Catalytic function of the laccase enzyme in response to chlorpyrifos and 2,4-dichlorophenoxyacetic acid: behavior in controlled and simulated environments.

Enzymes secreted by white-rot fungi, such as laccase, offer a promising solution for treating xenobiotic compounds dangerous to the environment and human health. This study aimed to perform a comprehensive analysis of the tolerance of Pleurotus pulmonarius LBM 105 and its laccase activity toward the pesticides 2,4-D and chlorpyrifos both in vitro and in silico. The fungal strain was able to grow in different concentrations of the pesticides, showing evident morphological alterations. Laccase activity and a 53 kDa electromorph were present in all treatments, showing significant stability with peak activity achieved at a pH of 5.6 and within a temperature range of 50-60 °C. Three laccase genes were mapped, annotated, and characterized from the genome. PplacI obtained better structural validation and affinity energy of - 5.05 and - 7.65 kcal mol with 2,4-D and chlorpyrifos, respectively. The Molecular Mechanics/Poisson-Boltzmann Surface Area analysis at 250 ns confirmed the docking results, revealing the existence of stronger hydrophobic interactions between laccase and chlorpyrifos and highlighting the importance of the Phe341 residue in stabilizing both complexes. Understanding the impact of pesticides on laccase's catalytic function is key to formulating and applying future biotechnological strategies with this enzyme.