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Home > Archive>Volume 38, Issue 6, 2019 >1-10. DOI:10.3969/j.issn.1673-1689.2019.06.001
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Recent Applications of Microbial Transglutaminase in Protein Modificaiton
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    Abstract:

    Transglutaminases are a family of enzymes to ligate the carbonyl group of glutamines and the ?着-amine group of lysine to form an amide bond between proteins. This conjugation technology was widely used in food and textile industry initially. Recently，microbial transglutaminases（MTGase） mediated ligation was developed into a useful tool for site-specific modification of protein because of the advantages，such as easy availability，mild reaction condition and Ca2+-independent etc. By introducing MTGase recognized Q-tag and K-tag into protein using genetic engineering technology，many molecules，including small molecular drugs，proteins，polymers，oligosaccharides and lipids are conjugated to proteins，and peptide cyclized through this site-specific acyl transfer reaction. These conjugates were extensively used in the fields of medicinal chemistry，chemical biology and biomaterials. This review focused on the recent progress of MTGase mediated site-specific protein modification.

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CHENG Xiaozhong, ZHAO Xinrui, HONG Haofei, YANG Min, ZHOU Zhifang, WU Zhimeng. Recent Applications of Microbial Transglutaminase in Protein Modificaiton[J]. Journal of Food Science and Biotechnology,2019,38(6):1-10.

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  • Online: January 07,2020
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