Exploring the noncovalent interaction between β-lactoglobulin and flavonoids under nonthermal process: Characterization, physicochemical properties, and potential for lycopene delivering.

ABSTRACT: The poor structure stability and low bioavailability of lycopene (LY) hampers the wide application in food field. Thus, it is crucial to explore novel deliver carrier for LY based on protein-flavonoid complexes. In this study, the noncovalent interaction mechanism between β-lactoglobulin (β-LG) and flavonoids (apigenin (API), luteolin (LUT), myricetin (MY), apigenin-7-O-glucoside, luteolin-7-O-glucoside, and myricetrin) under ultrasound treatment was explored. Results revealed that ultrasound treatment promoted reactive groups exposure and structural unfolding of β-LG to interact with six flavonoids. The main driving force between β-LG and flavonoids was hydrophobic interaction. The docking result showed that the preferred binding site for these flavonoids was on the outer surface of β-LG.

SUBMITTER: Song G 

PROVIDER: S-EPMC11773077 | biostudies-literature | 2025 Jan

REPOSITORIES: biostudies-literature