Citation: WANG Jianshan, XIA Hongjun, WAN Guangping, LIU Jiawei, BAI Quan. A novel dual-function weak cation exchange/hydrophobic interaction chromatography stationary phase with aminocaproic acid as the ligand for protein separation[J]. Chinese Journal of Chromatography, ;2016, 34(12): 1228-1233. doi: 10.3724/SP.J.1123.2016.08019 shu

A novel dual-function weak cation exchange/hydrophobic interaction chromatography stationary phase with aminocaproic acid as the ligand for protein separation

Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education of China, Institute of Modern Separation Science, Northwest University, Provincial Key Laboratory of Modern Separation Science of Shaanxi, Xi'an 710069, China

Received Date: 18 August 2016

Fund Project: National Natural Science Foundation of China (No. 21545007)

A novel dual-function mixed-mode stationary phase based on silica gel functionalized with aminocaproic acid as the ligand was prepared. Because of the ligand with hydrophobicity and containing carboxyl function groups, it could display hydrophobic interaction chromatography (HIC) character in a high salt concentration mobile phase and weak cation exchange chromatography (WCX) character in a low salt concentration mobile phase. As a result, it could be employed to separate proteins with both WCX and HIC modes. The resolution and selectivity of the stationary phase were evaluated under both HIC and WCX modes with protein standards. In comparison with the conventional WCX and HIC columns, the results were satisfactory and acceptable. Protein mass and bioactivity recoveries of more than 93% could be achieved in both WCX and HIC mode using this column. The results indicated that the novel dual-function mixed-mode column in many cases could replace the use of two individual WCX and HIC columns. Based on this two-dimensional (2D) column, a new two-dimensional liquid chromatography (2DLC) technology with a single column (2DLC-1C) was developed. Eight kinds of protein standards could be separated completely with online 2DLC-1C within 60 min. It was also applied to purify lysozyme from egg white successfully with a purity of 98.3%. It is important to proteome research and recombinant protein drug production for saving column expense and simplifying the process in biotechnology.
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