Laccase isoenzymes of Pleurotus eryngii: characterization, catalytic properties, and participation in activation of molecular oxygen and Mn2+ oxidation
Article Abstract:
Two laccase isoenzymes from the fungus Pleurotus eryngii were purified to electrophoretic homogeneity with an overall yield of 56.3%. Laccases I and II are monomeric glycoproteins with 7 and 1% content, molecular masses of 65 and 61 kDa, and pIs of 4.1 and 4.2, respectively. Findings showed that laccase in the presence of hydroquinones can participate in the production of both reduced oxygen species and manganic ions.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 1997
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Purification, characterization, and functional role of a novel extracellular protease from Pleurotus ostreatus
Article Abstract:
Researchers have isolated an extracellular serine protease from Pleurotus ostreatus that is structurally and kinetically unlike other proteases from the fungus and appears to regulate laccase activity. The properties of the enzyme are described.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2001
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Copper induction of laccase isoenzymes in the ligninolytic fungus Pleurotus ostreatus
Article Abstract:
Copper is the most potent inducer of laccase isoenzymes in Pleurotus ostreatus. These enzymes can oxidize many different substrates, including toxic phenols and azo dyes.
Publication Name: Applied and Environmental Microbiology
Subject: Biological sciences
ISSN: 0099-2240
Year: 2000
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