Journal
ARCHIVES OF MICROBIOLOGY
Volume 192, Issue 11, Pages 883-892Publisher
SPRINGER
DOI: 10.1007/s00203-010-0616-2
Keywords
Laccase; Phanerochaete flavido-alba; Olive oil wastewater; Multicopper oxidase
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The fungus Phanerochaete flavido-alba is highly efficient in the oxidation of olive oil wastewater-derived polyphenols. This capability is largely due to the action of a multicopper-oxidase (MCO), encoded by the pfaL gene. We describe the sequence and organization of pfaL gene and the biochemical characterization and predicted 3D structural model of the encoded protein. pfaL gene organization and peptide sequence are highly similar to those of P. chrysosporium MCOs. However, PfaL is the first MCO in the Phanerochaete genus to show evident laccase activity. Phylogenetic analysis places PfaL in a differentiated sub-branch of ferroxidases. Protein structure analysis reveals close similarity of PfaL and ferroxidases and provides clues about the differences of activity between both types of enzymes. To summarize, P. flavido-alba laccase is the first enzyme in the novel and biochemically poorly defined group of ferroxidases/laccases that shows efficacious oxidation of laccase substrates, biotechnologically exploitable in bioremediation approaches.
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