IMMOBILIZATION STUDIES OF AN INDUSTRIAL PENICILLIN ACYLASE PREPARATION ON A SILICA CARRIER

被引:0
|
作者
FONSECA, LP
CARDOSO, JP
CABRAL, JMS
机构
[1] Univ Tecn Lisboa, ENGN BIOQUIM LAB, INST SUPER TECN, P-1096 LISBON, PORTUGAL
[2] CO IND PROD ANTIBIOT SA, P-2580 ALENQUER, PORTUGAL
关键词
PENICILLIN ACYLASE; COVALENT IMMOBILIZATION; SILICA; SILANIZATION; OPERATIONAL STABILITY; REUTILIZATION CAPACITY; PENICILLIN-G HYDROLYSIS; 2 PARAMETER MODEL;
D O I
暂无
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 (EC 3.5. 1.11) was immobilized by covalent binding on a silica gel carrier activated by silanization. High immobilization yields, operational stability, enzyme loading and support reutilization capacity were obtained. The effects of several variables on the activation of the support and on the immobilization method were studied. Other supports and immobilization methods were assessed for the immobilization of penicillin acylase and compared with the basic process used. Activity versus temperature, pH, buffer molarity and penicillin concentration profiles were determined and compared for the free, crosslinked and covalently-bound silica carrier penicillin acylase preparations. The hydrolysis performance of the latter preparation was assessed in a batch basket reactor and the time course of the hydrolysis reaction modelled by a two parameter model equation. The operational stabilities of penicillin acylase coupled covalently to the silica gel support and immobilized by a crosslinking procedure using glutaraldehyde were also compared.
引用
收藏
页码:27 / 37
页数:11
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