Separation and evaluation of soybean protein hydrolysates prepared by immobilized metal ion affinity chromatography with different metal ions.
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.
College of Food Science & Nutritional Engineering, China Agricultural University, Beijing, 100083, China.
He
H
Liu
Xiao Lan
XL
Bao
Ying
Y
Lv
Jing Ting
JT
Xu
Shun Tang
ST
Guo
D000327:Adsorption; D000704:Analysis of Variance; D002846:Chromatography, Affinity / Q000379:methods*; D002851:Chromatography, High Pressure Liquid; D057927:Hydrophobic and Hydrophilic Interactions; D007098:Imino Acids / Q000737:chemistry; D019216:Metals, Heavy / Q000737:chemistry* / Q000378:metabolism; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D011485:Protein Binding; D012685:Sepharose / Q000737:chemistry; D030262:Soybean Proteins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D007098:Imino Acids; D019216:Metals, Heavy; D010455:Peptides; D030262:Soybean Proteins; D012685:Sepharose; C008109:iminodiacetic acid