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

Andrzej Paszczyński, Van-Ba Huynh, Ronald Crawford
DOI: http://dx.doi.org/10.1111/j.1574-6968.1985.tb00831.x 37-41 First published online: 1 August 1985


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.

  • Lignin biodegradation
  • white-rot fungi
  • oxidase
  • peroxidase
  • thiol

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