Applied Microbiology and Biotechnology

, Volume 51, Issue 4, pp 486–490

Stereoselective reduction of ethyl 4-chloro-3-oxobutanoate by Escherichia coli transformant cells coexpressing the aldehyde reductase and glucose dehydrogenase genes

Authors

  • M. Kataoka
    • Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan Tel.: +81-75-7536462 Fax: +81-75-7536128
  • K. Yamamoto
    • Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan Tel.: +81-75-7536462 Fax: +81-75-7536128
  • H. Kawabata
    • Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan Tel.: +81-75-7536462 Fax: +81-75-7536128
  • M. Wada
    • Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan Tel.: +81-75-7536462 Fax: +81-75-7536128
  • K. Kita
    • Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680-0945, Japan
  • H. Yanase
    • Department of Biotechnology, Faculty of Engineering, Tottori University, Tottori 680-0945, Japan
  • S. Shimizu
    • Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Kitashirakawa-Oiwakecho, Sakyo-ku, Kyoto 606-8502, Japan Tel.: +81-75-7536462 Fax: +81-75-7536128
ORIGINAL PAPER

DOI: 10.1007/s002530051421

Cite this article as:
Kataoka, M., Yamamoto, K., Kawabata, H. et al. Appl Microbiol Biotechnol (1999) 51: 486. doi:10.1007/s002530051421

Abstract

The asymmetric reduction of ethyl 4-chloro-3-oxobutanoate (COBE) to ethyl (R)-4-chloro-3-hydroxybutanoate [(R)-CHBE] using Escherichia coli cells, which coexpress both the aldehyde reductase gene from Sporobolomyces salmonicolor and the glucose dehydrogenase (GDH) gene from Bacillus megaterium as a catalyst was investigated. In an organic solvent-water two-phase system, (R)-CHBE formed in the organic phase amounted to 1610 mM (268 mg/ml), with a molar yield of 94.1% and an optical purity of 91.7% enantiomeric excess. The calculated turnover number of NADP+ to CHBE formed was 13 500 mol/mol. Since the use of E. coli JM109 cells harboring pKAR and pACGD as a catalyst is simple, and does not require the addition of GDH or the isolation of the enzymes, it is highly advantageous for the practical synthesis of (R)-CHBE.

Copyright information

© Springer-Verlag Berlin Heidelberg 1999