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Enantioselective oxidation of secondary alcohols at a quinohaemoprotein alcohol dehydrogenase electrode

Enantioselective oxidation of secondary alcohols at a quinohaemoprotein alcohol dehydrogenase... Quinohaemoprotein alcohol dehydrogenase fromComamonas testosteroni was co-immobilized with a redox polymer (a poly(vinylpyridine) complex functionalized with osmium bis(bipyridine) chloride) on an electrode. The enzyme electrode readily oxidizes primary alcohols and secondary alcohols with maximum current densities varying between 0.43 and 0.98 A m-2 depending on the substrate and the operation temperature. The affinity of the enzyme for aliphatic alcohols increases with the chain length of the substrate (i.e., 1-pentano1 [Km = 0.006 mM] is a much better substrate than ethanol [Km= 2.2 mM]). The same property is observed for secondary alcohols in the series 2-propanol (Km = 22 mM) to 2-octano1 (Km = 0.05 mM). The enzyme electrode is enantioselective in the oxidation of secondary alcohols. A strong preference is observed for the S-2-alcohols; the enantioselectivity increases with increasing chain length. The enantiomeric ratio (E) increases from 13 for (R,S)-2-butanol to approximately 80 for (R,S)-2-heptanol and (R,S)-2-octanol. This makes the enzyme electrode, potentially, a powerful tool for the preparation of a large range of alkanones and/or for the (kinetic) resolution of racemic alcohols. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Applied Biochemistry and Biotechnology Springer Journals

Enantioselective oxidation of secondary alcohols at a quinohaemoprotein alcohol dehydrogenase electrode

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References (25)

Publisher
Springer Journals
Copyright
Copyright © 1999 by Humana Press Inc.
Subject
Chemistry; Biotechnology; Biochemistry, general
ISSN
0273-2289
eISSN
1559-0291
DOI
10.1007/BF02787770
Publisher site
See Article on Publisher Site

Abstract

Quinohaemoprotein alcohol dehydrogenase fromComamonas testosteroni was co-immobilized with a redox polymer (a poly(vinylpyridine) complex functionalized with osmium bis(bipyridine) chloride) on an electrode. The enzyme electrode readily oxidizes primary alcohols and secondary alcohols with maximum current densities varying between 0.43 and 0.98 A m-2 depending on the substrate and the operation temperature. The affinity of the enzyme for aliphatic alcohols increases with the chain length of the substrate (i.e., 1-pentano1 [Km = 0.006 mM] is a much better substrate than ethanol [Km= 2.2 mM]). The same property is observed for secondary alcohols in the series 2-propanol (Km = 22 mM) to 2-octano1 (Km = 0.05 mM). The enzyme electrode is enantioselective in the oxidation of secondary alcohols. A strong preference is observed for the S-2-alcohols; the enantioselectivity increases with increasing chain length. The enantiomeric ratio (E) increases from 13 for (R,S)-2-butanol to approximately 80 for (R,S)-2-heptanol and (R,S)-2-octanol. This makes the enzyme electrode, potentially, a powerful tool for the preparation of a large range of alkanones and/or for the (kinetic) resolution of racemic alcohols.

Journal

Applied Biochemistry and BiotechnologySpringer Journals

Published: Dec 14, 2007

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