Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp strain Ac10 by rational mutagenesis

被引:6
作者
Kulakova, L
Galkin, A
Nakayama, T
Nishino, T
Esaki, N [1 ]
机构
[1] Kyoto Univ, Inst Chem Res, Uji, Kyoto 6110011, Japan
[2] Tohoku Univ, Grad Sch Engn, Dept Biomol Engn, Sendai, Miyagi 9808579, Japan
关键词
protease; cold-active enzymes; cold-adapted enzymes; psychrophile; thermostability; homology modeling;
D O I
10.1016/S1381-1177(03)00012-2
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
A serine alkaline protease (SapSh) from a psychrophilic bacterium Shewanella sp. strain Ac10 is a cold-active subtilase with low thermostability [Appl. Environ. Microbiol. 65 (1999) 611-617]. By means of homology modeling with other subtilase structures, we have constructed a mutant SapSh containing an extra salt bridge on its surface that exhibits higher thermostability and even higher V,(max)/K-m, (app) value than those of the wild-type SapSh. (C) 2003 Elsevier Science B.V. All rights reserved.
引用
收藏
页码:113 / 117
页数:5
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