AN EXTRACELLULAR ARYL-ALCOHOL OXIDASE FROM THE WHITE-ROT FUNGUS BJERKANDERA-ADUSTA

The production of an extracellular aryl-alcohol oxidase from the white-rot fungus Bjerkandera adusta was studied in carbon- and nitrogen-limitation. The purified oxidase consisted of two enzymic forms. Their molecular weights were 78,000 and the pIs 4.25 and 4.35. The enzyme oxidized several aromatic alcohols to the corresponding aldehydes, reducing simultaneously oxygen to hydrogen peroxide. KM for anis alcohol (4-methoxybenzyl alcohol) was 0.24 mm and for veratryl alcohol (3,4-dimethoxybenzyl alcohol) 1.5 mm. Of the tested aryl-alcohols the highest oxidation rate was obtained with anis alcohol. Ethanol, methanol, and different sugars such as glucose were not oxidized by the enzyme. The pH optimum of the enzyme was 5.7. At this pH the enzyme was stable for weeks at 4°C. The aryl-alcohol oxidase contained FAD as a prosthetic group. © 1990.