Open AccessProduction and properties of an extracellular peroxidase from Coriolus versicolor which catalyses C α ‐C β cleavage in a lignin model compound
Author(s) -
Dodson Paul J.,
Evans Christine S.,
Harvey Pat J.,
Palmer John M.
Publication year - 1987
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1987.tb02292.x
Subject(s) - chemistry , peroxidase , lignin peroxidase , lignin , coomassie brilliant blue , polyacrylamide gel electrophoresis , enzyme , gel electrophoresis , extracellular , organic chemistry , reagent , biochemistry , chromatography , biology , staining , genetics
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 non‐oxygenated 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 H 2 O 2 . Its spectral characteristics showed it to be a haemcontaining protein, and sodium dodecyl sulphate‐polyacrylamide 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 characterised from cultures of another white‐rot basidiomycete, namely Coriolus versicolor .