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
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
收藏
页码:26 / 29
页数:4
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