NH2-Fe3O4@SiO2 supported peroxidase catalyzed H2O2 for degradation of endocrine disrupter from aqueous solution: Roles of active radicals and NOMs

In this work, magnetic Fe3O4 was utilized to immobilize horseradish peroxidase (IM-HRP) in order to improve its stability and reusability by crosslinking method process with glutaraldehyde. The physicochemical properties of NH2-Fe3O4@SiO2 and IM-HRP were characterized by powder X-ray diffraction (XRD), Fourier transform infrared spectroscopy (FT-IR), Thermo-gravimetric Analysis (TGA) and Transmission electron microscopy (TEM). The thermal stability of immobilized-HRP was considerably improved in comparison with free counterpart. The catalytic performance of IM-HRP for estrogens removal from aqueous solution was evaluated, it was found that the presence of natural organic matters (NOM) have no significant effects on E2 removal and the E2 enzyme-degradation reached around 80% when pH = 7.0 with 0.552 x 10(-3) ratio of IM-HRP/H2O2, In addition, the active radicals responsible for estrogens degradation were identified with electro-spin resonance spectra (ESR). It was found that immobilization process on Fe3O4 showed no adverse effects on catalytic performance on HRP, estrogens degradation could be fitted well with pseudo second kinetic equation. Estrogens degradation efficiency was reduced in the presence of humic substances. Both center dot O-2(-) and center dot OH were detected in IM-HRP catalyzed H2O2 system and radicals quenching test indicated center dot O-2(-) played a more important role in estrogens removal. IM-HRP exhibited excellent stability and E2 removal efficiency could reach 45.41% after use seven times. Therefore, HRP enzymes immobilized on NH2-Fe3O4@SiO2 by cross-linking method in glutaraldehyde solutions was an effective way to improve stability and reusability of HRP, and which could avoid potential secondary pollution in water environment caused by free HRP after treatment. (C) 2017 Elsevier Ltd. All rights reserved