Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli
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概要
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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.
- 社団法人 日本農芸化学会の論文
著者
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Yang Hui-Lin
College of Bioscience and Bioengineering, South China University of Technology
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Pan Li
College of Bioscience and Bioengineering, South China University of Technology
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Lin Ying
College of Bioscience and Bioengineering, South China University of Technology
関連論文
- Purification and On-Column Activation of a Recombinant Histidine-Tagged Pro-Transglutaminase after Soluble Expression in Escherichia coli
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- A Comparison of the Unfolded Protein Response in Solid-State with Submerged Cultures of Aspergillus oryzae