A Review of Laccase Enzyme Research for Green Industry Applications (Review Article)

Author(s): Jisha Pulikkottil John*, A Robert Antony, and Emmanuel Simon

Abstract: Laccase is an important category of multicopper oxidases that facilitate the oxidation of diverse aromatic and non-aromatic substances while simultaneously reducing molecular oxygen to water. This review investigates the potential of laccase as a sustainable biocatalyst for different bioremediation purposes. The laccase molecular structure showcases a unique configuration of copper atoms categorized into three types (T1, T2, and T3), which create the catalytic core vital for electron transfer during oxidation processes. The microbial production of laccase has attracted significant interest due to the benefits of regulated cultivation environments, the ability to manipulate genes, and greater enzyme yields compared to plant-derived sources. A variety of natural and synthetic mediators have been discovered, which broaden the applicability of laccases in industrial applications. Bacterial laccases exhibit considerable adaptability in their use for environmental purposes. In the textile sector, they aid in the breakdown of dyes and the decolorization of wastewater without producing harmful byproducts. In the pulp and paper industry, laccases provide environmentally friendly substitutes for traditional chlorine-based bleaching methods. Furthermore, these enzymes can effectively break down a range of environmental pollutants, such as phenolic compounds, polycyclic aromatic hydrocarbons, and pharmaceutical waste. Recent developments have utilized laccase in the creation of biosensors that can identify phenolic compounds, pesticides, and environmental toxins, as well as in the development of biofuel cells for renewable energy generation. This review highlights the promise of laccase as a green catalyst that supports sustainable development objectives by presenting eco-friendly alternatives to traditional chemical methods in various industrial and environmental contexts.

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