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《Journal of Xiamen University(Natural Science)》 2010-01
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Preparation of Bovine Serum Albumin Affinity Monolith for Chiral Separation of D,L-tryptophan by Capillary Electrochromatography

YAO Chuan-yi,JIA Jing-bo,CHEN Wei-qi (College of Chemistry and Chemical Engineering,Xiamen University,Xiamen 361005,China)  
Enantioseparation of D,L-tryptophan was studied on an affinity monolithic column by capillary electrochromatography. A chitosan/silica hybrid monolithic column was prepared by the sol-gel method.Then the affinity stationary phase was synthesized by the in situ covalent immobilization of BSA on the monolithic column activated with glutaraldehyde.The monolith was used for chiral separation of D,L-tryptophan by capillary electrochromatography.The effects of pH,concentration of running buffer,and the content of organic modifier on the separation of D,L-tryptophan were investigated.The retention times of the solutes decrease and the resolution increases with the increase of buffer pH from 6.0 to 8.0.With the increase of buffer concentration from 5 to 50 mmol/L,the retention times of the solutes increase,while the resolution increases to a higher-value and then decreases.The organic modifier is not conducive to the chiral separation in this experimental system.A best separation of tryptophan enantiomers is achieved by using pH 7.5,20 mmol/L phosphate buffer,with the resolution of 2.44.
【Fund】: 国家自然科学基金(20876128);; 福建省自然科学基金(E0610030)项目
【CateGory Index】: O657.8
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