The Effect of Temperature on the Enantiomeric Resolutions on Albumin and
温度对蛋白和β-环糊精手性固定相拆分对映体的影响

The effect of column temperature on enantiomeric resolutions of tryptophan, warfarin and ketoprofen was investigated on bovine and human serum albumin (BSA and HSA) stationary phases, which were synthesized with s-triazine as the activator. It was observed that the entropy change made a great contribution to the separation of those enantiomers on albumin chiral stationary phases. The column temperature for the maximal resolution of tryptophan on the BSA stationary phase prepared by this method was about 35 degrees C, which was not 24 degrees C as reported for the BSA stationary phase synthesized with glutaric dialdehyde as the activator. This results may come from the different conformation of the immobilized BSA and HSA due to the different coupling methods used. On the other hand, it was indicated that the resolution of enantiomers on beta-CD chiral stationary phase was mainly contributed from the change of enthalpy, which means the resolution of chiral solutes on albumin and beta-CD stationary phases has different thermodynamic behaviors.