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Moreover, the changes in interactions between protein and anthocyanin can greatly influence the stability and functional performance of anthocyanin under different processing conditions (e.g., pressure, temperature, and pH). Hydrogen bonds, hydrophobic interactions, ionic interactions, and van der Waals forces are the main driving forces contributing to this complex’s formation. Among these, the binding of protein and anthocyanin has been studied extensively due to their high safety and abundant sources, as well as precise available chemical structures and high-reliability application techniques. Molecular dynamic simulation and docking analyses revealed that the binding site of the complex did not change under different processing conditions, but the solvent-accessible surface area varied under different conditions.Ī growing number of studies focusing on improving the stability of anthocyanin have been published in recent years these studies have indicated that chemical modification, copigmentation interaction (the interaction of anthocyanin and other pigments and cofactors, such as polyphenols, organic acids, nucleotides, and metal ions ), and the interaction with food macromolecules, such as starch, polysaccharide and protein, can all increase the stability of anthocyanin. Both HPP and thermal treatments increased the random coil content and showed limited effects on the α-helix and β-sheet contents of α-La and caused the aggregation of the complex to varying degrees. The results indicated that the thermal treatments significantly increased the quenching constants of the complex at pH 7.4/8.0 and 60/80 ☌, as well as the accessible fraction of protein at pH 8.0/80 ☌.
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The methods of circular dichroism spectroscopy, fluorescence quenching, dynamic light scattering, and molecular simulation were used to characterize the effects of processing-induced changes in protein structure, size distribution, binding site conformation, and residue charges on their binding characteristics between them. In this study, high pressure processing (HPP) and thermal treatment were comparatively evaluated by examining their impacts on the binding behavior and interaction between α-lactalbumin (α-La) and pelargonium-3-glucoside (P3G) under pH values of 6.0, 7.4, and 8.0.
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