Efficient Diclofenac Removal by Enzymatic Biocatalysis with Heat-Resistant Laccase Induced in Curvularia kusanoi L7 Cultures Through Biological Interactions with Trichoderma pleuroticola

The improper disposal of toxic drugs can cause significant damage to the environment. Various methods have been used for these purposes, with enzymatic catalysis being one of the most innovative, despite the drawback that enzymes may become denatured or lose activity depending on the temperature. The present research aimed to evaluate the catalytic capacity of purified heat-resistant laccase from Curvularia kusanoi L7 in the removal of diclofenac. The heat-resistant enzyme was obtained in Curvularia kusanoi L7 induced by biological interactions with Trichoderma pleuroticola, purified by three-phase partition and characterized their thermal stability and heat resistance. The degradative activity was evaluated on diclofenac sodium (0.5, 0.3, 0.1 mg/ml) by UV-VIS scanning and HPLC. Yields of over 80% and high purification factor where obtained. The induction process significantly increases the temperature range in which the enzyme reaches optimal activity, moving from 30-40°C to 60-70 °C (induced enzyme), increasing its stability and heat resistance at 80 °C. Diclofenac removal determined by both analytical methods showed over 95% degradation of this drug. It can be concluded that purified heat-resistant laccase from Curvularia kusanoi L7 allows an exhaustive degradation of diclofenac, making this enzymatic treatment a safe option to scale up in drug degradation processes.