PURIFICATION AND PROPERTIES OF A NEUTRAL PROTEASE PRODUCED BY LACTOBACILLUS-BREVIS

被引：5

作者：

AMUND, OO

OMIDIJI, O

ILORI, O

机构：

[1] Department of Biological Sciences, University of Lagos, Lagos

来源：

JOURNAL OF BIOTECHNOLOGY | 1990年 / 13卷 / 04期

关键词：

Cation; Lactobacillus; pH; Protease; Temperature;

D O I：

10.1016/0168-1656(90)90083-N

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 proteolytic enzyme was produced by a strain of Lactobacillus brevis isolated from an oriental beverage. The enzyme was extracted and purified 50-fold by gel filtration and ion-exchange chromatography. The optimum pH for the enzyme was 7.0, the optimum temperature 35°C and the molecular weight 34,674 Da. Furthermore, the enzyme was stimulated by cations including Ca2+, Mg2+, Na+ and K+ and inhibited by Zn2+ and Co2+ ions. Other inhibitors were EDTA, ascorbic acid and citric acid. The enzyme is probably a neutral metalloprotease. © 1993.

引用

页码：361 / 365

页数：5

共 20 条

[1]

AMRUTE SB, 1978, DEV IND MICROBIOL, V19, P465

[2] ESTIMATION OF MOLECULAR WEIGHTS OF PROTEINS BY SEPHADEX GEL-FILTRATION [J].