Mechanistic insights into Bisphenol A biodegradation by laccase and versatile peroxidase: a computational perspective

Bisphenol A (BPA) is an endocrine disruptor. It is used to produce polycarbonate plastic and epoxy resins. It is a significant water contaminant that profoundly impacts ecosystems and human health, necessitating its removal from aquatic environments. Two oxidoreductases, Laccase and Versatile Peroxidase (VP) were selected to explore their potential for BPA degradation. Enzymatic degradation offers several advantages over microbial and chemical degradation, as it is substrate-specific, effective, and safe. It is effective and time saving to use computational methods to elucidate the interactions and stability of enzyme-xenobiotic complexes. In the current study, we employed molecular docking, MD simulations, binding free energy calculations, principal component analysis, free energy landscape, and DFT analysis approaches to investigate the possible non-covalent interactions and their life span. The study revealed that both Laccase and VP exhibit the ability to degrade BPA. Laccase exhibited minimal conformational changes upon BPA binding, while VP undergoes a noticeable opening to accommodate the pollutant. VP exhibited a higher affinity for BPA than Laccase, as evidenced by their respective binding energies. <i>In vitro</i> studies are warranted to validate the results. Further analysis indicated that amino acid residues such as Ala and Val were crucial in binding BPA to both enzymes. The outcomes can be used to engineer and design efficient enzymes to degrade BPA.