Abstract
The interaction mechanism of whey proteins with theaflavin (TF1) in black tea was analyzed using multi-spectroscopy analysis and molecular docking simulations. The influence of TF1 on the structure of bovine serum albumin (BSA), β-lactoglobulin (β-Lg), and α-lactoalbumin (α-La) was examined in this work using the interaction of TF1 with these proteins. Fluorescence and ultraviolet-visible (UV-vis) absorption spectroscopy revealed that TF1 could interact with BSA, β-Lg and α-La through a static quenching mechanism. Furthermore, circular dichroism (CD) experiments revealed that TF1 altered the secondary structure of BSA, β-Lg and α-La. Molecular docking demonstrated that the interaction of TF1 with BSA/β-Lg/α-La was dominated by hydrogen bonding and hydrophobic interaction. The binding energies were -10.1 kcal mol(-1), -8.4 kcal mol(-1) and -10.4 kcal mol(-1), respectively. The results provide a theoretical basis for investigating the mechanism of interaction between tea pigments and protein. Moreover, the findings offered technical support for the future development of functional foods that combine tea active ingredients with milk protein. Future research will focus on the effects of food processing methods and different food systems on the interaction between TF1 and whey protein, as well as the physicochemical stability, functional characteristics, and bioavailability of the complexes in vitro or in vivo.