Stabilization of Nocardia EH1 epoxide hydrolase by immobilization

被引：23

作者：

Kroutil, W ^{[1
]}

Orru, RVA ^{[1
]}

Faber, K ^{[1
]}

机构：

[1] Graz Tech Univ, Inst Organ Chem, A-8010 Graz, Austria

来源：

BIOTECHNOLOGY LETTERS | 1998年 / 20卷 / 04期

关键词：

D O I：

10.1023/A:1005379314104

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

A partially purified epoxide hydrolase from Nocardia EH1 was stabilized by immobilization through ionic binding onto DEAE-cellulose. The biocatalyst showed more than twice the activity (225 %) of that of the free enzyme albeit at a marginal reduction in enantioselectivity. The addition of the nonionic detergent Triton X-100 during the immobilization further enhanced the stability as indicated by a dramatic shift in the temperature optimum from 35 to 45 degrees C. The stabilized immobilized biocatalyst could be successfully employed in repeated batch reactions (residual activity of 55 % after five cycles), which was not the case for whole cell reactions (residual activity less than or equal to 10%).

引用

页码：373 / 377

页数：5

共 15 条

[1] ANHYDRIDES AS ACYLATING AGENTS IN LIPASE-CATALYZED STEREOSELECTIVE ESTERIFICATION OF RACEMIC ALCOHOLS [J].