Separation and evaluation of soybean protein hydrolysates prepared by immobilized metal ion affinity chromatography with different metal ions.
Separation and evaluation of soybean protein hydrolysates prepared by immobilized metal ion affinity chromatography with different metal ions.
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DOI：
10.1093/chromsci/bms071
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发表时间：
2012-09
影响因子：
1.3
通讯作者：
He Liu;Xiaolan Bao;Y. Lv;Jingting Xu;Shuntang Guo
中科院分区：
文献类型：
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作者：
He Liu;Xiaolan Bao;Y. Lv;Jingting Xu;Shuntang Guo
由于氨基酸的差异，金属离子亲和层析被广泛用于纯化肽。然而，研究人员对这种方法中不同金属离子之间的分离差异感兴趣。在我们的研究中，通过亚氨基二乙酸-Sepharose上的固定金属离子量和大豆肽与固定亚氨基二乙酸-Mn(+)吸附剂的结合量来比较四种常用的金属离子，并通过高效液相色谱（HPLC）图谱进行评估。结果表明，由于金属离子的吸附行为不同，大豆蛋白肽在柱上的结合能力顺序为Fe(3+)>Cu(2+)>Zn(2+)>Ca(2+)。 HPLC图谱表明，四种金属离子吸附的肽表现出相似的强疏水特性。
Metal ion affinity chromatography is widely used to purify peptides on the basis of the dissimilarities of their amino acids. However, researchers are interested in the separation differences between different metal ions in this method. In our study, four kinds of commonly used metal ions are compared by the amount of immobilized metal ion on iminodiacetic acid-Sepharose and binding amount of soybean peptide to immobilized iminodiacetic acid-Mn(+) adsorbents and evaluated by high-performance liquid chromatography (HPLC) profiles. The results show that due to the different adsorption behaviors of metal ions, the binding ability order of soybean protein peptide on the column should be Fe(3+) > Cu(2+) > Zn(2+) > Ca(2+). The HPLC profiles show that peptides adsorbed by four kinds of metal ions display similar strong hydrophobic characteristics.