Insight into binding mechanism between three whey proteins and mogroside V by multi-spectroscopic and silico methods: Impacts on structure and foaming properties

In this work, the interaction mechanism, structure and foaming properties between three whey proteins (α-lactalbumin (ALa), β-lactoglobulin (BLg) and bovine serum albumin (BSA)) and Mogroside V (Mog) at pH 7.0 were systematically formulated via multi-spectroscopic analysis and silico methods. Mog quenched the fluorescence of three whey proteins in a static mode. Mog had greater binding affinity for ALa than that for BLg or BSA. Hydrogen bonds, van der Waals force and hydrophobic interaction acted as the primary driven forces in ALa/BLg/BSA-Mog system. Moreover, content of α-helix in ALa and β-sheet in BLg decreased after Mog addition, whereas there was no significant change in the secondary structure of BSA. In addition, hydrophobic crevice in ALa, “bottom of β-barrel” in BLg and interfacial region between two domains in BSA were the binding areas for Mog using molecular docking. Molecular dynamics (MD) simulation further demonstrated that the complex of ALa and Mog possessed the lowest binding free energy and most stable state. Furthermore, compared with single proteins, the foaming ability of protein/Mog complexes were improved. Especially, Ala-Mog attained the highest increase rate. Bubble morphology presented that three whey proteins containing Mog possessed compacter, smaller and even bubbles. This research could establish theoretical basis for the binding mechanism between different food proteins and low weight surfactants. Besides, whey protein-saponin complexes could be served as the novel food-grade foaming agents applied in food industry. [Display omitted] •Binding method of mogroside V (Mog) with three whey protein was static quenching mode.•Binding constant with Mog was in the sequence of ALa > BLg > BSA.•ALa/Mog complex was more stable than BLg/Mog or BSA/Mog via molecular dynamics.•Foaming properties of three whey protein was increased in the presence of Mog.