Applied Microbiology and Biotechnology

, Volume 37, Issue 1, pp 66–73

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

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

DOI: 10.1007/BF00174205

Cite this article as:
Mauersberger, S., Drechsler, H., Oehme, G. et al. Appl Microbiol Biotechnol (1992) 37: 66. doi:10.1007/BF00174205

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.

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
  3. 3.Max Delbrück Centre, for Molecular MedicineBerlin-BuchFRG

Personalised recommendations