[Effects of composition of mobile phases on retention behavior of solutes in hydrophobic interaction chromatography]

The retention behavior of aromatic alcohol homologues in hydrophobic interaction chromatography (HIC) was investigated for the first time. The differences in retention behavior between proteins and small solutes, and the eluted range and ability of different salts to small solutes and biopolymers, are elucidated with the parameter Z of the stoichiometric displacement retention model. The retention of aromatic alcohols follows the homologue rule. By the comparison of the changes of Z in different salt solutions, it is found that for small molecules the salt type only changes the hydration degree; but for proteins, it not only changes the hydration of proteins and stationary phase, but also affects the conformation of protein molecules near the contact regions between the protein and the stationary phase surface.