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

R.H.H. van den Heuvel, J. Partridge, C. Laane, P.J. Halling, W.J.H. van Berkel

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


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.
Original languageEnglish
Pages (from-to)213-216
Number of pages3
JournalFEBS Letters
Issue number2-3
Publication statusPublished - 17 Aug 2001


  • vanillyl-alcohol oxidase
  • biocatalysis
  • flavoprotein
  • medium engineering
  • quinone methide
  • Penicillium-simplicissimum
  • substrate-specificity
  • organic- solvents
  • 4-alkylphenols
  • flavinylation
  • catalysis
  • mechanism
  • enzymes


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