Improvement of the activity and thermostability of microbial transglutaminase by multiple-site mutagenesis

被引：34

作者：

Mu, Dongdong ^{[1
,2
]}

Lu, Jiaojiao ^{[1
]}

Shu, Chang ^{[1
]}

Li, Haowen ^{[1
]}

Li, Xingjiang ^{[1
]}

Cai, Jing ^{[1
]}

Luo, Shuizhong ^{[1
]}

Yang, Peizhou ^{[1
]}

Jiang, Shaotong ^{[1
]}

Zheng, Zhi ^{[1
]}

机构：

[1] Hefei Univ Technol, Sch Food Sci & Engn, Key Lab Agr Prod Proc Anhui Prov, Hefei, Anhui, Peoples R China

[2] Nankai Univ, Coll Life Sci, Key Lab Mol Microbiol & Technol, Minist Educ, Tianjin, Peoples R China

来源：

BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY | 2018年 / 82卷 / 01期

关键词：

Microbial transglutaminase; enzymatic activity; thermostability; penta-site mutagenesis; Escherichia coli; ESCHERICHIA-COLI; STREPTOVERTICILLIUM-MOBARAENSE; PRO-TRANSGLUTAMINASE; PURIFICATION; EXPRESSION; PEPTIDE;

D O I：

10.1080/09168451.2017.1403881

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：

Microbial transglutaminase (MTG) is an enzyme widely used in the food industry. Mutiple-site mutagenesis of Streptomyces mobaraensis transglutaminase was performed in Escherichia coli. According to enzymatic assay and thermostability study, among three penta-site MTG mutants (DM01-03), DM01 exhibited the highest enzymatic activity of 55.7 +/- 1.4 U/mg and longest half-life at 50 degrees C (418.2min) and 60 degrees C (24.8min).

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收藏

页码：106 / 109

页数：4

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