Abstract
The processing stability and antioxidant capacity of blueberry anthocyanins (ANs) in the presence of whey protein isolate (WPI) were examined. WPI was found to enhance both the stability and antioxidant activity of ANs during processing and simulated in vitro digestion, especially at a concentration of 0.15 mg·mL−1. Fluorescence and ultraviolet-visible absorption spectroscopy showed that ANs were primarily stabilized by hydrophobic forces between WPI and malvidin-3-O-galactoside (M3G), the major anthocyanin monomer. Circular dichroism and Fourier-transform infrared spectroscopy confirmed that the structure of WPI changed and the microenvironments of certain amino acid residues were modulated by non-covalent binding to M3G; furthermore, fewer α-helices and more β-sheets were formed. Molecular docking studies revealed that WPI, especially immunoglobulin (IgG), contributed the most to ANs stability via hydrogen bonds and hydrophobic forces according to molecular docking scores (−141.30 kcal/mol). These results provided an important fundamental basis for improving the stabilities of ANs in milk systems.
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