CHARACTERIZATION OF BETA-GALACTOSIDASE FROM KLUYVEROMYCES-LACTIS

被引：0

作者：

CAVAILLE, D ^{[1
]}

COMBES, D ^{[1
]}

机构：

[1] INST NATL SCI APPL,CTR BIOINGN GILBERT DURAND,INRA,LA,CNRS,URA 544,F-31077 TOULOUSE,FRANCE

来源：

BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY | 1995年 / 22卷

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The properties and kinetic studies of a lactase from Kluyveromyces lactis are presented. The enzyme was subjected to both normal and denaturing electrophoresis and shown to be a dimer of M(r) of 200000, composed of two identical subunits. The lactase is a glycoprotein with 45% (w/w) carbohydrate. The Michaelis-Menten constants were determined with respect to o-nitrophenyl beta-D-galactopyranoside and lactose and were 1.7 and 17.3 mM, respectively. Galactose and glucose were competitive and non-competitive Inhibitors, respectively. A mathematical description of the kinetic data from a total lactose hydrolysis is proposed. High enzyme stability required K+ and Mg2+, and the activity was rapidly lost in deionized water.

引用

页码：55 / 64

页数：10

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