Impact of non-covalent interactions on the solvation of ovalbumin in an aqueous environment of different pHs: Thermodynamic and diffusion studies.

The solvation behavior of protein is an important factor in protein-based food products. In the present study, the xylitol (XY) - ovalbumin (OVN) interaction in an aqueous solution of different pH conditions is analyzed in two methods. In one method, the thermodynamic parameters Gibbs free energy, free volume, and internal pressure are calculated by using ultrasonic velocity, density, and viscosity in addition the refractive index is also measured. The second method is a theoretical method in which using the Laplace transform technique the diffused amount of protein have been calculated for OVN with and without XY in different pH environment. The addition of XY with OVN makes the system with more free energy and free volume as the internal pressure decreases. This trend shows that preferential interaction occurs between solvent-solute molecules. The diffusivity of OVN is reduced after the addition of XY representing the strength of protein-protein interaction. The effect of pH changes is well reflected in both experimental and theoretical results. The results confirm that acidic pH extremity offers more solvation of OVN compared to alkaline pH extremity.