In Silico characterization of acylamidase from Actinoalloteichus hoggarensis: A promising biocatalyst for the bioremediation of persistent organic pollutants

Abstract

Widespread contamination by persistent organic micropollutants, particularly polycyclic aromatic hydrocarbons (PAHs) from petrochemical activities, poses risks to ecosystems and human health, necessitating sustainable remediation strategies. Enzymatic bioremediation offers a promising alternative, with amidases emerging as versatile catalysts. This study investigates the catalytic potential of an acylamidase from Actinoalloteichus hoggarensis , a thermotolerant and halotolerant actinobacterium isolated from the Algerian Sahara Desert, whose extremophilic origin suggests inherent stability for harsh conditions. Using a comprehensive in silico approach, the enzyme's structural and functional properties were characterized, and its interactions with 34 micropollutants were evaluated via molecular docking. A high-quality three-dimensional model was generated and validated. Conserved domain analysis classified the enzyme within the amidase signature family. Molecular docking revealed strong binding affinities across diverse contaminants. Among PAHs, benzo[ a ]pyrene exhibited the strongest affinity, followed by chrysene and anthracene. The enzyme also showed notable interactions with the plastic additive triphenyl phosphate, highlighting its substrate versatility. Molecular dynamics simulations confirmed the stability of enzyme-ligand complexes (RMSD < 0.35 nm) and provided insights into key binding residues. These results indicate that this acylamidase possesses structural determinants accommodating both PAHs and other organic micropollutants, providing a computational foundation for its application in enzymatic bioremediation.