Revolutionizing the potential of laccase from Bacillus paralicheniformis as an eco-friendly solution to reduce polychlorinated dibenzofurans contamination through integrated computational approach

Abstract

Several risks to ecosystems and human health are increasing day by day and among them, Polychlorinated dibenzofurans (PCDFs) are persistent environmental pollutants which pose significant risks because of its resistance, bioaccumulation, and toxicity. Their effective degradation remains a pressing challenge for sustainable environmental remediation. This study investigates the potential of the laccase enzyme from Bacillus paralicheniformis as an eco-friendly solution to reduce PCDF contamination. The enzyme’s structural and functional properties were analyzed using advanced computational tools such as Discovery Studio, Prankweb, and MetaCyc, which identified key binding sites and metabolic pathways involved in aromatic compound degradation. Toxicity assessments using ToxinPred and Toxtree confirmed the non-toxic nature of laccase and the systemic toxicity of PCDFs. Molecular docking studies showed high binding affinities between laccase and PCDFs, particularly 1,2,3,4,7,8-Hexachlorodibenzofuran and 1,2,3,7,8-Pentachlorodibenzofuran, with binding energies of −7.3 and −7.2 kcal/mol, respectively. Interaction analyses highlighted PRO A:433, HIS B:431, and LYS B:466 residues involved in the stabilization of the enzyme–substrate complex. Molecular dynamics simulations for 100 ns further indicated the stability of the docked complex. These findings demonstrate the laccase enzyme’s potential as a safe and effective tool for bioremediation, providing a foundation for eco-friendly strategies to mitigate PCDF contamination.