7

作者：

Afrin, R ^{[1
]}

Haruyama, T ^{[1
]}

Yanagida, Y ^{[1
]}

Kobatake, E ^{[1
]}

Aizawa, M ^{[1
]}

机构：

[1] Tokyo Inst Technol, Grad Sch Biosci & Biotechnol, Dept Biol Informat, Midori Ku, Yokohama, Kanagawa 2268501, Japan

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2000年 / 9卷 / 4-6期

关键词：

Teflon; protease; immobilization; peptide synthesis;

D O I：

10.1016/S1381-1177(99)00104-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

alpha-Chymotrypsin (Chy) was entrapped in polytetrafluoroethylene (PTFE) particles. The entrapped enzyme showed twofold catalytic activity for amino acid ester hydrolysis in aqueous solution than free enzyme. The Chy/PTFE particles also catalyzed the peptide synthesis in aqueous solution with a yield of 14%. Both the synthetic and the hydrolytic activities of the entrapped enzyme were enhanced as compared with the free enzyme. The PTFE matrix should provide the enzyme molecules by creating a hydrophobic environment which results in enhanced peptide synthesis in aqueous solution. (C) 2000 Elsevier Science B.V. All rights reserved.

引用

页码：259 / 267

页数：9

共 19 条

[1]

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[2]

Bergmann M, 1938, J BIOL CHEM, V124, P321

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