Covalent immobilization of penicillin acylase from Streptomyces lavendulae

被引：39

作者：

Torres-Bacete, J ^{[1
]}

Arroyo, M ^{[1
]}

Torres-Guzmán, R ^{[1
]}

de la Mata, I ^{[1
]}

Castillón, MP ^{[1
]}

Acebal, C ^{[1
]}

机构：

[1] Univ Complutense Madrid, Fac Ciencias Biol, Dept Bioquim & Biol Mol 1, E-28040 Madrid, Spain

来源：

BIOTECHNOLOGY LETTERS | 2000年 / 22卷 / 12期

关键词：

enzyme immobilization; Eupergit C; penicillin V acylase; Streptomyces lavendulae;

D O I：

10.1023/A:1005601607277

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：

Penicillin acylase from Streptomyces lavendulae has been covalently immobilized to epoxy-activated acrylic beads (Eupergit C). Consecutive modification of the matrix with bovine serum albumin leads to a new biocatalyst (ECPVA) with enhanced activity (1.5 fold) in the hydrolysis of penicillin V respect to its soluble counterpart. This biocatalyst had a K-m value of 7.6 mM, slightly higher than K-m for native acylase (3 mM). In addition, ECPVA can be recycled for at least 50 consecutive batch reactions without loss of catalytic activity.

引用

页码：1011 / 1014

页数：4

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