Enzymes are biocatalysts crucial for accelerating chemical reactions under mild conditions, thus finding widespread applications across various industries. Laccases, belonging to the multicopper oxidase family, are notable for their ability to catalyze the oxidation of diverse substrates using molecular oxygen as the electron acceptor. Their enzymatic activity, governed by four copper atoms at the active site, facilitates the conversion of phenolic compounds and environmental pollutants into less harmful forms, making them invaluable in green chemistry initiatives. Despite their potential, free laccases suffer from operational limitations such as poor stability and difficulty in reuse. Immobilization techniques, particularly covalent binding and physical adsorption, offer solutions by enhancing enzyme stability, facilitating recovery, and enabling their reuse in industrial processes. Covalent binding involves the formation of stable bonds between laccases and supports like silica or carbon nanotubes, improving enzyme resilience to harsh conditions and maintaining catalytic efficiency. Physical adsorption, on the other hand, utilizes reversible interactions to bind enzymes to surfaces like kaolinite or diatomite, offering simplicity and cost-effectiveness in industrial applications. Both methods show promise in overcoming the challenges associated with free laccase use, with recent advancements focusing on optimizing support materials and immobilization techniques to enhance enzyme performance in bioremediation, biosensor development, and pharmaceutical applications. This article highlights the versatility and potential of immobilized laccases in addressing environmental challenges and advancing sustainable industrial processes.