CAJ | 학술논문

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.
이옥미심섬유소위기질,통과배양록병완（EPI）교련활화、아안기이을산（IDA）수식、금속리자Cu,Fe,Zn,Ni오합제득친화흡부제.통과홍외광보（FTIR）、X사선광전자능보（XPS）、원자흡수분광광도법（AAS）대기표정.고찰료pH、리자강도、초시농도、세탈액등인소대오합료불동금속리자적흡부제흡부우혈청백단백（BSA）적영향.결과표명：대강친화성적Cu（Ⅱ）오합친화흡부제대BSA적흡부주요수배위작용공제,이대약친화성적Fe（Ⅱ）、Zn（Ⅱ）、Ni（Ⅱ）오합친화흡부제칙주요수정전작용영향,배위작용위보.
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.