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Adsorption characteristics of bovine serum albumin and rifampicin on immobilized metal ion affinity mesoporous adsorbents

机译:固定化金属离子亲和性介孔吸附剂对牛血清白蛋白和利福平的吸附特性

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摘要

Bovine serum albumin and rifampicin adsorption are studied by using MCM-41 and SBA-15 immobilized with metal ion, Cu2+, Ni2+ and Co2+ during their synthesis as the adsorbents. Batch equilibrium adsorption experiment were carried out to study the effect of the solution pH, types of adsorbents, types of metal immobilized on the mesoporous adsorbents and metal loading concentration on adsorption capacity. Buffered BSA and rifampicin was contacted with the adsorbents, shaken and centrifuged. BSA and rifampicin concentration was determined by UV/Vis spectrophotometer while adsorbate-adsorbent interactions were determined by Fourier Transform Infrared (FTIR). The adsorption capacity of BSA was highest at pH 4 near the pI of BSA at 4.9 while rifampicin uptake was maximum at pH 7 near the pKa2 of rifampicin. This is due to electrostatic attraction between proteins and surface of adsorbents. It was found that cationic form of rifampicin exhibited very high degree of adsorption with the cationic exchanger of adsorbents. Immobilization of metal ions into mesoporous framework has proven to increase the adsorption rate of BSA and rifampicin, and metal ions with different concentration also gave some influence to the adsorption capacity.
机译:以金属离子,Cu2 +,Ni2 +和Co2 +固定化的MCM-41和SBA-15为吸附剂,研究了牛血清白蛋白和利福平的吸附。进行了间歇平衡吸附实验,研究了溶液的pH值,吸附剂类型,固定在中孔吸附剂上的金属类型以及金属负载量对吸附容量的影响。使缓冲的BSA和利福平与吸附剂接触,摇动并离心。用紫外/可见分光光度计测定牛血清白蛋白(BSA)和利福平的浓度,用傅立叶变换红外光谱(FTIR)测定被吸附物与吸附剂的相互作用。 BSA的吸附容量在4.9的BSA pI附近在pH 4时最高,而利福平的吸收在rifampicin的pKa2附近在pH 7时最大。这是由于蛋白质和吸附剂表面之间的静电吸引。已经发现,利福平的阳离子形式在吸附剂的阳离子交换剂上表现出非常高的吸附度。已证明将金属离子固定在中孔骨架中可以提高BSA和利福平的吸附速率,而且不同浓度​​的金属离子也对吸附容量有一定影响。

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