Molecular details of ovalbumin solvation by an aqueous solution of xylitol in different pH environment:Ultrasonic and molecular simulation studies

Abstract

Artificial sweetener-protein interactions are playing a major role in enhancing the functional properties of protein-based food and pharmaceutical products. This article discusses the molecular details of ovalbumin (OA) solvation in an aqueous solution of xylitol (XY) in different pH environments. This task can be accomplished by both Ultrasonic and Molecular Simulation studies. In ultrasonic studies, density, ultrasound velocity, viscosity, and surface tension have been measured for OA in various pH of phosphate buffer with and without XY. Further, some of the calculated parameters such as adiabatic compressibility, intermolecular free length, free volume, etc have been worked out. From ultrasonic results, pH dependent preferential hydration of OA was noticed in the presence of XY in an aqueous environment. In Molecular Dynamics Simulation (MDS) studies, water and XY accumulation to OA surface for different pH models were analyzed. The different states of protonation of the OA surface promote two distinct effects on the solvent and cosolvent orientation.