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
收藏
页码：1497 / 1502
页数：6
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