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Tuning of the product spectrum of vanillyl‐alcohol oxidase by medium engineering
Author(s) -
van den Heuvel Robert H.H,
Partridge Johann,
Laane Colja,
Halling Peter J,
van Berkel Willem J.H
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02658-8
Subject(s) - chemistry , alkene , alcohol , medicinal chemistry , yield (engineering) , selectivity , solvent , acetonitrile , electrophile , organic chemistry , photochemistry , catalysis , materials science , metallurgy
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.