Different fungal manganese-oxidizing peroxidases: a comparison between Bjerkandera sp. and Phanerochaete chrysosporium.
Two manganese-oxidizing peroxidases differing in glycosylation degree were purified from fermenter cultures of Bjerkandera sp. They were characterized and compared with the three manganese-oxidizing peroxidase isoenzymes obtained from the well-known ligninolytic fungus Phanerochaete chrysosporium. All the enzymes showed similar molecular masses but those from P. chrysosporium had less acidic isoelectric point. Moreover, the latter strictly required Mn2+ to oxidize phenolic substrates whereas the Bjerkandera peroxidases had both Mn-mediated and Mn-independent activity on phenolic and non-phenolic aromatic substrates. Taking into account these results, and those reported for Bjerkandera adusta and different Pleurotus species, we concluded that two different types of Mn(2+)-oxidizing peroxidases are secreted by ligninolytic fungi.
Palma
C
C
Department of Chemical Engineering, University of Santiago de Compostela, Spain.
Martínez
A T
AT
Lema
J M
JM
Martínez
M J
MJ
D000595:Amino Acid Sequence; D002384:Catalysis; D006031:Glycosylation; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism*; D008345:Manganese / Q000494:pharmacology*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry / Q000378:metabolism*; D020075:Phanerochaete / Q000201:enzymology*; D011124:Polyporaceae / Q000201:enzymology*
D007527:Isoenzymes; D008345:Manganese; D010544:Peroxidases