Abstract
Whey proteins and oligomeric proanthocyanidins have nutritional value and are widely used in combination as food supplements. However, the effect of the interactions between proanthocyanidins and whey proteins on their stability has not been studied in depth. In this work, we aimed to characterize the interactions between β-Lactoglobulin (β-LG) and α-lactalbumin (α-LA) and oligomeric proanthocyanidins, including A1, A2, B1, B2, B3, and C1, using multi-spectroscopic and molecular docking methods. Fluorescence spectroscopic data revealed that all of the oligomeric proanthocyanidins quenched the intrinsic fluorescence of β-LG or α-LA by binding-related fluorescence quenching. Among the six oligomeric proanthocyanidins, A1 showed the strongest affinity for β-LG (Ka = 2.951 (±0.447) × 104 L∙mol−1) and α-LA (Ka = 1.472 (±0.236) × 105 L∙mol−1) at 297 K. β-LG/α-LA and proanthocyanidins can spontaneously form complexes, which are mainly induced by hydrophobic interactions, hydrogen bonds, and van der Waals forces. Fourier-transform infrared spectroscopy (FTIR) and circular dichroism spectroscopy showed that the secondary structures of the proteins were rearranged after binding to oligomeric proanthocyanidins. During in vitro gastrointestinal digestion, the recovery rate of A1 and A2 increased with the addition of WPI by 11.90% and 38.43%, respectively. The addition of WPI (molar ratio of 1:1) increased the retention rate of proanthocyanidins A1, A2, B1, B2, B3, and C1 during storage at room temperature by 14.01%, 23.14%, 30.09%, 62.67%, 47.92%, and 60.56%, respectively. These results are helpful for the promotion of protein–proanthocyanidin complexes as functional food ingredients in the food industry.
Highlights
Proanthocyanidins are condensed polyphenol polymers of monomeric flavan-3-ols, and they are widely found in fruits, berries, nuts, and seeds [1]
Maintaining the stability of proanthocyanidins during processing, storage, and gastrointestinal digestion to maximize their nutritional value is of great importance
This study aimed to characterize the interactions between β-LG or α-LA and six types of oligomeric proanthocyanidins (B1, B2, B3, A1, A2, and C1, Figure S1) by using multispectroscopic and molecular docking methods
Summary
Proanthocyanidins are condensed polyphenol polymers of monomeric flavan-3-ols, and they are widely found in fruits, berries, nuts, and seeds [1]. C1 have received considerable attention because of their abundance in plants. These proanthocyanidins, with a degree of polymerization of no more than three, have great potential as functional foods. They may penetrate the intestinal wall and can be detected in human plasma [5]. Proanthocyanidins are unstable in the alkaline environment of intestine [8], which limits their healthful function in vivo. Food proanthocyanidins can be damaged by high temperature, oxygen, and irradiation during processing or storage [7]. Maintaining the stability of proanthocyanidins during processing, storage, and gastrointestinal digestion to maximize their nutritional value is of great importance
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