Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Microbiology & Fermentation Technology Notes
Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli
Hui-Lin YANGLi PANYing LIN
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2009 年 73 巻 11 号 p. 2531-2534

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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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© 2009 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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