Covalent immobilization of penicillin acylase from Streptomyces lavendulae

被引：38
|
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
收藏
页码：1011 / 1014
页数：4
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