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

来源：

JOURNAL OF MOLECULAR CATALYSIS B-ENZYMATIC | 2003年 / 22卷 / 1-2期

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

页码：113 / 117

页数：5

共 26 条

[1] Cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella strain Ac10:: Gene cloning and enzyme purification and characterization
Kulakova, L
Galkin, A
Kurihara, T
Yoshimura, T
Esaki, N
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 1999, 65 (02) : 611 - 617
[2] Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A: enzyme purification and characterization
Runying Zeng
Rui Zhang
Jing Zhao
Nianwei Lin
Extremophiles, 2003, 7 : 335 - 337
[3] Cold-active serine alkaline protease from the psychrophilic bacterium Pseudomonas strain DY-A:: enzyme purification and characterization
Zeng, RY
Zhang, R
Zhao, J
Lin, NW
EXTREMOPHILES, 2003, 7 (04) : 335 - 337
[4] Identification of cold-inducible inner membrane proteins of the psychrotrophic bacterium, Shewanella livingstonensis Ac10, by proteomic analysis
Jungha Park
Jun Kawamoto
Nobuyoshi Esaki
Tatsuo Kurihara
Extremophiles, 2012, 16 : 227 - 236
[5] Identification of cold-inducible inner membrane proteins of the psychrotrophic bacterium, Shewanella livingstonensis Ac10, by proteomic analysis
Park, Jungha
Kawamoto, Jun
Esaki, Nobuyoshi
Kurihara, Tatsuo
EXTREMOPHILES, 2012, 16 (02) : 227 - 236
[6] Cold-active DnaK of an Antarctic psychrotroph Shewanella sp Ac10 supporting the growth of dnaK-null mutant of Escherichia coli at cold temperatures
Yoshimune, K
Galkin, A
Kulakova, L
Yoshimura, T
Esaki, N
EXTREMOPHILES, 2005, 9 (02) : 145 - 150
[7] Purification and Characterization of an Extracellular Cold-active Protease Produced by the Psychrotrophic Bacterium Serratia Sp WJ39
Ji, Xiu-ling
Taj, Muhammad Kamran
Lu, Xiao-bo
Lin, Lian-bing
Zhang, Qi
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MATERIALS, MACHINES AND DEVELOPMENT OF TECHNOLOGIES FOR INDUSTRIAL PRODUCTION, 2014, 618 : 330 - +
[8] Construction of a low-temperature protein expression system using a cold-adapted bacterium, Shewanella sp strain Ac10, as the host
Miyake, Ryoma
Kawamoto, Jun
Wei, Yun-Lin
Kitagawa, Masanari
Kato, Ikunoshin
Kurihara, Tatsuo
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APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2007, 73 (15) : 4849 - 4856
[9] Cold-active DnaK of an Antarctic psychrotroph Shewanella sp. Ac10 supporting the growth of dnaK-null mutant of Escherichia coli at cold temperatures
Kazuaki Yoshimune
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Ljudmila Kulakova
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Extremophiles, 2005, 9 : 145 - 150
[10] Unexpectedly high thermostability of an NADP-dependent malic enzyme from a psychrophilic bacterium, Shewanella livingstonensis Ac10
Luo, Gonglinfeng
Fujii, Sotaro
Koda, Takumi
Tajima, Takahisa
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Hida, Akiko
Kato, Junichi
JOURNAL OF BIOSCIENCE AND BIOENGINEERING, 2021, 132 (05) : 445 - 450

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