Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli

Hui-Lin YANG; Li PAN; Ying LIN

doi:10.1271/bbb.90422

Microbiology & Fermentation Technology Notes

Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli

Hui-Lin YANG, Li PAN, Ying LIN

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Keywords: microbial transglutaminase, soluble recombinant expression, high-density culture, Escherichia coli, on-column activation

JOURNAL FREE ACCESS

2009 Volume 73 Issue 11 Pages 2531-2534

DOI https://doi.org/10.1271/bbb.90422

View "Advance Publication" version (November 7, 2009).

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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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