Immobilization of whole cell penicillin G acylase in open pore gelatin matrix

被引：33

作者：

Norouzian, D ^{[1
]}

Javadpour, S

Moazami, N

Akbarzadeh, A

机构：

[1] Pasteur Inst Iran, Pilot Biotechnol Dept, Tehran 13164, IR, Iran

[2] IROST, Biotechnol Res Ctr, Tehran, IR, Iran

来源：

ENZYME AND MICROBIAL TECHNOLOGY | 2002年 / 30卷 / 01期

关键词：

whole cell penicillin G acylase; immobilization;

D O I：

10.1016/S0141-0229(01)00445-8

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：

Permeabilization of the cells of E. coli with N-cetyl-N, N, N-trimethylammoniumbromide (CTAB) showed 40% increase in penicillin G acylase activity. The treated cells were immobilized in porous beads of gelatin cross-linked with glutaraldehyde. Upon entrapment the catalytic properties of enzyme were changed as compared to non-immobilized form. Hydrolysis of penicillin G by immobilized system showed 60% conversion of substrate to 6-aminopenicillanic acid in batch system, whereas in continuous system, the conversion rate was 85%. The immobilized form of whole cell penicillin acylase showed low K-m toward penicillin G as a substrate. (C) 2002 Elsevier Science Inc. All rights reserved.

引用

页码：26 / 29

页数：4

共 47 条

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