Thermodynamics of the interaction between oleic acid, OA, with egg lysozyme was investigated at pH 7.0 and in phosphate buffer by isothermal titration calorimetry, ITC. The extended solvation model was used to reproduce the heats of OA+lysozyme interactions. The binding parameters recovered from the extended solvation theory, attributed to the structural change of lysozyme. The binding parameters found for the interaction of OA with lysozyme, indicate that at low concentrations of OA, lysozyme structure was destabilized but in the higher concentrations of OA, lysozyme was partially denaturated.

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