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通过多位点诱变提高微生物转谷氨酰胺酶的活性和热稳定性。

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

作者信息

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

机构信息

a School of Food Science and Engineering, Key Laboratory for Agricultural Products Processing of Anhui Province , Hefei University of Technology , Hefei , China.

b The Key Laboratory of Molecular Microbiology and Technology, Ministry of Education , College of Life Sciences, Nankai University , Tianjin , China.

出版信息

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

DOI:10.1080/09168451.2017.1403881
PMID:29198166
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).

摘要

微生物转谷氨酰胺酶(MTG)是一种在食品工业中广泛使用的酶。在大肠杆菌中对茂原链霉菌转谷氨酰胺酶进行了多位点诱变。根据酶活性测定和热稳定性研究,在三个五位点MTG突变体(DM01 - 03)中,DM01表现出最高的酶活性,为55.7±1.4 U/mg,并且在50°C时半衰期最长(418.2分钟),在60°C时半衰期为24.8分钟。

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