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Abstract
Laccases occur widely in fungi; they have been characterized less frequently in higher
plants. Here we have focused on more recent reports on the occurrence of laccase and
its functions in physiological development and industrial utility. The reports of
molecular weights, pH optima, and substrate specificity are extremely diverse. Conclusive
proof of the occurrence of laccase in a tissue must demonstrate that the enzyme be
able to oxidize quinol with concomitant uptake of oxygen. Laccase is involved in the
pigmentation process of fungal spores, the regeneration of tobacco protoplasts, as
fungal virulence factors, and in lignification of cell walls and delignification during
white rot of wood. Commercially, laccases have been used to delignify woody tissues,
produce ethanol, and to distinguish between morphine and codeine. A very wide variety
of bioremediation processes employ laccase in order to protect the environment from
damage caused by industrial effluents. Research in recent years has been intense,
much of it elicited by the wide diversity of laccases, their utility and their very
interesting enzymology.