Impacts of hesperidin on whey protein functionality: Interacting mechanism, antioxidant capacity, and emulsion stabilizing effects

Abstract

The objective of this work was to explore the possibility of improving the antioxidant capacity and application of whey protein (WP) through non-covalent interactions with hesperidin (HES), a citrus polyphenol with nutraceutical activity. The interaction mechanism was elucidated using several spectroscopic methods and molecular docking analysis. The antioxidant capacity of the WP-HES complexes was analyzed and compared to that of the proteins alone. Moreover, the resistance of oil-in-water emulsions formulated using the WP-HES complexes as antioxidant emulsifiers to changes in environmental conditions (pH, ion strength, and oxidant) was evaluated. Our results showed that HES was incorporated into a single hydrophobic cavity in the WP molecule, where it was mainly held by hydrophobic attractive forces. As a result, the microenvironments of the non-polar tyrosine and tryptophan residues in the protein molecules were altered after complexation. Moreover, the α-helix and β-sheet regions in the protein decreased after complexation, while the β-turn and random regions increased. The antioxidant capacity of the WP-HES complexes was greater than that of the proteins alone. Non-radiative energy transfer from WP to HES was detected during complex formation. Compared to WP alone, the WP-HES complexes produced emulsions with smaller mean droplet diameters, exhibited higher pH and salt stability, and had better oxidative stability. The magnitude of these effects increased as the HES concentration was increased. This research would supply valuable information on the nature of the interactions between WP and HES. Moreover, it may lead to the creation of dual-function antioxidant emulsifiers for application in emulsified food products.

Enhancing Antioxidant Retention through Varied Wall Material Combinations in Grape Spray Drying and Storage

“…Our exploration revealed hesperidin’s exclusive presence within the whey treatment, hinting at potential interactions with whey proteins that augment its stability or encapsulation efficiency [ 39 ]. This could emanate from hydrophobic interactions or hydrogen bonding, culminating in a robust matrix that is able to withstand the rigors of spray drying.…”

Physicochemical Properties of Nanoliposomes Encapsulating Grape Seed Tannins Formed with Ultrasound Cycles

“…Despite their high antioxidant capacity, the incorporation of tannins into food is restricted due to their interaction with salivary proline, leading to an unpleasant astringent taste [13]. While the interaction mechanism of tannins with salivary proteins has been extensively investigated [14][15][16], their interaction with lipids has yet to be explored and is mainly limited to studies involving emulsions [17,18]. Nanoliposomes emerge as a promising solution for encapsulating tannins, preventing undesired reactions and enabling the introduction of the active ingredient into food without compromising flavor.…”