Preparation of NiFe2O4 architectures for affinity separation of histidine-tagged proteins

• NiFe2O4 architectures have been synthesized by the hydrothermal method.
• NiFe2O4 architectures mainly consist of radial fibers.
• NiFe2O4 architectures can capture directly His-tagged proteins from the mixture of lysed cells.

NiFe2O4 architectures were synthesized by a hydrothermal method. NiFe2O4 architectures consist of radial fibers with 30 nm in diameters and 1 µm in lengths. These architectures possess an excellent magnetic response and have Brunauer–Emmett–Teller (BET) surface area of 73.1 m2/g. Due to their high Ni2+ density, these architectures can be used to magnetically separate histidine-tagged (His-tagged) proteins directly from the mixture of lysed cells. The results show that the architectures present negligible nonspecific adsorption and high protein binding activity with the max value of 120.1 mg/g.

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