PREPARATION AND PROPERTIES OF AN IMMOBILIZED DERIVATIVE OF PENICILLINASE

被引：10

作者：

KLEMES, Y

CITRI, N

机构：

[1] Institute of Microbiology, Hebrew University—Hadassah Medical School, Jerusalem

来源：

BIOTECHNOLOGY AND BIOENGINEERING | 1979年 / 21卷 / 05期

关键词：

D O I：

10.1002/bit.260210512

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：

Penicillinase (β‐lactamase I, EC 3.5.2.6)secreted by Bacilluus cereus, strain 569/H, was covalently attached to aminoethyl cellulose via glutaraldehyde. The immobilized derivative shows increased thermostability and decreased susceptibility to conformational changes induced by certain substrates of penicillinase. The decline in the rate of such substrates was consequently suppressed by immobilization. A marked increase in Km was observed with all substrates except for the unsubstituted 6‐aminopenicillanic acid. The altered properties of the new derivative are attributed to the constraint imposed by immobilization on the conformational flexibility of the enzyme molecule. Thus, apart from obvious technological interest, immobilized penicillinase provides a useful model for the study of the role of flexibility in the function of an enxyme. Copyright © 1979 John Wiley & Sons, Inc.

引用

页码：897 / 905

页数：9

共 16 条

[1] ACQUISITION OF SUBSTRATE-SPECIFIC PARAMETERS DURING CATALYTIC REACTION OF PENICILLINASE [J].