Lignin peroxidase from fungi: Phanerochaete chrysosporium

Lignin peroxidase of Phanerochaete chrysosporium can be produced and purified relatively easily. Described here is production and separation of six isoenzymes, using a commonly studied wild-type strain. The fungus is grown on a chemically defined nitrogen-limiting medium in stationary or agitated flasks, the extracellular broth containing the lignin peroxidases is concentrated, and the isoenzymes are separated and purified by anionexchange chromatography. The isoenzymes have similar physical and catalytic properties but somewhat different kinetic properties. They are encoded at least in part by different structural genes. Lignin peroxidascs, in the presence of H₂O₂, oxidize their aromatic substrates by one electron to cation radicals, which undergo diverse reactions of ionic and radical nature. Purification and characterization of lignin peroxidases from other lignin-degrading fungi have also been reported.