CLONING AND CHARACTERIZATION OF BETA-GALACTOSIDE AND BETA-GLUCOSIDE HYDROLYZING ENZYMES OF THERMOTOGA-MARITIMA

被引：15

作者：

GABELSBERGER, J ^{[1
]}

LIEBL, W ^{[1
]}

SCHLEIFER, KH ^{[1
]}

机构：

[1] TECH UNIV MUNICH,LEHRSTUHL MIKROBIOL TECH,ARCISSTR 21,W-8000 MUNICH 2,GERMANY

来源：

FEMS MICROBIOLOGY LETTERS | 1993年 / 109卷 / 2-3期

关键词：

THERMOTOGA-MARITIMA; THERMOSTABLE ENZYME; BETA-GALACTOSIDASE; BETA-GLUCOSIDASE;

D O I：

10.1016/0378-1097(93)90009-Q

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

A gene library of the hyperthermophilic bacterium Thermotoga maritima strain MSB8 was constructed in Escherichia coli. Two non-related T. maritima chromosomal DNA fragments were physically characterized. They conferred the synthesis of thermostable X-Gal (5-bromo-4-chloro-3-indolyl-beta-D-galactopyranoside)-hydrolysing activity upon the host organism. The biochemical properties of the recombinant enzymes indicated that genes for a beta-galactosidase (BgaA) and a broad-specificity beta-glucosidase (BglA) had been isolated. The genes were designated bgaA and bglA, respectively. According to analytical size exclusion chromatography data, BgaA and BglA had native molecular masses of approximately 240 kDa and 95 kDa, respectively. Both enzymes apparently have dimeric subunit structure. An additional beta-glucosidase (designated BglB) activity, clearly distinct from BglA in terms of substrate specificity, could be detected in a crude extract of T. maritima.

引用

页码：131 / 137

页数：7

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