Bridging Simulation and Sustainability: Laccase Immobilization on Bio-Polymeric Hybrids for Degradation of...

We present the development and comprehensive characterization of a biocatalytic system comprising laccase immobilized on a polystyrene-chitosan (PS-chitosan) carrier. The material was synthesized using electrospinning, which enabled the formation of a porous structure with a large surface area, offering favorable properties. Laccase from Trametes versicolor was successfully immobilized on the PS-chitosan with a yield of 87% and an activity retention of 83%. The immobilization was assessed by means of Fourier transform infrared spectroscopy (FTIR), confocal laser scanning microscopy (CLSM), electrokinetic potential measurements, and scanning electron microscopy (SEM). Kinetic analyses and thermodynamic studies confirmed that immobilization favorably influenced the catalytic properties of the laccase. Molecular docking and molecular dynamics simulations enabled identification of the preferred sites for binding of the enzyme to the material, as well as visualization of the interaction between the immobilized enzyme and the estrogen 17α-ethinylestradiol (EE2) substrate. The system enabled the removal of EE2 from model samples and real wastewater, achieving removal efficiencies of 86% and 44%, respectively. Overall, the study provides new insight into the immobilization binding of laccase to a PS-chitosan support and confirms the bioremediation potential of laccase immobilized on PS-chitosan, paving the way for developing efficient biocatalytic systems.