Enzymatic activities of an extracellular, manganese-dependent peroxidase from Phanerochaete chrysosporium
Open Access
- 1 August 1985
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 29 (1-2) , 37-41
- https://doi.org/10.1016/0378-1097(85)90267-8
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.Keywords
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