In silico analysis of laccases as candidate enzymes for PFAS bioremediation in a multienzymatic system

Per- and polyfluorinated alkyl substances (PFAS) are a class of synthetic chemicals that are widely used in many different industrial sectors due to their properties as waterproofing agents and surfactants. In recent years, they have emerged as environmental contaminants because of their high resistance to biodegradation, their ubiquitous presence in the environment and their propensity to bioaccumulation. The chemical and physical techniques currently used for their degradation are highly energy consuming and expensive, making bioremediation one of the most promising treatments for PFAS breakdown. This work proposes an in silico approach to evaluate potential enzymatic candidates for PFAS degradation from the laccase family proteins, which are widely used in bioremediation projects thanks to their broad range catalytic capacities. At present, there is no known single enzyme approach that has been demonstrated to be effective. Consequently, this work explores the potential of employing the combined activity of at least two enzymes. The bioinformatics techniques that will be treated comprehend the search for orthologous enzymes using alignment tools, the investigation of functional domains and the analysis of docking simulations employed to predict how PFAS molecules might bind to the active sites of laccases.