Physicochemical Characterization of Interactions between Blueberry Polyphenols and Food Proteins from Dairy and Plant Sources

Bianca Chima, Paul Mathews, Scott Morgan, Sarah A Johnson, Charlene B Van Buiten, Bianca Chima, Paul Mathews, Scott Morgan, Sarah A Johnson, Charlene B Van Buiten

Abstract

Polyphenols are widely known for their benefits to human health; however, dietary intake of this class of compounds is low in the United States due to low intake of fruits and vegetables. Dairy foods (i.e., milk, yogurt) have been shown to increase polyphenol bioavailability via protein-polyphenol interactions, which may have important implications for human health. Increasing consumer interest in sustainability and health has led to the introduction of a variety of novel plant-based proteins and related food products as dairy alternatives. This study compared whey, a popular dairy-based food protein, to pea and hemp proteins for their abilities to form complexes with polyphenols from blueberries, which are a widely consumed fruit in the US with demonstrated health effects. Physical and chemical characteristics of each protein extract in the presence and absence of blueberry polyphenols were investigated using a variety of spectroscopic methods. The influence of polyphenol complexation on protein digestion was also assessed in vitro. While all proteins formed complexes with blueberry polyphenols, the hemp and pea proteins demonstrated greater polyphenol binding affinities than whey, which may be due to observed differences in protein secondary structure. Polyphenol addition did not affect the digestion of any protein studied. Solution pH appeared to play a role in protein-polyphenol complex formation, which suggests that the effects observed in this model food system may differ from food systems designed to mimic other food products, such as plant-based yogurts. This study provides a foundation for exploring the effects of plant-based proteins on phytochemical functionality in complex, "whole food" matrices, and supports the development of plant-based dairy analogs aimed at increasing polyphenol stability and bioavailability.

Keywords: digestion; plant-based; polyphenol; protein; protein–polyphenol interaction; whey.

Conflict of interest statement

The authors declare no conflict of interest.

Figures

Figure 1
Figure 1
Intermolecular interactions between contents of commercial protein powders and powdered blueberries cause the formation of insoluble complexes. (A) Increasing turbidity of commercial protein solutions by blueberry powder points to nutrient interactions. Increases in turbidity exceed absorbance of blueberry-only control (A600 = 0.027). Values are expressed as mean ± SD. Asterisks (*) indicate significant differences (*** = p ≤ 0.001, **** = p ≤ 0.0001) based on two-way ANOVA with Tukey’s multiple comparisons. (B) Molecular weight profiles of each commercial protein powder in the absence or presence of powdered blueberries. Molecular weight is represented as kilodaltons (kDa).
Figure 2
Figure 2
Protein–polyphenol interactions driving increases in turbidity are pH-dependent. Values are expressed as mean ± SD. Different letters indicate significant differences (p < 0.05) based on two-way ANOVA with Tukey’s multiple comparisons.
Figure 3
Figure 3
Quenching of protein isolates by BPE. Fluorescence emission spectra (A) whey, (B) pea and (C) hemp as a function of BPE concentration. (D) Stern-Volmer plot of F0/F as a function of BPE for each protein isolate. (E) Double-log Modified Stern-Volmer plot.
Figure 4
Figure 4
Structural analysis of protein isolates in the presence and absence of BPE at pH 6.8. (A) Far-UV spectra of all proteins demonstrate differences in secondary structure between all proteins, but no change upon the addition of BPE. (B) Near-UV spectra suggest that all proteins do not have tertiary structure. (C) Calculation of relative helicity reveals the helical conformation of whey and hemp, but not pea protein. Helicity is not affected by the addition of BPE. Values are expressed as mean ± SD. Different letters indicate significant differences (p < 0.05) based on two-way ANOVA with Tukey’s multiple comparisons.
Figure 5
Figure 5
Comparison of free amino acids in solution before and after in vitro digestion in the presence or absence of BPE. Data are expressed as mM leucine equivalents as determined by a standard curve. Values are expressed as mean ± SD. Asterisks (*) indicate significant differences (** = p ≤ 0.01, *** = p ≤ 0.001, **** = p ≤ 0.0001) based on two-way ANOVA with Šídák’s multiple comparisons.

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