Purification and properties of a protease produced by Bacillus subtilis CN2 isolated from a Vietnamese fish sauce

被引:37
作者
Uchida, H
Kondo, D
Yamashita, S
Tanaka, T
Tran, LH
Nagano, H
Uwajima, T
机构
[1] Univ Fukui, Fac Engn, Dept Appl Chem & Biotechnol, Fukui 9108507, Japan
[2] Hanoi Univ Technol, Inst Food Technol Biotechnol, Hanoi, Vietnam
[3] Gifu Univ, Fac Educ, Gifu 5011193, Japan
关键词
Bacillus subtilis; caseinolytic activity; collagenolytic activity; protease; serine enzyme; Vietnamese fish sauce;
D O I
10.1023/B:WIBI.0000043168.15067.44
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
Bacillus subtilis CN2 isolated from a Vietnamese fish sauce produced a large quantity of an alkaline protease, when grown on a soy peptone medium. The protease was purified to an electrophoretically homogeneous state and crystallized in its pure condensed solution. The molecular weight was determined to be 27,636 Da, and the N-terminal amino acid sequence was AQSVPYGISQIKAPAL. The optimum pH and temperature were pH 10.0 and 50 degreesC, respectively. The protease was active over a wide pH range of pH 7.0-11.0, and also active over a broad temperature range of 30-60 degreesC. The enzyme was potently inhibited by 1 mM phenylmethanesulphonyl fluoride, but resistant to 1 mM sodium dodecyl sulphate (SDS).
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页码:579 / 582
页数:4
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