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

Abstract

Enzymes secreted by white-rot fungi, such as laccase, offer a promising solution for treating xenobiotic compounds dangerousto the environment and human health. This study aimed to perform a comprehensive analysis of the tolerance of Pleurotuspulmonarius LBM 105 and its laccase activity toward the pesticides 2,4-D and chlorpyrifos both in vitro and in silico. Thefungal 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 activityachieved at a pH of 5.6 and within a temperature range of 50–60 °C. Three laccase genes were mapped, annotated, and characterizedfrom the genome. PplacI obtained better structural validation and affinity energy of − 5.05 and − 7.65 kcal mol−1with 2,4-D and chlorpyrifos, respectively. The Molecular Mechanics/Poisson-Boltzmann Surface Area analysis at 250 nsconfirmed the docking results, revealing the existence of stronger hydrophobic interactions between laccase and chlorpyrifosand highlighting the importance of the Phe341 residue in stabilizing both complexes. Understanding the impact of pesticideson laccase’s catalytic function is key to formulating and applying future biotechnological strategies with this enzyme.