Random mutagenesis and disulfide bond formation improved thermostability in microbial transglutaminase.

ABSTRACT: Microbial transglutaminase (MTG) from Streptomyces mobaraensis is widely used in the food and pharmaceutical industries for cross-linking and post-translational modification of proteins. It is believed that its industrial applications could be further broadened by improving its thermostability. In our previous study, we showed that the introduction of structure-based disulfide bonds improved the thermostability of MTG, and we succeeded in obtaining a thermostable mutant, D3C/G283C, with a T₅₀ (incubation temperature at which 50% of the initial activity remains) 9 °C higher than that of wild-type MTG. In this study, we performed random mutations using D3C/G283C as a template and found several amino acid substitutions that contributed to the improvement of thermostability, and inv

SUBMITTER: Suzuki M 

PROVIDER: S-EPMC11445358 | biostudies-literature | 2024 Oct

REPOSITORIES: biostudies-literature