PRODUCTION AND PROPERTIES OF AN EXTRACELLULAR METALLOPROTEASE FROM A PSYCHROPHILIC PSEUDOMONAS-FLUORESCENS

被引：11

作者：

MARGESIN, R

SCHINNER, F

机构：

[1] Institute of Microbiology, University of Innsbruck, Innsbruck

来源：

JOURNAL OF BIOTECHNOLOGY | 1992年 / 24卷 / 02期

关键词：

METALLOPROTEASE; PSEUDOMONAS-FLUORESCENS; PSYCHROPHILIC;

D O I：

10.1016/0168-1656(92)90125-S

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：

A psychrophilic Pseudomonas fluorescens forming protease was isolated from glacier materials. The largest amount of protease was excreted at a cultivation temperature of 10-degrees-C after 96 h. The purified enzyme was a metalloprotease (inhibition by EDTA) and had a molecular mass of approximately 50 kDa and an isoelectric point of 7.4-7.5. Maximal activity towards azocasein was observed at 40-degrees-C and pH 6.0-7.0. The enzyme showed a high thermo-instability and a low activation energy. Only up to a casein concentration of 0.4% a Michaelis-Menten kinetics was observed.

引用

页码：207 / 210

页数：4

共 8 条

[1]

BRADFORD MM, 1976, ANAL BIOCHEM, V72, P248, DOI 10.1016/0003-2697(76)90527-3

[2]

EGGEN R, 1990, FEMS MICROBIOL LETT, V71, P17

[3] ISOLATION AND CHARACTERIZATION OF A STREPTOMYCES C5 MUTANT STRAIN HYPERPRODUCTIVE OF EXTRACELLULAR PROTEASE [J].