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

Ljudmila Kulakova; Andrey Galkin; Toru Nakayama; Tokuzo Nishino; Nobuyoshi Esaki

doi:10.1016/S1381-1177(03)00012-2

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

Ljudmila Kulakova, Andrey Galkin, Toru Nakayama, Tokuzo Nishino, Nobuyoshi Esaki

ENG - Biomolecular Engineering

Research output: Contribution to journal › Article › peer-review

10 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	113-117
Number of pages	5
Journal	Journal of Molecular Catalysis - B Enzymatic
Volume	22
Issue number	1-2
DOIs	https://doi.org/10.1016/S1381-1177(03)00012-2
Publication status	Published - 2003 Apr 1

Keywords

Cold-active enzymes
Cold-adapted enzymes
Homology modeling
Protease
Psychrophile
Thermostability

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10.1016/S1381-1177(03)00012-2

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

abstract = "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 Vmax/Km,app value than those of the wild-type SapSh.",

keywords = "Cold-active enzymes, Cold-adapted enzymes, Homology modeling, Protease, Psychrophile, Thermostability",

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Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. strain Ac10 by rational mutagenesis. / Kulakova, Ljudmila; Galkin, Andrey; Nakayama, Toru et al.
In: Journal of Molecular Catalysis - B Enzymatic, Vol. 22, No. 1-2, 01.04.2003, p. 113-117.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Improvement of thermostability of cold-active serine alkaline protease from the psychrotrophic bacterium Shewanella sp. strain Ac10 by rational mutagenesis

AU - Kulakova, Ljudmila

AU - Galkin, Andrey

AU - Nakayama, Toru

AU - Nishino, Tokuzo

AU - Esaki, Nobuyoshi

PY - 2003/4/1

Y1 - 2003/4/1

N2 - 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 Vmax/Km,app value than those of the wild-type SapSh.

AB - 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 Vmax/Km,app value than those of the wild-type SapSh.

KW - Cold-active enzymes

KW - Cold-adapted enzymes

KW - Homology modeling

KW - Protease

KW - Psychrophile

KW - Thermostability

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SN - 1381-1177

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EP - 117

JO - Journal of Molecular Catalysis - B Enzymatic

JF - Journal of Molecular Catalysis - B Enzymatic

IS - 1-2

ER -

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

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Keywords

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