Enhancing the thermostability of transglutaminase from Streptomyces mobaraensis based on the rational design of a disulfide bond.

doi:10.1016/j.pep.2022.106079

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Article

Enhancing the thermostability of transglutaminase from Streptomyces mobaraensis based on the rational design of a disulfide bond.

Protein expression and purification - 1 Aug 2022

Wang Hongjing, Chen Haiqing, Li Qingbin, Yu Fan, Yan Yaru, Liu Shuang, Tian Jian, Tan Jianxin

Abstract excerpt

Transglutaminase (TGase), a transferase, is widely adopted in the food industry and other biological fields due to its unique characteristics of modifying proteins by intra- or intermolecular cross-linking. However, obtaining a mutant TGase that is highly thermostable and active would significantly aid in food processing. Therefore, this study sought to improve the thermostability of TGase by introducing an...

Topics

Disulfides
Enzyme Stability
Mutation
Streptomyces
Temperature
Transglutaminases

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Open in PubMed

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PMID: 35272012
DOI: 10.1016/j.pep.2022.106079

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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