PRODUCTION OF HYDROGEN-PEROXIDE BY ARYL-ALCOHOL OXIDASE FROM THE LIGNINOLYTIC FUNGUS PLEUROTUS-ERYNGII

Production of extracellular hydrogen peroxide by fungal oxidases is been investigated as a requirement for lignin degradation. Aryl-alcohol oxidase activity is described in extracellular liquid and mycelium of Pleurotus eryngii and studied under non-limiting nitrogen conditions. This aryl-alcohol oxidase catalyses conversion of primary aromatic alcohols to the corresponding aldehydes and H2O2, showing no activity with aliphatic and secondary aromatic alcohols. The enzyme is stable at pH 4.0-9.0, has maximal activity at 45°-50°C and pH 6.0-6.5, is inhibited by Ag+, Pb2+ and NaN3, and has a Km of 1.2 m M using veratryl alcohol as substrate. A single protein band with aryl-alcohol oxidase activity was found in zymograms of extracellular and intracellular crude enzyme preparations from P. eryngii. © 1990 Springer-Verlag.