Production and properties of an extracellular peroxidase from<i>Coriolus versicolor</i>which catalyses C_α-C_βcleavage in a lignin model compound

Abstract

An extracellular peroxidase capable of degrading a lignin-model compound has been isolated from cultures of Coriolus versicolor, a white-rot basidiomycete. The enzyme was produced in nonoxygenated stationary cultures under conditions of carbon limitation with the addition of veratryl alcohol as an inducer. The enzyme was separated and shown to have veratryl alcohol oxidase activity, and to be capable of oxidation of a wide range of aromatic substrates in the presence of H202. Its spectral characteristics showed it to be a haemcontaining protein, and sodium dodecyl sulphatepolyacrylamide gel electrophoresis (SDS-PAGE) stained with Coomassie blue or by periodic acid-Schiff's reagent showed it to be a glycosylated protein of 50 kDa. This is the first demonstration that a peroxidase similar to the lignin peroxidase isolated from Phanerochaete chrysosporium has been char-