PURIFICATION AND PROPERTIES OF A NOVEL SURFACE-ACTIVE AGENT-RESISTANT AND ALKALINE-RESISTANT PROTEASE FROM BACILLUS SP Y

被引：76

作者：

SHIMOGAKI, H ^{[1
]}

TAKEUCHI, K ^{[1
]}

NISHINO, T ^{[1
]}

OHDERA, M ^{[1
]}

KUDO, T ^{[1
]}

OHBA, K ^{[1
]}

IWAMA, M ^{[1
]}

IRIE, M ^{[1
]}

机构：

[1] HOSHI COLL PHARM, DEPT MICROBIOL, SHINAGAWA KU, TOKYO 142, JAPAN

来源：

AGRICULTURAL AND BIOLOGICAL CHEMISTRY | 1991年 / 55卷 / 09期

关键词：

D O I：

10.1080/00021369.1991.10870947

中图分类号：

S3 [农学（农艺学）];

学科分类号：

0901 ;

摘要：

In the course of a search for an alkaline stable protease for industrial use, an alkaline protease (protease BYA) was isolated from an alkalophilic Bacillus sp. Y, and its properties were characterized. Its optimum pH was pH 10.0-12.5, when casein was used as a substrate. In addition to the stability of protease BYA at pH 6.5-13.0, it was also very stable towards various surface-active agents, such as sodium dodecyl sulfate and sodium linear alkylbenzene sulfonate. Protease BYA was most active at 70-degrees-C. The isoelectric point (pI) of protease BYA was about 10.1. Protease BYA was characterized as a serine protease because of its sensitivity to phenylmethanesulfonyl fluoride and diisopropyl fluorophosphate. The protease seems to be related to proteases of the subtilisin family, such as subtilisin BPN', subtilisin Carlsberg, and No. 221 protease.

引用

页码：2251 / 2258

页数：8