Purification and characterization of peroxidases from the dye-decolorizing fungus Bjerkandera adusta

Abstract

A peroxidase oxidizing Mn2+ (MnP) is described for the first time in Bjerkandera adusta, a fungus efficiently degrading xenobiotic compounds. The MnP appeared as two isoenzymes, which were purified to homogeneity together with two lignin peroxidases (LiP). Their N-terminal sequences were identical, but the MnP isoenzymes showed more basic isoelectric points and differences in amino acid composition and catalytic properties. The B. adusta LiP is similar to LiP from Phanerochaete chrysoporium. However, the interest of the MnP described here is related to its ability to catalyze Mn(2+)-mediated as well as Mn(2+)-independent reactions on aromatic compounds, which may be of use for applications in biotechnology and environmental technology.