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Improvement of the activity and thermostability of microbial transglutaminase by multiple-site mutagenesis
Authors:Dongdong Mu  Jiaojiao Lu  Chang Shu  Haowen Li  Xingjiang Li  Jing Cai
Affiliation:1. School of Food Science and Engineering, Key Laboratory for Agricultural Products Processing of Anhui Province, Hefei University of Technology, Hefei, China;2. The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education, College of Life Sciences, Nankai University, Tianjin, Chinad.mu@hfut.edu.cn
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:Microbial transglutaminase  enzymatic activity  thermostability  penta-site mutagenesis  Escherichia coli
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