Oxidation of Chlorpromazine by Lipoxygenase Immobilized on Magnetic Fe3O4 Nanoparticles.

In this work, soybean lipoxygenase enzyme was immobilized on the magnetic Fe3O4 nanoparticles to oxidate chlorpromazine (CPZ). The physicochemical properties of the nanoparticles were characterized with transmission electronic microscopy (TEM), fourier transform infrared spectroscopy (FTIR), X-ray diffraction (XRD) and thermal gravimetric analysis (TGA), and the magnetic properties were detected by a vibrating sample magnetometer (VSM). The TEM images indicated the surface and the size of the immobilized enzyme were much rougher and thicker than those of the naked particles. The analyses of XRD patterns showed that the structure of the magnetic nanoparticles had no significant change while the nanoparticles also exhibited higher superparamagnetism at room temperature. Compared to free enzyme or the enzyme immobilized with other methods, the optimal pH, temperature and H2O2 concentration for the activity of immobilized enzyme did not have great changes, but the immobilized enzyme was more stable and less sensitive to the change of the influence factors than free counterpart. The immobilized enzyme could be recovered easily by magnetic separation and could be reused for many times in the process of CPZ oxidation. The results obtained by simulating the model of Michaelis-Menten indicated that the reaction of CPZ oxidation followed Michaelis-Menten kinetics and the enzyme still retained its affinity for CPZ while the enzyme was immobilized.