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Repeated use of a hydrophobic ligand-containing porous membrane for protein recovery
Institution:1. Department of Specialty Materials, Faculty of Engineering, Chiba University, Inage, Chiba 263, Japan;2. Industrial Membranes Development Department, Asahi Chemical Industry Co. Ltd., Fuji, Shizuoka 416, Japan;3. Takasaki Radiation Chemistry Research Establishment, Japan Atomic Energy Research Institute, Takasaki, Gunma 370-12, Japan;1. Department of Biochemical Engineering, University College London, Bernard Katz Building, London WC1H 0AH, UK;2. Innovations Technology Access Centre – Micro and Nanotechnology, Rutherford Appleton Laboratory, Science and Technology Facilities Council, Harwell Oxford, Didcot OX11 0QX, UK;3. School of Science and Technology, Nottingham Trent University, Nottingham, NG1 4BU, UK;1. State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China;2. The Institute for Advanced Studies, Wuhan University, Wuhan 430072, China;3. Department of Chemistry, Shaoxing University, Shaoxing 312000, China;1. Graduate School of Environmental Studies, Tohoku University, Aramaki 6-6-11-605, Aoba, Sendai 980-8579, Japan;2. Advanced Institute for Materials Research, Tohoku University, Katahira 2-1-1, Aoba, Sendai 980-8577, Japan
Abstract:A porous hollow-fiber membrane containing a phenyl group as a hydrophobic ligand was prepared by radiation-induced graft polymerization of glycidyl methacrylate, followed by successive ring-opening reactions with phenol and water. Bovine serum albumin (BSA) was bound to the ligand during permeation of a BSA solution in phosphate buffer containing 2M (NH4)2SO4 through the pores of the hollow fiber. Subsequent elution with an (NH4)2SO4-free buffer exhibited an elution percentage of 82%. Repeated cycles of adsorption and elution caused the accumulation of BSA on the pore surface, resulting in a decrease in the binding capacity of BSA with increasing number of cycles. In contrast, by permeating 1 M NaOH after each elution, the binding capacity of BSA was maintained even after ten cycles. This alkaline regeneration was found to be effective in ensuring repeated use of the phenyl-group-containing porous membrane for recovery of proteins.
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