Abstract
Laccase (Benzenediol: oxygen oxidoreductase; E.C.1.10.3.2), a multicopper oxidase that is
a known lignin-degrading enzyme, can catalyse an ample array of substrates, from phenolic, nonphenolic
compounds, aromatic amines, diamines, heterocyclic compounds to organic/inorganic metal
compounds, etc., bestowed they have not too high redox potentials. Despite many laccase-producing
organisms like bacteria, insects, plants, and animals, white rot filamentous fungi are the best producers
of this enzyme. In the presence of laccase, pesticides (fungicides, herbicides, insecticides, etc.) of various
chemical compositions (organophosphates, organochlorines, carbamates, pyrethrin & pyrethroids,
etc.) are oxidized into the water with collateral reduction of four electrons of molecular oxygen with
various efficiencies. Bioremediation efficiency can be increased in the presence of various natural or
synthetic mediators, viz. ABTS, violuric acid, 1- hydroxy benzotriazole, vanillin, syringaldehyde, PEG,
etc. Immobilized laccase on various supporting materials increased the enzyme's stability, reliability,
and reusability for continuous application, particularly for industrial processes. The present review
discusses the structure, catalytic cycle, general mechanism of oxidation, and various scopes and challenges
of pesticide degradation by this multifaceted biocatalyst which could lead to a green sustainable
environment.
Graphical Abstract
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