通过4步化学反应对磁性Fe3O4@SiO2纳米粒子进行化学修饰,设计和制备了一种N,N'-二(5-四唑亚甲基)胺修饰的金属螯合磁性纳米粒子。用X射线光电子能谱(XPS)、Zeta电位对该新型吸附剂进行了表征。用静态吸附法研究了螯合Cu吸附剂对溶菌酶、细胞色素C和α-糜蛋白酶的吸附性能以及溶液pH值、盐浓度、蛋白初始浓度对吸附量的影响。结果表明,吸附剂对蛋白质的吸附主要通过金属配位机理进行,且符合Langmuir吸附模型,对溶菌酶、细胞色素C和α-糜蛋白酶的最大吸附量分别20.0、13.5和17.9 mg/g。此外,将螯合Cu(Ⅱ)吸附剂用于混合蛋白质样品的吸附,发现此吸附剂对混合蛋白质样品中的溶菌酶具有选择性吸附作用,说明此金属螯合吸附剂在蛋白质选择性分离富集中具有一定应用价值。
A bis(5-methyltetrazolium)amine-bonded magnetic nanoparticle adsorbent was prepared by chemically modifying magnetic nanoparticles Fe3O4@SiO2 via four steps chemical reactions. The physical properties of the adsorbent were characterized by X-ray photoelectron spectroscopy (XPS) and Zeta potential. The static adsorption behavior of lysozyme, cytochrome C and chymotrypsin on the chelated Cu(Ⅱ) adsorbent, as well as the influences of the pH value of solution, ion strength and initial protein concentration on the adsorption capacity were evaluated with batch method. The results illustrated that the adsorption of protein proceeded via metal coordination mechanism and was also in accordance with Langmuir adsorption model, and the maximum adsorption capacities of lysozyme, cytochrome C and chymotrypsin were calculated to be 20.0 mg/g, 13.5 mg/g, and 17.9 mg/g, respectively. In addition, the chelated Cu(Ⅱ) adsorbent was employed to adsorb protein mixture, showing that this new type of adsorbent had selective adsorption to protein mixture. These results illustrated that the metal-chelated adsorbent had potential application value in selectively separating and enriching proteins.
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