Iron magnetic nanoparticles have attracted much attention. They have been used in enzyme immobilization because of their properties such as product is easily separated from the medium by magnetic separation. The present work was designed to immobilize horseradish peroxidase on Fe3O4 magnetic nanopraticles without modification.In the present study, horseradish peroxidase (HRP) was immobilized on non-modified Fe3O4 magnetic nanoparticles. The immobilized HRP was characterized by FT-IR spectroscopy, scanning electron microscopy, and energy dispersive X-ray. In addition, it retained 55% of its initial activity after 10 reuses. The optimal pH shifted from 7.0 for soluble HRP to 7.5 for the immobilized HRP, and the optimal temperature shifted from 40°C to 50°C. The immobilized HRP is more thermostable than soluble HRP. Various substrates were oxidized by the immobilized HRP with higher efficiencies than by soluble HRP. Km values of the soluble and immobilized HRP were 31 and 45mM for guaiacol and 5.0 and 7.0mM for H2O2, respectively. The effect of metals on soluble and immobilized HRP was studied. Moreover, the immobilized HRP was more stable against high concentrations of urea, Triton X-100, and isopropanol.Physical immobilization of HRP on iron magnetic nanoparticles improved the stability toward the denaturation induced by pH, heat, metal ions, urea, detergent, and water-miscible organic solvent.
显示更多 [+] 显示较少 [-]
AGRIS - 国际农业科技情报系统
Share
出版者
John Wiley & Sons, Ltd
其它主题
Scanning electron microscopy; Energy-dispersive x-ray analysis; Activity; Metal ions; Fourier transform infrared spectroscopy; Energy dispersive x-ray; Protein immobilization; Scanning electron microscopy; Immobilized; Magnetic separation; Octoxynol; Ft-ir spectroscopy; Soluble horseradish peroxidase
语言
英语
类型
Journal Article; Text
2024-02-28
2026-02-03
MODS