Laccase-based biocatalytic systems application in sustainable degradation of pharmaceutically active contaminants.

The outflow of pharmaceutically active chemicals (PhACs) exerts a negative impact on biological systems even at extremely low concentrations. For instance, enormous threats to human and aquatic species have resulted from the widespread use of antibiotics in ecosystems, which stimulate the emergence and formation of antibiotic-resistant bacterial species and associated genes. Additionally, it is challenging to eliminate these PhACs by employing conventional physicochemical water treatment techniques. Enzymatic approaches, including laccase, have been identified as a promising alternative to eliminate a broad array of PhACs from water matrices. However, their application in environmental bioremediation is hindered by several factors, including the enzyme's stability and its location in the aqueous environment. Such obstacles may be surmounted by employing laccase immobilization, which enables enhanced stability (including inactivation caused by the substrate), and thus improved catalysis. This review emphasizes the potential hazards of PhACs to aquatic organisms within the detection concentration range of ngL-1 to µgL-1, as well as the deployment of laccase-based multifunctional biocatalytic systems for the environmentally friendly mitigation of anticancer drugs, analgesics/NSAIDs, antibiotics, antiepileptic agents, and beta blockers as micropollutants. This approach could reduce the underlying toxicological consequences. In addition, current developments, potential applications, and viewpoints have focused on computer-assisted investigations of laccase-PhACs binding at enzyme cavities and degradability prediction.