Study On Preparation Of Molecular Imprinted Polymer And Performance For The Protein

Protein nutrition is essential to life,and the separation and purification of protein is attracting more and more attentions.Molecular imprinting technology can screen target molecules selectively.Therefore,in this paper,the molecular imprinting technique was applied to separation and purification of protein,and molecularly imprinted membrane and molecularly imprinted hollow magnetic microspheres were prepared using Bovine Serum Albumin?BSA?as the template and theirs performances were also studied.1.Using functionalized ionic liquid chloride 1-Vinyl-3-carbamyl methyl imidazole[VAFMIM]Cl as functional monomer,phosphate buffer solution?PBS,pH7.2?as solvent,N,N-methylene bisacrylamide?MBA?as crosslinking agent,ammonium sulfate?APS?as initiator and N,N,N,N-tetramethylethylenediamine?TEMED?as the catalyst,the bovine serum albumin imprinted membrane?CP-MIM?with supermacroporous was perpared by freezing polymerization.The effects of different experimental conditions on membrane binding capacity,and the adsorption mechanism were studied.Choosing Ovalbumin?OVA?,Lysozyme?Lys?and Bovine Hemoglobin?BHb?as competitive protein to investigate the selectivity of molecularly imprinted membrane for BSA.The static penetration and dynamic filtration to imprinting and separation effect of CP-MIM were investigated.Sodium dodecyl sulfate polyacrylamide gel electrophoresis?SDS-PAGE?was used to analyze samples.The results showed that the molecularly imprinted membrane has specific effect on the separation of BSA.2.Using vinyl chloride-1-3-carbamyl methyl imidazole ionic liquid?[VAFMIM]Cl?,N-isopropylacrylamide?NIPAm?and?-methyl methacrylate??-MAA?as the multifunctional monomers,tris?hydroxymethyl?aminomethane buffer solution?Tris-HCl,10mmol/L,pH7.0?as solvent,N,N-methylene bisacrylamide?MBA?as crosslinking agent,ammonium persulfate?APS?as initiator and N,N,N,N-tetramethylethylenediamine?TEMED?as catalyst,a smart BSA molecular imprinting hollow magnetic microsphere?HMIP?of multiple responses?magnetic,thermo-sensitive,ion and pH responses?was prepared.On the basic of morphology and characteristics the different experimental conditions for preparing magnetic microsphere?Fe₃O₄?were investigated.The effects on HMIP binding ability under different experimental conditions were also studied,and the adsorption mechanism and the effect of multiple response of HMIP were investigated.Choosing Ovalbumin?OVA?,Lysozyme?Lys?and Bovine Hemoglobin?BHb?experiment as competitive protein,the selectivity of HMIP for BSA was investigated.Sodium dodecyl sulfate polyacrylamide gel electrophoresis?SDS-PAGE?was applied to analyze samples.The results showed that the HMIP provide a feasible method for the separation of BSA.