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Immobilization of Pleurotus eryngii Laccase via a Protein–Inorganic Hybrid for Efficient Degradation of Bisphenol A as a Potent Xenobiotic
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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.
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This review examines how laccase enzymes, naturally produced by fungi and other organisms, can be used as eco-friendly biocatalysts for breaking down environmental pollutants. Researchers highlight advances in enzyme immobilization and nanotechnology that have improved laccase stability and reusability for treating dyes, pesticides, pharmaceuticals, and microplastic additives. The study explores hybrid systems that combine laccase with other treatment technologies to achieve more complete pollutant breakdown.
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This review evaluates the potential of laccase enzymes, primarily from fungi and bacteria, to break down micropollutants in wastewater including pharmaceuticals, pesticides, and endocrine-disrupting compounds. Researchers found that laccase-based treatments offer an environmentally friendly alternative to conventional chemical methods for removing these contaminants. The study also discusses how immobilizing laccases on support materials can improve their stability and reusability in water treatment systems.
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Researchers investigated whether polyethylene microplastics affect the ability of the enzyme laccase to remove bisphenol A from wastewater. PE microplastics enhanced laccase activity by 96%, with the plastic surface enabling greater enzyme-substrate contact and improved BPA adsorption, suggesting microplastics could inadvertently improve some enzymatic treatment processes.
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This study tested the ability of laccase enzyme from the fungus Pycnoporus sanguineus to bioremediate bisphenol A (BPA) from water, measuring degradation rates and breakdown products. The enzyme achieved significant BPA removal under optimized conditions, offering a biological treatment approach.
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