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

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

doi:10.6084/m9.figshare.5662249.v1

tbbb_a_1403881_sm4002.docx (161.03 kB)

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

journal contribution

posted on 2017-12-04, 08:51 authored by Dongdong Mu, Jiaojiao Lu, Chang Shu, Haowen Li, Xingjiang Li, Jing Cai, Shuizhong Luo, Peizhou Yang, Shaotong Jiang, Zhi Zheng

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).