The displacement adsorption enthalpies (ΔH) of denatured α-Amylase (by 1.8 mol L−1 GuHCl) adsorbed onto a moderately hydrophobic surface (PEG-600, the end-group of polyethylene glycol) from solutions (x mol L−1 (NH4)2SO4, 0.05 mol L−1 KH2PO4, pH 7.0) at 298 K are determined by microcalorimeter. Further, entropies (ΔS), Gibbs free energies (ΔG) and the fractions of ΔH, ΔS, and ΔG for net adsorption of protein and net desorption of water are calculated in combination with adsorption isotherms of α-Amylase
based on the stoichiometric displacement theory for adsorption (SDT-A) and its thermodynamics. It is found that the displacement
adsorptions of denatured α-Amylase onto PEG-600 surface are exothermic and enthalpy driven processes, and the processes of
protein adsorption are accompanied with the hydration by which hydrogen bond form between the adsorbed protein molecules favor
formation of β-sheet and β-turn structures. The Fourier transformation infrared spectroscopy (FTIR) analysis shows that the
contents of ordered secondary structures of adsorbed α-Amylase increase with surface coverages and salt concentrations increment.