Abstract
ABSTRACTBased on a crosslinked chitosan (CS)/polyvinyl alcohol (PVA) matrix membrane, an immobilized metal ion affinity membrane (IMAM) using Cu2+ and Ni2+ ions as affinity ligands was prepared for purification of the His‐tagged recombinant protein. The affinity membrane possessed a favorable membrane structure including 1.39 μm average pore size and 0.33 mL·cm−2·s−1 water flux under 0.08 MPa pressure at 25 °C. The Cu2+ and Ni2+ ions capacities immobilized on the IMAM were 155.6 and 137.3 μmol·disk−1, respectively. The IMAM had an excellent specific affinity to His‐tagged protein. About 10‐fold purification factor for the model protein was obtained in a batch adsorption, and serine hydroxymethyl transferase could be purified to a single band in sodium dodecyl sulfate–polyacrylamide gel electrophoresis analysis from its crude extract solution with an affinity membrane cartridge by a dynamic purification process. This work provides a promising IMAM for the purification of His‐tagged recombinant proteins. © 2018 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2019, 136, 47347.
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