Laccase Immobilization on Copper-Magnetic Nanoparticles for Efficient Bisphenol Degradation

Laccase activity is influenced by copper (Cu) as an inducer. In this study, laccase was immobilized on Cu and Cu-magnetic (Cu/Fe(2)O(4)) nanoparticles (NPs) to improve enzyme stability and potential applications. The Cu/Fe(2)O(4) NPs functionally activated by 3-aminopropyltriethoxysilane and glutaraldehyde exhibited an immobilization yield and relative activity (RA) of 93.1 and 140%, respectively. Under optimized conditions, Cu/Fe(2)O(4) NPs showed high loading of laccase up to 285 mg/g of support and maximum RA of 140% at a pH 5.0 after 24 h of incubation (4°C). Immobilized laccase, as Cu/Fe(2)O(4)-laccase, had a higher optimum pH (4.0) and temperature (45°C) than those of a free enzyme. The pH and temperature profiles were significantly improved through immobilization. Cu/Fe(2)O(4)-laccase exhibited 25-fold higher thermal stability at 65°C and retained residual activity of 91.8% after 10 cycles of reuse. The degradation of bisphenols was 3.9-fold higher with Cu/Fe(2)O(4)-laccase than that with the free enzyme. To the best of our knowledge, Rhus vernicifera laccase immobilization on Cu or Cu/Fe(2)O(4) NPs has not yet been reported. This investigation revealed that laccase immobilization on Cu/Fe(2)O(4) NPs is desirable for efficient enzyme loading and high relative activity, with remarkable bisphenol A degradation potential.