title: Purification and characterization of vanillyl-alcohol oxidase from Byssochlamys fulva V107.
abstract: 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.
authors.affiliation: Department of Biological Function and Genetic Resources Science, Okayama University, Tsushima-Naka, Okayama 700-8530, Japan.
authors.forename: H
authors.initials: H
authors.lastname: Furukawa
authors.forename: M
authors.initials: M
authors.lastname: Wieser
authors.forename: H
authors.initials: H
authors.lastname: Morita
authors.forename: T
authors.initials: T
authors.lastname: Sugio
authors.forename: T
authors.initials: T
authors.lastname: Nagasawa