Microwave-assisted extraction enhances the epicatechin and bovine serum albumin the interaction by inducing protein...

This study evaluated the effects of microwave-assisted extraction (MAE) on the structure of bovine serum albumin (BSA) in its interaction with epicatechin (EC). The results showed that EC spontaneously bound to BSA via static quenching, primarily driven by hydrophobic interactions. Low temperature MAE at 298 K decreased the stability of the EC-BSA complex, Ksv and Kb, and reduced binding affinity by weakening single binding site mode. Moreover, MAE significantly declined the α-helix content and increased β-sheet, β-turn, random coil, and carbonyl group content in BSA, thereby changing structural properties and enhancing structural disorder of BSA. In summary, low temperature MAE exhibited some regularity in influencing the binding interaction between BSA and EC and could induce conformational changes of BSA. This suggested that low temperature MAE might provide an important theoretical basis for selectively regulating protein conformation and potential physiological functions by modulating the interactions between phenolic compounds and proteins.