TGases are widely distributed in prokaryotes and eukaryotes. The covalent modifications of proteins promoted by TGase facilitate extensive applications in food, medicine, and other industries. Transglutaminases (TGase, EC 2.3.2.13), also referred to protein-glutamine γ-glutamyltransferases, are enzymes capable of catalyzing acyl-transfer reactions between the γ-carboxamide group of protein or peptide-bound glutamine and ε-amino group of lysine or other primary amines (Zhu et al. ConclusionsĪRTP is a potentially efficient tool for microbial mutation breeding to bring some significant changes required for the industrial applications. It was shown that the overexpression of TGase zymogen gene in the mutants contributes to the increase in TGase production. Compared to the wild-type strain, the transcription levels of the zymogen TGase genes in the mutants increased significantly as indicated by quantitative real-time PCR, while the gene nucleotide sequences of the mutants did not change at all. The best mutant Sm5-V1 exhibited a maximum TGase activity of 5.85 U/mL during flask fermentation. ResultsĪfter eight rounds of iterative ARTP mutagenesis, four genetically stable mutants, Sm5-V1, Sm6-V13, Sm2-V10, and Sm7-V12, were identified, which showed increased TGase production by 27, 24, 24, and 19%, respectively. mobaraensis mutants with increased TGase production. To improve the fermentation production of transglutaminase (TGase) from Streptomyces mobaraensis for applications in the food industry, the atmospheric and room-temperature plasma (ARTP) mutagenesis was applied to breed S.
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