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

Dongdong Mu; Jiaojiao Lu; Chang Shu; Haowen Li; Xingjiang Li; Jing Cai; Shuizhong Luo; Peizhou Yang; Shaotong Jiang; Zhi Zheng

doi:10.1080/09168451.2017.1403881

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

Biosci Biotechnol Biochem. 2018 Jan;82(1):106-109. doi: 10.1080/09168451.2017.1403881. Epub 2017 Dec 4.

Authors

Dongdong Mu^{1

2}, Jiaojiao Lu¹, Chang Shu¹, Haowen Li¹, Xingjiang Li¹, Jing Cai¹, Shuizhong Luo¹, Peizhou Yang¹, Shaotong Jiang¹, Zhi Zheng¹

Affiliations

¹ a School of Food Science and Engineering, Key Laboratory for Agricultural Products Processing of Anhui Province , Hefei University of Technology , Hefei , China.
² b The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education , College of Life Sciences, Nankai University , Tianjin , China.

PMID: 29198166
DOI: 10.1080/09168451.2017.1403881

Abstract

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 °C (418.2 min) and 60 °C (24.8 min).

Keywords: Escherichia coli; Microbial transglutaminase; enzymatic activity; penta-site mutagenesis; thermostability.

MeSH terms

Enzyme Activation
Enzyme Stability
Escherichia / genetics
Mutation
Streptomyces / enzymology*
Temperature
Transglutaminases / genetics
Transglutaminases / metabolism*

Substances

Transglutaminases