Overproduction of microbial transglutaminase in Escherichia coli, in vitro refolding, and characterization of the refolded form.

@article{Yokoyama2000OverproductionOM,
  title={Overproduction of microbial transglutaminase in Escherichia coli, in vitro refolding, and characterization of the refolded form.},
  author={Kei-ichi Yokoyama and Norifumi Nakamura and Katsuya Seguro and Keiko Kubota},
  journal={Bioscience, biotechnology, and biochemistry},
  year={2000},
  volume={64 6},
  pages={1263-70}
}
(MTG) The Streptoverticillium transglutaminase gene, synthesized previously for yeast expression, was modified and resynthesized for overexpression in E. coli. A high-level expression plasmid, pUCTRPMTG-02(+), was constructed. Furthermore, to eliminate the N-terminal methionine, pUCTRPMTGD2 was constructed. Cultivation of E. coli transformed with pUCTRPMTG02(+) or pUCTRPMTGD2 yielded a large amount of MTG (200-300 mg/liter) as insoluble inclusion bodies. The N-terminal amino acid residue of the… CONTINUE READING