Abstract
To enhance the dye removal efficiency by natural enzyme, horseradish peroxidase (HRP) was immobilized onto amine-functionalized superparamagnetic iron oxide and used as a biocatalyst for the oxidative degradation of acid black-HC dye. The anchored enzyme was characterized by vibrating sample magnetometry, Fourier transform infrared spectroscopy, X-ray diffraction, thermogravimetry, scanning electron microscopy, Brunauer–Emmett–Teller and Barrett–Joyner–Halenda methods, nitrogen adsorption–desorption measurements, Zeta potential, energy dispersive X-ray spectroscopy, and transmission electron microscopy. The Michaelis constant values of free and immobilized HRP were determined to be 4.5 and 5 mM for hydrogen peroxide and 12.5 and 10 mM for guaiacol, respectively. Moreover, the maximum values of free and immobilized HRP were 2.4 and 2 U for H2O2, respectively, and 1.25 U for guaiacol. The immobilized enzyme was thermally stable up to 60°C, whereas the free peroxidase was stable only up to 40°C. In the catalytic experiment, the immobilized HRP exhibited superior catalytic activity compared with that of free HRP for the oxidative decolorization and removal of acid black-HC dye. The influence of experimental parameters such as the catalyst dosage, pH, H2O2 concentration, and temperature on the removal efficiency was investigated. The reaction followed second-order kinetics, and the thermodynamic activation parameters were determined.
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Keshta, B.E., Gemeay, A.H. & Khamis, A.A. Impacts of horseradish peroxidase immobilization onto functionalized superparamagnetic iron oxide nanoparticles as a biocatalyst for dye degradation. Environ Sci Pollut Res 29, 6633–6645 (2022). https://doi.org/10.1007/s11356-021-16119-z
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DOI: https://doi.org/10.1007/s11356-021-16119-z