cyanidin-3-o-beta-glucopyranoside and casein-hydrolysate

The interaction between cyanidin-3-O-glucoside with casein and casein hydrolysates and its effects on the antioxidant activity of complexes were investigated. Fluorescence spectroscopy results indicated that the interaction between cyanidin-3-O-glucoside and casein was primarily mediated by Van der Waals forces or hydrogen bonds and stronger than the interaction between cyanidin-3-O-glucoside and casein hydrolysates mainly via hydrophobic interaction. Circular dichroism and Fourier-transform infrared spectroscopy analysis showed the secondary structure of casein/casein hydrolysates had a slight change after binding with cyanidin-3-O-glucoside. And larger particles formed due to the protein aggregation induced by the complexation of casein/casein hydrolysates with cyanidin-3-O-glucoside. The antioxidant activity assessments revealed that the synergistic effect was observed in FRAP assay, whereas an antagonistic effect in ABTS assay between casein/casein hydrolysates and cyanidin-3-O-glucoside, which were produced due to the casein/casein hydrolysates-cyanidin-3-O-glucoside interaction. These results would be helpful in designing functional beverages containing anthocyanins and protein hydrolysates with enhanced antioxidant ability.

Topics: Anthocyanins; Antioxidants; Caseins; Circular Dichroism; Glucosides; Hydrogen Bonding; Hydrophobic and Hydrophilic Interactions; Protein Structure, Secondary; Spectrometry, Fluorescence; Spectroscopy, Fourier Transform Infrared