ArticleApplied microbiology and biotechnology2024
Random mutagenesis and disulfide bond formation improved thermostability in microbial transglutaminase.
Article in Applied microbiology and biotechnology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Thermostability engineering of microbial transglutaminase using artificial intelligence and investigation of its underlying mechanisms.Bioresources and bioprocessing · 2026Article
- Microbial transglutaminase in food biotechnology: from biochemical mechanisms to industrial applications.Applied microbiology and biotechnology · 2026Review
- Introduction of multiple disulfide bonds increases the thermostability of transglutaminase.Scientific reports · 2025Article
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Authors and funding
8 authors.
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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 T
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