Calorimetric determination of the total enthalpy changes (ΔHi) of guanidine-denatured lysozyme (Lys) during the adsorption with simultaneously refolding on the surface of hydrophobic
interaction chromatography packings was carried out at 250.001C. The measured ΔHiin the circumstances should include the changes in the three fractions: adsorption, dehydration and molecular conformation.
It was found that when the unfolded Lys molecules are adsorbed and refold on the surface, entropy-driving caused by the dehydration
of Lys mainly dominates the foregoing process. The refolding enthalpies of Lys, ΔΔHiwere found to be 10~100 folds higher than that measured in usual solutions.</o:p>