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Background:  Protein purification is the most complicated issue in the downstream processes of recombinant protein production; therefore, improved selective purification methods are important. Affinity-based protein purification method using His-tag and Ni-NTA resins is one of the most common strategies. MNPs can be used as a beneficial alternative for Ni-NTA resins. However, there is no data on the capability of MNPs for protein purification from inclusion bodies; this issue is studied here.Methods:  Recombinant His-tagged proteins of EGFP-His and SK-His were expressed in  E. coli  BL-21 (DE3) in soluble and inclusion body forms, respectively. MNPs including Fe 3 O 4  magnetic core, SiO 2  shell, and Ni 2+  on the surface were synthesized by sol-gel and hydrothermal reactions and then characterized by XRD, VSM, and SEM imaging. Both synthesized Fe 3 O 4 @NiSiO 3  and Fe 3 O 4 @Ni x SiO y  MNPs were employed to purify EGEP-His and SK-His under native and denaturing conditions, respectively. The quantity and purity of purified proteins were analyzed by micro-Bradford assay and SDS-PAGE, respectively.Results:  Both synthesized MNPs were spherical and well-dispersed with the size ranging from 290 to 415 nm. Synthesized MNPs contained Fe 3 O 4,  SiO 2  shell, and Ni 2+  on their structures with suitable magnetization properties. Using Fe 3 O 4 @NiSiO 3  and Fe 3 O 4 @Ni x SiO y  yielded 192 and 188 µg/mg of SK-His, as compared to 207 and 195 µg/mg of EGFP-His, respectively.Conclusion:  MNPs containing magnetic Fe 3 O 4  core, SiO 2  shell, and Ni 2+ on their surface are versatile alternatives for Ni-NTA resins in protein purification for proteins expressed in both soluble and inclusion body forms.

Affinity Based Nano-Magnetic Particles for Purification of Recombinant Proteins in Form of Inclusion Body