玉米芯纤维素基金属螯合亲和吸附剂对牛血清白蛋白的吸附研究  

Preparation of Corn Cellulose Based Adsorbents with Metal-Chelated Affinity and Their Adsorption Behaviour for BSA

作　　者：李步海[1] 张永红[1] 

机构地区：[1]中南民族大学化学与材料科学学院分析化学国家民委重点实验室,武汉430074

出　　处：《中南民族大学学报（自然科学版）》2012年第4期1-5,共5页Journal of South-Central University for Nationalities：Natural Science Edition

基　　金：国家民委院校科研基金资助项目(MJY00004)

摘　　要：以玉米芯纤维素为基质,通过环氧氯丙烷(EPI)交联活化、亚氨基二乙酸(IDA)修饰、金属离子Cu,Fe,Zn,Ni螯合制得亲和吸附剂.通过红外光谱(FTIR)、X射线光电子能谱(XPS)、原子吸收分光光度法(AAS)对其表征.考察了pH、离子强度、初始浓度、洗脱液等因素对螯合了不同金属离子的吸附剂吸附牛血清白蛋白(BSA)的影响.结果表明:对强亲和性的Cu(Ⅱ)螯合亲和吸附剂对BSA的吸附主要受配位作用控制,而对弱亲和性的Fe(Ⅱ)、Zn(Ⅱ)、Ni(Ⅱ)螯合亲和吸附剂则主要受静电作用影响,配位作用为辅.Several biosorbents were successfully prepared using coin cellulose as supporting materials, epichlorohydrin （EPI） as crosslinking agent and iminodiacetic acid （IDA） as modification agent. Adsorbents with metal-chelated affinity were obtained by chelating with Cu, Fe, Zn and Ni metal ions respectively. These novel adsorbents were characterized with FIIR, XPS and AAS. The effects of pH, ionic strength, initial concentration, desorbents on the adsorption of adsorbents for BSA were studied. It was proposed that the retention of protein on Cu （ 11 ） chelating affinity adsorbent was mainly dominated by the coordination role between the immobilized metal and protein. The protein retention on Fe（ II ）, Zn（ lI ） and Ni（ 11 ） chelating affinity adsorbents with weak affinity was mainly controlled by the electrostatic interaction between metal chelating ligand and protein, whereas the coordination role was additional in the protein retention.

关 键 词：纤维素 金属螯合亲和吸附剂 吸附 洗脱 牛血清白蛋白 

分 类 号：O652.6[理学—分析化学]