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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