Abstract
Microbial transglutaminase (MTG) is widely used as a protein crosslinking enzyme. Pro-transglutaminase from Streptomyces mobaraensis was expressed in Escherichia coli as a fusion protein carrying a C-terminal histidine tag (pro-MTG-His6) under high-density culture. A new method of on-column activation was designed for production. According to SDS-PAGE, 88.9% of pro-MTG-His6 was transferred to mature MTG-His6 with storage stabilization.
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Yang, H. L., Pan, L., & Lin, Y. (2009). Purification and on-column activation of a recombinant histidine-tagged pro-transglutaminase after soluble expression in Escherichia coli. Bioscience, Biotechnology and Biochemistry, 73(11), 2531–2534. https://doi.org/10.1271/bbb.90422
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