parameters First binding sites Second binding sites p 1 1 gi 2.00±0.03 5.11±0.08 Ka/M 49967.89±21.15 130462.30±13.06 ΔH/ kJ mol-1site-1 -2.05±0.05 -0.08±0.01 ΔG/ kJ mol-1 site-1 -26.80±0.15 -29.18±0.25 ΔS/ kJ mol-1 site-1 0.09±0.01 0.10±0.01 -0.36±0.03 0.09±0.02

Table 2: Binding parameters for lysozyme+βCD interaction recovered from Eqs.1 and 2 at pH 12. p=1 indicates that the binding is non-cooperative in two sets of binding sites. Enthalpic force in the first binding sites is more important than entropic one, indicating that electrostatic interaction plays an important role in the interaction of lysozyme with βCD. The interaction in the second binding sites is stronger and both enthalpy and entropy driven but hydrophobic interaction has more important than electrostatic force.