摘要：Graphical abstractDisplay OmittedAbstractAn extracellular lipase partially purified fromBacillus thermoamylovoransBHK67 was effectively immobilized onto modified magnetic MgFe2O4nanoparticles (NPs). NPs were prepared by the sol-gel auto-combustion method and characterized by Fourier transform infrared (FTIR) spectroscopy, X-ray diffraction (XRD), Ultra-Violet–Visible Spectroscopy (UV–vis) and atomic force microscopy (AFM). Protein loading reached a saturated amount of about 0.20mg lipase per milligram of MgFe2O4NPs with 78.9% binding efficiency. The NPs-bound lipase also showed stability following exposure ton-propanol andiso-propanol or FeCl2and MgCl2metal ions at (1mM) at 55°C. NPs-bound lipase also retained 50% of its original hydrolytic activity even after 8thcycle, as well as after 12h of incubation at 55°C. NPs-bound lipase in an esterification reaction ofn-propanol and gallic acid (25mM) performed for 12h at 55°C producedn-propyl gallate with a conversion rate of 82%. Synthesizedn-propyl gallate possessed strong antioxidant activity, which was confirmed by DPPH assay, and in addition has anticancerous activity which was tested on a human L132 cell line.
