Purification and characterization of vanillyl-alcohol oxidase from Byssochlamys fulva V107.
Vanillyl-alcohol oxidase from Byssochlamys fulva V107 was purified to apparent homogeneity as shown by SDS-PAGE and gel-permeation HPLC. The enzyme is a homodimeric flavoenzyme consisting of two 58 kDa subunits. It catalyzes the dehydrogenation of different 4-hydroxybenzylic structures, including the conversion of 4-hydroxybenzyl alcohols such as vanillyl alcohol to the corresponding aldehydes, eugenol to coniferyl alcohol, and 4-alkylphenols to 1-(4-hydroxyphenyl)alcohols. The latter reaction was S-stereospecific and was used for the synthesis of S-1-(4-hydroxyphenyl)ethanol and -propanol with enantiomeric excesses of 81.9 and 86.0%, respectively. The catalytic and structural similarities to a Penicillium vanillyl-alcohol oxidase and Pseudomonas 4-alkylphenol methylhydroxylases are discussed.
Furukawa
H
H
Department of Biological Function and Genetic Resources Science, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan.
Wieser
M
M
Morita
H
H
Sugio
T
T
Nagasawa
T
T