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Protein-imprinted polyacrylamide (PAM)-grafted calcium alginate (CaA) microspheres were synthesized via free-radical grafting polymerization with potassium persulfate and sodium bisulfite as initiators. FTIR, 13C-NMR and SEM were used for characterization. Swelling behaviors were studied and it was found that modified calcium alginate (CaA) microspheres possessed larger swelling degree than calcium alginate, because grafted hydrophilic PAM side chains contributed to more water absorption. Moreover, the durability of the swollen samples was improved for the modified microspheres. Compared with calcium alginate microspheres, modified calcium alginate samples exhibited higher absorption capacity (approximately, 13.1 and 10.3 mg/g) for MIPs in single and binary protein solution. The rebinding selectivity of CaA-g-PAM microspheres (approximately, 2.7) was higher than that of calcium alginate (CaA) microspheres (approximately, 1.5) in binary protein solution. It was suggested that the introduction of PAM side chains was beneficial for the specific recognition of protein. [ABSTRACT FROM AUTHOR]

Bovine serum albumin imprinted polyethylene glycol 600 (PEG600) grafted Calcium alginate (CaA) hydrogel microspheres were prepared and characterized. The adsorption and recognition properties of PEG600 grafted calcium alginate (CaA- g-PEG600) microspheres were evaluated and the results showed that the crosslinking structure of CaA- g-PEG600 microspheres exerted an obvious effect on the adsorption capacity and imprinting properties for bovine serum albumin. The adsorption isotherms and recognition properties indicated that the imprinted modified microspheres had excellent rebinding affinity toward target proteins and the imprinting efficiency varied according to PEG600 grafting degree. The adsorption capacity and the imprinting factor were 5.5 mg g and 3.6, respectively. Adsorption kinetics of CaA- g-PEG600 microspheres in accordance with the molecular weight between crosslinks ( Mc) was investigated and the structural influence on protein selective rebinding was discussed. Furthermore, the binary solution separation performance of CaA- g-PEG600 microspheres with different Mc was investigated by selective binding bovine serum albumin from protein mixture solution. [ABSTRACT FROM AUTHOR]