Substrate specificity and stereoselectivity of fatty alcohol oxidase from the yeastCandida maltosa

✍ Scribed by Stephan Mauersberger; Hannelore Drechsler; Günther Oehme; Hans-Georg Müller

• Book ID: 104651676
• Publisher: Springer
• Year: 1992
• Tongue: English
• Weight: 826 KB
• Volume: 37
• Category: Article
• ISSN: 1432-0614
• DOI: 10.1007/bf00174205

✦ Synopsis

In Candida maltosa and other alkane-utilizing yeasts a membrane-bound fatty alcohol oxidase (FAOD) is induced by growth on n-alkanes. The oxidation of 1-alkanols to the corresponding aldehydes is accompanied by the stoichiometric consumption of 1 mol 02 and formation of 1 mol hydrogen peroxide (H202). 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 txmol H202/ minx mg protein for 1-0ctanol, as well as the transformation of 2-alkanols (C8 to C16 ) to ketones. Other compounds as a,to-alkanediols, ro-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 ( -)enantiomers only, leaving the S(+)-2-alkanol untouched.