Purification and Characterization of L-2,3-Butanediol Dehydrogenase of Brevibacterium saccharolyticum C-1012 Expressed in Escherichia coli

@article{Takusagawa2001PurificationAC,
  title={Purification and Characterization of L-2,3-Butanediol Dehydrogenase of Brevibacterium saccharolyticum C-1012 Expressed in Escherichia coli},
  author={Y. Takusagawa and M. Otagiri and S. Ui and T. Ohtsuki and A. Mimura and M. Ohkuma and T. Kudo},
  journal={Bioscience, Biotechnology, and Biochemistry},
  year={2001},
  volume={65},
  pages={1876 - 1878}
}
  • Y. Takusagawa, M. Otagiri, +4 authors T. Kudo
  • Published 2001
  • Biology, Medicine
  • Bioscience, Biotechnology, and Biochemistry
    • The L-2,3-butanediol dehydrogenase produced in E. coli JM109/pLBD2-CTC was purified by 5 steps. The molecular mass of this enzyme was estimated at 110 kDa and the subunit was mesured to be 30 kDa. The L-BDH had some differences from the BDHs from other sources in substrate specificity, pI value, pH stability, effects of divalent cations, and organic acids. 
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