Enhancing enzyme efficiency: Immobilization techniques for fungal laccases in bioremediation

Enzymes are biocatalysts crucial for acceleratingchemical reactions under mild conditions, thusfinding widespread applications across variousindustries. Laccases, belonging to the multicopperoxidase family, are notable for their ability tocatalyze the oxidation of diverse substrates usingmolecular oxygen as the electron acceptor. Theirenzymatic activity, governed by four copper atomsat the active site, facilitates the conversion ofphenolic compounds and environmental pollutantsinto less harmful forms, making them invaluablein green chemistry initiatives. Despite their potential,free laccases suffer from operational limitationssuch as poor stability and difficulty in reuse.Immobilization techniques, particularly covalentbinding and physical adsorption, offer solutionsby enhancing enzyme stability, facilitating recovery,and enabling their reuse in industrial processes.Covalent binding involves the formation of stablebonds between laccases and supports like silica orcarbon nanotubes, improving enzyme resilience toharsh conditions and maintaining catalyticefficiency. Physical adsorption, on the other hand,utilizes reversible interactions to bind enzymes tosurfaces like kaolinite or diatomite, offeringsimplicity and cost-effectiveness in industrialapplications. Both methods show promise inovercoming the challenges associated with freelaccase use, with recent advancements focusingon optimizing support materials and immobilizationtechniques to enhance enzyme performance inbioremediation, biosensor development, andpharmaceutical applications. This article highlightsthe versatility and potential of immobilizedlaccases in addressing environmental challengesand advancing sustainable industrial processes.