Abstract
Several investigations have revealed the ability of phenolic compounds to form complexes with proteins and change their conformation. In the present paper, the interaction between trypsin and ellagic acid is studied using several techniques. The absorption investigation suggested an interaction between trypsin and ellagic acid. The fluorescence study illustrated that the hydrogen bonds and Van der Waals forces have a role in the static complex formation between trypsin and Ellagic acid (EA). On the other hand, the thermal stability study indicated that the trypsin-EA interaction could lead to a higher Tm point (47.5 to 52.5 °C) and stability for the enzyme. Based on the CD analysis, the α-helix and β-sheet percent changed after joining with ellagic acid. Ellagic acid showed an uncompetitive role in the trypsin function in the kinetic analysis. Finally, the molecular docking and simulation investigations confirmed the structural and functional alterations in the trypsin structure obtained in the spectroscopic study. The results of this study help shed more light on the trypsin behavior against the phenolic compound, especially ellagic acid.
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