Elucidation of the relationship between milk protein-stevioside interactions and interfacial layer properties based on multi-spectroscopy and interfacial rheology

Food Chem. 2024 Dec 16:468:142512. doi: 10.1016/j.foodchem.2024.142512. Online ahead of print.

Abstract

The intricate interactions between stevioside (STE) and milk protein (mixtures of whey protein isolate and sodium caseinate, WPI/SC) as well as interfacial stabilization mechanisms were investigated. At the molecular scale, it was observed that the incorporation of the steviol hydrophobic skeleton enhanced the surface hydrophobicity of WPI/SC (from 1560.73 to 2175.63), favoring the reduction of the energy barrier for adsorption. At the mesoscopic scale, the analysis of adsorption kinetics and interfacial dilatational rheological response revealed that STE and WPI/SC had a synergistic effect on the attenuation of oil-water interfacial tension, with the lowest value of interfacial tension of 9.46 mN/m. Meanwhile, at low concentrations of STE, the WPI/SC-STE complexes unfolded and self-assembled at the interface to form a spring-like interfacial layer that relaxed in response to external deformation. In contrast, at high concentrations of STE, it gradually replaced WPI/SC-STE complexes at the interface and destabilized the interfacial layer.

Keywords: Interfacial dilatational rheology; Lissajous plots; Non-covalent interaction; Oil-water interface; Spring-like interfacial layer; Stevioside.