Interaction between the Polyphenols from Pinus koraiensis Seeds Scales and Whey Protein Studied by Fluorescence and Ultraviolet Spectroscopy
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Abstract:
The interaction between the polyphenols from Pinus koraiensis seed scales and whey protein and associated modes of action were studied by ultraviolet-visible absorption spectroscopy and fluorescence spectroscopy. The analysis by ultraviolet-visible absorption spectroscopy revealed that the polyphenols from Pinus koraiensis seed scales interacted with whey protein and yielded new complexes, which also changed the microenvironment surrounding the spatial structures of the aromatic residues of proteins, and induced the conformational change of whey protein. The fluorescence spectroscopy analysis showed that the polyphenols had a strong fluorescence quenching effect on the whey protein, and the quenching type belonged to the static quenching of the formed complexes. The apparent binding constants (KA) of their interactions at different temperatures were calculated as: 1.111 × 104 L/mol (25 ℃), 2.201 × 104 L/mol (30 ℃), 6.206×104 L/mol (35 ℃), and the corresponding number of the binding sites (n) were 0.885, 0.937 and 1.043, respectively. The analysis of thermodynamic parameters revealed that the interaction between the polyphenols from Pinus koraiensis seed scales and whey protein was an endothermic process, and the main interactive force was hydrophobic interaction.
