Bioremediation

Industrial wastes, agricultural (biocides) residues, and municipal discharges leave numerous pollutants, xenobiotics, and other hazardous chemicals in the environment. Active research is conducted to evaluate the ability of laccases to oxidatively detoxify or degrade these compounds, such as bisphenol A or 2,4-dichlorophenol (endocrine-disrupting or estrogenic), cyprodinil (fungicide), chlorinated phenol or a-naphthanol (pesticide leftover), and various aromatics [65a, 66-72].

The laccase catalysis could result in either degradation, polymerization, or immobilization of the target molecules [1, 2, 5, 6, 9, 48]. For instance, laccases may dehalogenate or oligomerize chlorophenols to reduce their toxicity. Laccases may also polymerize xenobiotics as such or copolymerize them with other substances (for example, humic acid) to facilitate molecular mass-based removals such as adsorption, sedimentation, or filtration.

Laccases have also been studied for degrading sulfur-containing coal substances, for potential applications in coal biodesulfurization/upgrading, bioreme-diation around coal mines, and emission reduction of acid rain-causing agents from power plants [4, 8].

To commercialize such bioremediations, many technical hurdles need to be overcome. Among them, immobilizing laccase on a solid or gel carrier seems to be a prerequisite, considering the needs of using the enzyme in numerous cycles (to reduce cost) and/or in heterogeneous multi-phase systems (to enhance the contact between the water-soluble enzyme and insoluble substrates).

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