A NEW ALKALINE SERINE-PROTEASE FROM ALKALOPHILIC BACILLUS SP - CLONING, SEQUENCING, AND CHARACTERIZATION OF AN INTRACELLULAR PROTEASE

被引：13
|
作者：
YAMAGATA, Y [1 ]
ICHISHIMA, E [1 ]
机构：
[1] TOHOKU UNIV,FAC AGR,DEPT APPL BIOL CHEM,MOLEC ENZYMOL LAB,AOBA KU,SENDAI,MIYAGI 981,JAPAN
来源：
CURRENT MICROBIOLOGY | 1995年 / 30卷 / 06期
关键词：
D O I：
10.1007/BF00369863
中图分类号：
Q93 [微生物学];
学科分类号：
071005 ; 100705 ;
摘要：
To obtain a new serine protease from alkalophilic Bacillus sp. NKS-21, shotgun cloning was carried out. As a result, a new protease gene was obtained. It encoded an intracellular serine protease (ISP-1) in which there was no signal sequence. The molecular weight was 34,624. The protease showed about 50% homology with those of intracellular serine proteases (ISP-1) from Bacillus subtilis, B. polymyxa, and alkalophilic Bacillus sp. No. 221. The amino acid residues that form the catalytic triad, Ser, His and Asp, were completely conserved in comparison with subtilisins (the extracellular proteases from Bacillus). The cloned intracellular protease was expressed in Escherichia coli, and its purification and characterization were carried out. The enzyme showed stability under alkaline condition at pH 10 and tolerance to surfactants. The cloned ISP-1 digested well nucleoproteins, clupein and salmin, for the substrates.
引用
收藏
页码：357 / 366
页数：10
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