Abstract
The protein–sucralose (SL) interaction is gaining significant attention in food and medicinal formulations, because of the unique features of SL in comparison to regular sugars. The main goal of this study is to determine the fluctuation in ovalbumin (OA) conformation in various pH and the presence of the cosolvent SL. Density, ultrasonic velocity, and viscosity, results were used to calculate physicochemical parameters like change in Gibbs free energy, free volume, and internal pressure. The inclusion of SL with OA records a large magnitude of denaturation at acidic pH compared to alkaline pH reflects in the variation of refractive index and change in Gibbs free energy. These results reveal that the inclusion of SL with OA favours the dipole–dipole interactions among the component molecules. Results obtained from Laplace transform studies show that the reduction of diffusion in OA towards SL confirms the denaturation of OA in the presence of SL. Both physicochemical and theoretical analysis suggests that SL makes a larger magnitude of conformational changes in OA at acidic pH compared to alkaline pH.
Published Version
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