title: Mn-peroxidase from Bjerkandera adusta 90-41. Purification and substrate specificity.
abstract: Mn-peroxidase has been purified to homogeneity from culture liquid of white-rot fungus Bjerkandera adusta 90-41 grown on medium containing lignosulfonates. According to the data on SDS-PAGE and isoelectrofocusing, the molecular mass of the enzyme is 43 kD and the isoelectric point is 3.5. The pH-optimum in the reaction of MnSO4 oxidation is 4.5. The substrate specificity of the enzyme has been studied. In contrast to previously known Mn-peroxidases from B. adusta, the isolated enzyme has no activity with veratryl alcohol. The enzyme can oxidize ammonium 2, 2-azino-bis(ethyl-6-benzothiazoline sulfonate) (ABTS), o-phenylenediamine, and phenol red in the absence of Mn2+. Oxidation of ABTS and o-phenylenediamine is stimulated by Mn2+, whereas in the reaction of oxidation of phenol red Mn2+ acts as an inhibitor. Some aromatic substrates, such as pyrocatechol and guaiacol, are oxidized only in the presence of Mn2+.
authors.affiliation: Department of Mycology and Algology, School of Biology, Lomonosov Moscow State University, Moscow, 119899, Russia. kdz@enzyme.chem.msu.ru
authors.forename: E I
authors.initials: EI
authors.lastname: Dzedzyulya
authors.forename: E G
authors.initials: EG
authors.lastname: Becker
mesh_terms: D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D010544:Peroxidases / Q000302:isolation & purification* / Q000378:metabolism; D011124:Polyporaceae / Q000201:enzymology*
chemical_list: D010544:Peroxidases; C051129:manganese peroxidase