Thermodynamics of the interaction between Cr3+ with β-lactoglobulin type A (BLG-A) was investigated at pH 7.0 and 37 o C by isothermal titration calorimetry. A new method to follow the effect of Cr 3+ on the stability of BLG-A was introduced. The new solvation model was used to reproduce the enthalpies of BLG-A+ Cr 3+ interactions over the whole range of Cr 3+ concentrations. The solvation parameters recovered from the new equation are attributed to the structural change of BLG-A and its biological activity. The results obtained indicate that there is a set of two identical binding sites for Cr for the first and second binding site, respectively. The enthalpy of binding for one mole of Cr +3 ion to one mole of the binding site on BLG-A (ΔH=104.60 kJ mol -1 ) is obtained.