Introduction of multiple disulfide bonds increases the thermostability of transglutaminase

Introduction of multiple disulfide bonds increases the thermostability of transglutaminase

Abstract Microbial transglutaminase (MTG) is an enzyme that catalyzes the cross-linking of glutamine and lysine residues in proteins. Because of its ability to modify proteins, MTG has various applications in the medical and food industries. Most studies have aimed to enhance the thermal stability o...

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Bibliographic Details
Main Authors: Takuto Ono, Kazutoshi Takahashi, Yoshinori Hirao, Yasuhiro Mihara, Isao Abe, Ayaka Shirasawa, Masayuki Sugiki
Format: Article
Language:English
Published: Nature Portfolio 2025-07-01
Series:Scientific Reports
Subjects:
Microbial transglutaminase
Disulfide bond
Thermal stability
Mutant
Enzyme kinetics
Online Access:https://doi.org/10.1038/s41598-025-07842-5
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https://doi.org/10.1038/s41598-025-07842-5

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