Purification and characterization of vanillyl-alcohol oxidase from Byssochlamys fulva V107

Vanillyl-alcohol oxidase from Byssochlamys fulva V107 was purified to appar ent 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 th e conversion of 4-hydroxybenzylalcohols such as vanillyl alcohol to the cor responding aldehydes, eugenol to coniferyl alcohol, and Li-alkylphenols to 1-(4-hydroxyphenyl)alcohols. The latter reaction was S-stereospecific and w as used for the synthesis of S-1-(4-hydroxyphenyl)ethanol and -propanol wit h enantiomeric excesses of 81.9 and 86.0%, respectively. The catalytic and structural similarities to a Penicillium vanillyl-alcohol oxidase and Pseud omonas 4-alkylphenol methylhydroxylases are discussed.