In this study, silica-coated magnetic iron oxide nanoparticles (MNPs@SiO₂) were covalently conjugated onto graphene oxide (GO/MNP@SiO₂) for protein isolation. First, MNPs were precisely coated with a silica layer on the surface by using the reverse microemulsion method, followed by incubation with 3-glycidyloxypropyltrimethoxysilane (GPTS) to produce the GPTS-functionalized MNPs@SiO₂ (GPTS-coated MNPs@SiO₂) that display epoxy groups on the surface. The silica shell on the MNPs was optimized at 300 µL of Igepal^®CO-520, 5 mg of MNP, 100 µL of TEOS, 100 µL of NH₄OH and 3% of 3-glycidyloxypropyltrimethoxysilane (GPTS). Simultaneously, polyethyleneimine (PEI) was covalently conjugated to GO to enhance the stability of GO in aqueous solutions and create the reaction sites with epoxy groups on the surface of GPTS-coated MNP@SiO₂. The ratio of PEI grafted GO and GPTS-coated MNP@SiO₂ (GO/MNP ratio) was investigated to produce GO/MNPs@SiO₂ with highly saturated magnetization without aggregation. As a result, the GO/MNP ratio of 5 was the best condition to produce the GO/MNP@SiO₂ with 9.53 emu/g of saturation superparamagnetization at a magnetic field of 2.0 (T). Finally, the GO/MNPs@SiO₂ were used to separate bovine serum albumin (BSA) to investigate its protein isolation ability. The quantity of BSA adsorbed onto 1 mg of GO/MNP@SiO₂ increased sharply over time to reach 628 ± 9.3 µg/mg after 15 min, which was 3.5-fold-higher than that of GPTS-coated MNP@SiO₂. This result suggests that the GO/MNP@SiO₂ nanostructure can be used for protein isolation.

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