OXIDATION REACTIONS CATALYZED BY MANGANESE PEROXIDASE ISOENZYMES FROM CERIPORIOPSIS-SUBVERMISPORA
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Date
1995
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ELSEVIER SCIENCE BV
Abstract
A total of 11 manganese peroxidase isoenzymes (MnP1-MnP11) with isoelectric points (pIs) in the range of 4.58-3.20 were isolated from liquid- and solid-state cultures of the basidiomycete Ceriporiopsis subvermispora. In the presence of hydrogen peroxide, these isoenzymes showed different requirements for Mn(II) in the oxidation of vanillylacetone, o-dianisidine, p-anisidine and ABTS, whereas oxidation of guaiacol by any isoenzyme did not take place when this metal was omitted, K-m values for o-dianisidine and p-anisidine in the absence of Mn(II) are in the range of 0.5-1.0 mM and 4.5-42.0 mM, respectively, Oxalate and citrate, but not tartrate, accelerate the oxidation of o-dianisidine, both in the presence and in the absence of Mn(II). MnPs from this fungus are able to oxidize kojic acid without externally added hydrogen peroxide, indicating that they can also act as oxidases. In this reaction, however, the requirement for Mn(II) is absolute.
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Keywords
LIGNIN DEGRADATION, BASIDIOMYCETE, PEROXIDASE, MANGANESE, ENZYMATIC OXIDATION, BASIDIOMYCETE PHANEROCHAETE-CHRYSOSPORIUM, LIGNIN PEROXIDASE, MN-PEROXIDASE, GLYOXAL OXIDASE, BIODEGRADATION, ENZYME