Improved catalytic efficiency of catalase from Bacillus subtilis by rational mutation of Lys114

被引：15

作者：

Cao, Wenlong ^{[1
,2
,3
,4
]}

Kang, Zhen ^{[1
,2
,3
,4
]}

Liu, Song ^{[2
,3
,4
]}

Liu, Long ^{[1
,2
,3
,4
]}

Du, Guocheng ^{[1
,3
,4
,6
]}

Chen, Jian ^{[1
,3
,4
,5
]}

机构：

[1] Jiangnan Univ, Synerget Innovat Ctr Food Safety & Nutr, Wuxi 214122, Peoples R China

[2] Jiangnan Univ, Minist Educ, Key Lab Ind Biotechnol, Wuxi 214122, Peoples R China

[3] Jiangnan Univ, Sch Biotechnol, Wuxi 214122, Peoples R China

[4] Jiangnan Univ, Synergy Innovat Ctr Modern Ind Fermentat, Wuxi 214122, Peoples R China

[5] Jiangnan Univ, Natl Engn Lab Cereal Fermentat Technol, Wuxi 214122, Peoples R China

[6] Jiangnan Univ, Minist Educ, Key Lab Carbohydrate Chem & Biotechnol, Wuxi 214122, Peoples R China

来源：

PROCESS BIOCHEMISTRY | 2014年 / 49卷 / 09期

基金：

国家高技术研究发展计划(863计划); 美国国家科学基金会;

关键词：

Catalase; Enzyme engineering; Site-directed mutagenesis; Catalytic efficiency; AMINO-ACID-RESIDUES; THERMOSTABILITY; PURIFICATION; IDENTIFICATION; MECHANISMS; STABILITY; ESTERASE;

D O I：

10.1016/j.procbio.2014.05.016

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：

Alkaline catalases with good properties are desirable in the textile industry. In the present work, by applying the PoPMuSiC algorithm for the calculation of the folding free energy, Lys114 of a Bacillus catalase was rationally selected and engineered to improve the thermostability. Interestingly, the Lys114Tyr, Lys114Val, Lys114Met and Lys114Ile variants showed higher catalytic efficiencies when compared with the wild-type protein. In particular, the Lys114Tyr variant showed the highest catalytic efficiency, which was 5.3-fold of the wild-type catalase. The production of the Lys114Tyr variant may represent an improved catalase suitable for industrial purposes. (C) 2014 Elsevier Ltd. All rights reserved.

引用

页码：1497 / 1502

页数：6

共 34 条

[31] Identification of essential amino acid residues for catalytic activity and thermostability of novel chitosanase by site-directed mutagenesis [J].