Different fungal manganese-oxidizing peroxidases: a comparison between Bjerkandera sp. and Phanerochaete chrysosporium

• Published in: Journal of biotechnology Vol. 77; no. 2; pp. 235 - 245
• Main Authors: Palma, C., Martı́nez, A.T., Lema, J.M., Martı́nez, M.J.
• Format: Journal Article
• Language: English
• Published: Lausanne Elsevier B.V 17.02.2000; Amsterdam Elsevier; New York, NY
• Subjects: Amino Acid Sequence; aromatic compounds; Biological and medical sciences; Biology of microorganisms of confirmed or potential industrial interest; Biotechnology; Bjerkandera adusta; Bjerkandera sp; Catalysis; Catalyst activity; Catalytic properties; enzyme activity; Enzymes; Fermentation; Fundamental and applied biological sciences. Psychology; Fungi; Glycosylation; Isoenzymes - chemistry; Isoenzymes - metabolism; Manganese; Manganese - pharmacology; manganese-oxidizing peroxidase; manganese-oxidizing peroxidases; Miscellaneous; Mission oriented research; Mn-oxidizing peroxidases; Molecular Sequence Data; Oxidation; Oxidation-Reduction; Peroxidases - chemistry; Peroxidases - metabolism; Phanerochaete - enzymology; Phanerochaete chrysosporium; phenolic compounds; Plant cell culture; Polyporaceae - enzymology; Purification; Catalytic properties; Bjerkandera sp; Mn-oxidizing peroxidases; Phanerochaete chrysosporium; Purification; Enzyme; Manganese peroxidase; Basidiomycetes; Fungi; Peroxidases; Enzymatic activity; Oxidoreductases; Kinetic parameter; Comparative study; Physicochemical properties; Thallophyta
• ISSN: 0168-1656; 1873-4863
• DOI: 10.1016/S0168-1656(99)00218-7

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 Mn 2+ 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.