Next-generation bioremediation: Molecular decoding of fungal laccases for efficient degradation of bisphenol a and...

Bisphenol A (BPA) and its derivatives are pervasive environmental pollutants and known to be toxic and antiandrogenic endocrine disruptors. Despite global regulatory efforts, the environmental persistence and bioaccumulation potential of BPA and its derivatives, remain critical challenges. This study aims to characterize the atomic-level interactions between bisphenol derivatives and Laccase (Lac) enzymes from various white-rot fungal species, by utilizing advanced computational approaches. Therefore, molecular docking and molecular dynamics simulation were performed by AutoDock Vina and GROMACS software, respectively. The molecular docking results indicated that Lac from Botrytis aclada exhibited the highest binding affinities for bisphenol A (BPA, -7.8 kcal/mol) and bisphenol S (BPS, -7.7 kcal/mol), while Lac from Trametes hirsuta showed an exceptional affinity for bisphenol AF (BPAF, -8.5 kcal/mol). Additionally, Lac from Rigidoporus microporus demonstrated strong binding with bisphenol E (BPE, -8.1 kcal/mol) and bisphenol F (BPF, -7.8 kcal/mol). Molecular dynamics simulations confirmed the stability of these complexes over 100 ns, with RMSD values below 0.45 nm and binding free energies ranging from -21.83 to -3.24 kJ/mol. These findings provide critical insights into the enzymatic degradation of bisphenol derivatives, establishing a robust framework for next-generation bioremediation strategies. However, further investigation through in vitro assessments is necessary to confirm these results.