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Immobilization of Pleurotus eryngii Laccase via a Protein–Inorganic Hybrid for Efficient Degradation of Bisphenol A as a Potent Xenobiotic
Summary
Laccase, an enzyme produced by the fungus Pleurotus eryngii, was immobilized onto a protein-inorganic hybrid support to improve its stability and reusability for plastic degradation. Immobilization protected the enzyme from denaturation and allowed it to retain activity across repeated degradation cycles. This system demonstrates a practical route toward enzyme-based plastic breakdown that could be scaled for bioremediation.
In the present investigation, an eco-friendly biocatalyst was developed using Pleurotus eryngii laccase (PeLac) through a copper (Cu)-based protein-inorganic hybrid system for the degradation of bisphenol A, a representative xenobiotic. After partial purification, the specific activity of crude PeLac was 92.6 U/mg of total protein. Immobilization of PeLac as Cu3(PO4)2-Lac (Cu-PeLac) nanoflowers (NFs) at 4 °C resulted in a relative activity 333% higher than that of the free enzyme. The Cu-PeLac NFs exhibited greater pH and temperature stability and enhanced catalytic activity compared to free laccase. This enhanced activity was validated through improved electrochemical properties. After immobilization, Cu-PeLac NFs retained up to 8.7-fold higher residual activity after storage at 4 °C for 30 days. Free and immobilized laccase degraded bisphenol A by 41.6% and 99.8%, respectively, after 2 h of incubation at 30 °C. After ten cycles, Cu-PeLac NFs retained 91.2% degradation efficiency. In the presence of potent laccase inhibitors, Cu-PeLac NFs exhibited a 47.3-fold improvement in bisphenol A degradation compared to free PeLac. Additionally, the synthesized Cu-PeLac NFs demonstrated lower acute toxicity against Vibrio fischeri than Cu nanoparticles. This study presents the first report of PeLac immobilization through an eco-friendly protein-inorganic hybrid system, with promising potential for degrading bisphenol A in the presence of inhibitors to support sustainable development.