Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste

• Protein G imprinted monolithic macroporous cryogel was prepared.
• The imprinted cryogel had affinity to protein G and able to capture it from cell lysate.
• The Protein G adsorption best described by the Langmuir isotherm.

Monolithic macroporous cryogel imprinted with protein G was prepared using a functional co-monomer of N-methacryloyl-l-phenylalanine and 2-hydroxyethyl methacrylate. The chemical structure of the cryogel prepared was studied by FTIR-spectroscopy and its porosity was analysed using scanning electron microscopy. The cryogel was used to purify protein G from recombinant Escherichia coli cell lysate and the effect of pH, temperature, ionic strength, flow rate, etc on the adsorption of protein G to the monolithic column have been investigated. The selectivity of the imprinted cryogel was studied using protein A and myoglobin. It was possible to capture about 9 mg of Protein G per g of the cryogel.