Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering

van den Heuvel, R.H.H. and Partridge, J. and Laane, C. and Halling, P.J. and van Berkel, W.J.H. (2001) Tuning of the product spectrum of vanillyl-alcohol oxidase by medium engineering. FEBS Letters, 503 (2-3). pp. 213-216. ISSN 0014-5793 (http://dx.doi.org/10.1016/S0014-5793(01)02658-8)

Full text not available in this repository.Request a copy

Abstract

The flavoenzyme vanillyl-alcohol oxidase (VAO) catalyzes the conversion of 4-alkylphenols through the initial formation of p-quinone methide intermediates. These electrophilic species are stereospecifically attacked by water to yield (R)-1-(4'- hydroxyphenyl) alcohols or rearranged in a competing reaction to 1-(4'-hydroxyphenyl)alkenes. Here, we show that the product spectrum of VAO can be controlled by medium engineering. When the enzymatic conversion of 4-propylphenol was performed in organic solvent, the concentration of the alcohol decreased and the concentration of the cis-alkene, but not the trans-alkene, increased. This change in selectivity occurred in both toluene and acetonitrile and was dependent on the water activity of the reaction medium. A similar shift in alcohol/cis-alkene product ratio was observed when the VAO-mediated conversion of 4- propylphenol was performed in the presence of monovalent anions that bind specifically near the enzyme active site. (C) 2001 Federation of European Biochemical Societies.

ORCID iDs

van den Heuvel, R.H.H., Partridge, J., Laane, C., Halling, P.J. ORCID logoORCID: https://orcid.org/0000-0001-5077-4088 and van Berkel, W.J.H.;
  • Item type:Article
    ID code:328
    Dates:
    Date
    Event
    17 August 2001
    Published
    Subjects:Science > Chemistry
    Department:Faculty of Science > Pure and Applied Chemistry
    Depositing user:Users 16 not found.
    Date deposited:13 Mar 2006
    Last modified:11 Nov 2024 08:20
    URI:https://strathprints.strath.ac.uk/id/eprint/328
CORE (COnnecting REpositories)