Both calorimetric determination of displacement adsorption enthalpies ΔH and measurement of adsorbed amounts of lysozyme (Lyz) denatured by 1.8 mol L−1 guanidine hydrochloride (GuHCl) on a moderately hydrophobic packings at 298 K, pH 7.0 and various salt concentrations were
carried out. Based on the thermodynamics of stoichiometric displacement theory (SDT) the fractions of thermodynamic functions,
which related to four subprocesses of denatured protein refolding on the surface, were calculated and thermodynamic analysis
that which one of the subprocesses plays major role for contribution to the thermodynamic fractions was made in detail. The
moderately hydrophobic surface can provide denatured Lyz energy and make it gain more conformation with surface coverage or
salt concentration increment. The displacement adsorptions of denatured Lyz onto PEG-600 surface are exothermic, more structure-ordered
and enthalpy driven processes.