Enzymatic activities of an extracellular, manganese-dependent peroxidase from Phanerochaete chrysosporium

TLDR: An extracellular peroxidase was purified by chromatofocusing column chromatography from the growth medium of ligninolytic cultures of the white-rot fungus Phanerochaete chrysosporium Burds BKM-1767 and produced hydrogen peroxide, which could be used as a co-substrate by ligninases such as those that oxidize veratryl alcohol, or by the peroxids itself to oxidize lign

Abstract: An extracellular peroxidase was purified by chromatofocusing column chromatography from the growth medium of ligninolytic cultures of the white-rot fungus Phanerochaete chrysosporium Burds BKM-1767 The enzyme was electrophoretically pure with an Mr of 45 000–47 000 It contained an easily dissociable heme, and required Mn2+ ions for activity In the presence of hydrogen peroxide and Mn2+ it oxidized compounds such as vanillylacetone, 2,6-dimethyloxyphenol, curcumin, syringic acid, guaiacol, syringaldazine, divanillylacetone, and coniferyl alcohol It did not oxidize veratryl alcohol In reactions requiring Mn2+ and O2, but not hydrogen peroxide, the enzyme oxidized glutathione, dithiothreitol, and NADPH with production of hydrogen peroxide The hydrogen peroxide produced could be used as a co-substrate by ligninases such as those that oxidize veratryl alcohol, or by the peroxidase itself to oxidize lignin model compounds