β-Casein, a highly amphiphilic calcium-sensitive phosphoprotein, has specific features that promote its application as a nanocarrier for hydrophobic bioactives. Luteolin is a flavonoid with rich biological activities existing in vegetables and fruits. It is important to understand the interaction of β-casein with luteolin for the development of β-casein-based delivery systems. Here, the interaction mode between luteolin and β-casein was investigated with multispectral techniques, computer simulation, and biological methods. The results demonstrated that luteolin could bind to β-casein spontaneously which is driven by hydrophobic interactions and statically quench the intrinsic fluorescence of β-casein. Molecular docking and molecular dynamics simulation showed that β-casein formed a stable complex with luteolin. It could be concluded that luteolin was encapsulated in β-casein micelles and exhibited higher antioxidant activity than luteolin alone. These results would be helpful to understand the interaction mechanism of luteolin with β-casein and indicated that β-casein micelles were very promising as delivery vehicles for luteolin. PRACTICAL APPLICATIONS: Adding bioactive compounds to food is an efficient method of functional food processing, and protein is an excellent natural carrier for these substances. β-Casein is a milk protein with a unique amphiphilic structure that makes it a natural nanocarrier for active ingredients. This study created β-casein nanocarriers and encapsulated luteolin based on the interaction mechanism between β-casein with luteolin. Luteolin encapsulated in β-casein micelles demonstrated higher antioxidant activity when compared to free luteolin. This research will provide useful data for the development of functional foods based on β-casein and luteolin in the food industry.
Keywords: computer simulations; fluorescence quenching; luteolin; nanocarrier; self-assembly; β-casein.
© 2022 Wiley Periodicals LLC.