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Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste B Analytical technologies in the biomedical and life sciences
- Asliyuce, Sevgi, Mattiasson, Bo, Mamo, Gashaw
- Journal of chromatography 2016 v.1021 pp. 204-212
- Escherichia coli, Fourier transform infrared spectroscopy, adsorption, chemical structure, chromatography, ionic strength, myoglobin, pH, porosity, porous media, scanning electron microscopy, temperature
- 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 9mg of Protein G per g of the cryogel.