Characterization of the Enantioselective Properties of the Quinohemoprotein Alcohol Dehydrogenase of<i>Acetobacter pasteurianus</i>LMG 1635. 1. Different Enantiomeric Ratios of Whole Cells and Purified Enzyme in the Kinetic Resolution of Racemic Glycidol

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  • MACHADO Sonia Salgueiro
    Department of Microbiology and Enzymology, Kluyver Institute for Biotechnology, Delft University of Technology
  • WANDEL Ute
    Department of Microbiology and Enzymology, Kluyver Institute for Biotechnology, Delft University of Technology
  • JONGEJAN Jaap A.
    Department of Microbiology and Enzymology, Kluyver Institute for Biotechnology, Delft University of Technology
  • STRAATHOF Adrie J. J.
    Department of Microbiology and Enzymology, Kluyver Institute for Biotechnology, Delft University of Technology
  • DUINE Johannis A.
    Department of Microbiology and Enzymology, Kluyver Institute for Biotechnology, Delft University of Technology

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  • Characterization of the Enantioselective Properties of the Quinohemoprotein Alcohol Dehydrogenase of Acetobacter pasteurianus LMG 1635. 1. Different Enantiomeric Ratios of Whole Cells and Purified Enzyme in the Kinetic Resolution of Racemic Glycidol.
  • Characterization of the enantioselective properties of the quinohemoprotein alcohol dehydrogenase of Acetobacter pasteurianus LMG 1635

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  Resting cells of Acetobacter pasteurianus LMG 1635 (ATCC 12874) show appreciable enantioselectivity (E=16-18) in the oxidative kinetic resolution of racemic 2,3-epoxy-1-propanol, glycidol. Distinctly lower values (E=7-9) are observed for the ferricyanide-coupled oxidation of glycidol by the isolated quinohemoprotein alcohol dehydrogenase, QH-ADH, which is responsible for the enantiospecific oxidation step in whole cells. The accuracy of E-values from conversion experiments could be verified using complementary methods for the measurement of enantiomeric ratios. Effects of pH, detergent, the use of artificial electron acceptors, and the presence of intermediate aldehydes, could be accounted for. Measurements of E-values at successive stages of the purification showed that the drop in enantioselectivity correlates with the separation of QH-ADH from the cytoplasmic membrane. It is argued that the native arrangement of QH-ADH in the membrane-associated complex favors the higher E-values. The consequences of these findings for the use of whole cells versus purified enzymes in biocatalytic kinetic resolutions of chiral alcohols are discussed.<br>

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