Enantioselective oxidation of secondary alcohols at a quinohaemoprotein alcohol dehydrogenase electrode

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 c...

Full description

Saved in:
Bibliographic Details
Published in:Applied biochemistry and biotechnology 1998-11, Vol.75 (2-3), p.151-162
Main Authors: SOMERS, W. A. C, STIGTER, E. C. A, VAN HARTINGSVELDT, W, VAN DER LUGT, J. P
Format: Article
Language:English
Subjects:
Alcohol
Alcohol dehydrogenase
Alcohols
Aliphatic alcohols
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
Butanol
Comamonas testosteroni
Dehydrogenase
Dehydrogenases
Electrodes
Enantiomers
Enzyme electrodes
Enzymes
Ethanol
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
Octanol
Osmium
Oxidation
Polymers
Polyvinyl pyridine
Propanol
Substrates
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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^sup -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 [K^sub m^ = 0.006 mM] is a much better substrate than ethanol [K^sub m^= 2.2 mM]). The same property is observed for secondary alcohols in the series 2-propanol (K^sub m^ = 22 mM) to 2-octano1 (K^sub m^ = 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.[PUBLICATION ABSTRACT]
ISSN:0273-2289
1559-0291
DOI:10.1007/BF02787770