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Applied Microbiology and Biotechnology

, Volume 37, Issue 1, pp 66–73 | Cite as

Substrate specificity and stereoselectivity of fatty alcohol oxidase from the yeast Candida maltosa

  • Stephan Mauersberger
  • Hannelore Drechsler
  • Günther Oehme
  • Hans-Georg Müller
Biochemical Engineering
Received:
Accepted:

Summary

In Candida maltosa and other alkene-utilizing yeasts a membrane-bound fatty alcohol oxidase (FAOD) is induced by growth on n-alkenes. The oxidation of 1-alkanols to the corresponding aldehydes is accompanied by the stoichiometric consumption of 1 mol O2 and formation of 1 mol hydrogen peroxide (H2O2). The FAOD of C. maltosa shows a broad substrate specificity. It catalyses the oxidation of 1-alkanols (C4 to C22), with a maximal activity of 1.85 gmmol H2O2/ min × mg protein for 1-octanol, as well as the transformation of 2-alkanols (C8 to C16) to ketones. Other compounds as α,ω-alkenediols, ω-hydroxypalmitic acid, phenylalkanols and terpene alcohols are substrates for the enzyme, although mostly with decreased activities. The oxidation of the racemic 2-alkanols by the FAOD proceeds with very high stereoselectivity for the R(−)-enatiomers only, leaving the S(+)-2-alkanol untouched.

Keywords

Aldehyde Ketone Candida Substrate Specificity Maltosa 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer-Verlag 1992

Authors and Affiliations

  • Stephan Mauersberger
    • 1
  • Hannelore Drechsler
    • 1
  • Günther Oehme
    • 2
  • Hans-Georg Müller
    • 1
  1. 1.Department of EnzymologyCentral Institute of Molecular BiologyBerlin-BuchFederal Republic of Germany
  2. 2.Division of Complex CatalysisCentral Institute of Organic ChemistryRostockFederal Republic of Germany

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