ArticleFrontiers in microbiology2025
Multi-omics investigation of high-transglutaminase production mechanisms in
Article in Frontiers in microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- An efficient endogenous type I-E CRISPR-Cas genome-editing platform for producing transglutaminase inEngineering microbiology · 2026Article
- Preparation, characterization and anticancer applications of HAase from Pedobacter heparinus.BMC cancer · 2026Article
- Microbial transglutaminase in food biotechnology: from biochemical mechanisms to industrial applications.Applied microbiology and biotechnology · 2026Review
- Programmable synthetic engineering of adaptive microbial cell factories: from amide transforming enzymes to advanced biocatalytic systems.Frontiers in bioengineering and biotechnology · 2026Review
- Mechanistic Insight for Improving Transglutaminase Production Through Combined HVCP and LiCl Mutagenesis in Streptomyces mobaraensis.Current microbiology · 2025Article
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Authors and funding
9 authors.
Funding
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Abstract
Transglutaminase (TGase) has been widely applied in the food industry. However, achieving high-yield TGase production remains a challenge, limiting its broader industrial application. In this study, a high-yield strain with stable genetic traits was obtained through UV-ARTP combined mutagenesis, achieving a maximum TGase activity of 13.77 U/mL, representing a 92.43% increase. Using this strain as a forward mutation gene pool, comparative genomic research identified 95 mutated genes, which were mostly due to base substitutions that led to changes in codon usage preference. Transcriptomic analysis revealed significant expression changes in 470 genes, with 232 upregulated and 238 downregulated genes. By investigating potential key regulatory factors, comprehensive analysis indicated that changes in codon usage preference, amino acid metabolism, carbon metabolism, protein export processes, TGase activation, and spore production pathways collectively contributed to the enhancement of TGase activity. Subsequently, the in vitro activation efficiency of TGase was further improved using co-cultivation techniques with neutral proteases secreted by
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