Molecular dynamics simulation and in vitro digestion to examine the impact of theaflavin on the digestibility and structural properties of myosin

In this study, the interaction mechanism between theaflavin and myosin was explored to confirm the potential application of theaflavin in the meat protein system. A series of theaflavin and myosin solutions were prepared for spectroscopic studies. Spectroscopy results showed that theaflavins formed complexes with myosin and affected the microenvironment of myosin. And that addition of theaflavin cause static quenching of the myosin solution. Theaflavin and bovine myosin combined through hydrophobic interaction to form a complex, and gradually increasing the temperature was conducive to the binding of theaflavin and bovine myosin. This interaction results in a decrease in the α -helix content of myosin. Molecular dynamics simulation results confirmed that hydrophobic interactions and hydrogen bonds made the protein structure more compact and stable. And the in vitro digestion process was simulated. The results showed that the addition of theaflavin could significantly reduce the digestibility of myosin.