The phytochemical composition and physicochemical attributes of polyphenol-enriched protein particle ingredients produced with pulse proteins (e.g. chickpea protein, pea protein, and a chickpea-pea protein blend) and polyphenols recovered from wild blueberry pomace were investigated for colloidal and interfacial properties. Anthocyanins were the major polyphenol fraction (27.74-36.47 mg C3G/g) of these polyphenol-rich particles (44.95-62.08 mg GAE/g). Dispersions of pea protein-polyphenol particles showed a superior phase stability before and after heat treatment compared to the chickpea pea protein-polyphenol system. This observation was independent of the added amount of NaCl in the dispersion. In general, at quasi equilibrium state, pulse protein-polyphenol particles and parental pulse protein ingredients showed similar oil-water interfacial tension. However, pea protein-polyphenol particles demonstrated a reduced diffusion-driven oil-water interfacial adsorption rate constant compared to the parental pea protein ingredient. Overall, the obtained results suggest application potential of pea protein-polyphenol particles as a functional food/beverage ingredient.

BACKGROUND: The use of rutin in the food industry is limited by its poor solubility. Encapsulation can be used as an effective way to improve polyphenol solubility. Proteins with high safety, biocompatibility and multiple binding sites are known as the most promising encapsulating carriers. Therefore, the improvement of rutin solubility by pH-driven encapsulation of rutin in soy protein isolate (SPI) nanoparticles, as well as the form of rutin after encapsulation and rutin-protein binding index were investigated.
RESULTS: SPI had a high encapsulation efficiency (87.5%) and loading amount (10.6%) for rutin. When the mass ratio of protein to rutin was 5:1, the highest concentration of rutin in solution was 3.27 g L-1 , which was a 51.57-fold increase compared to the original rutin. At this situation, rutin transformed from crystalline to amorphous form. During the formation of nanoparticles, SPI was in a dynamic change of unfolding and refolding. Rutin deprotonated in alkaline conditions increasing its solubility and bound to protein to form nanoparticles during the process of returning to neutral. Hydrophobic interactions and hydrogen bonding promoted the formation of the nanoparticles and there were at least 1-2 binding sites between rutin and each SPI molecule.
CONCLUSIONS: The results suggested that encapsulation of rutin in protein nanoparticles can effectively increase the solubility of rutin. This study may provide important information for the effective utilization of polyphenol functional foods. © 2023 Society of Chemical Industry.

Antigen detection during Western blotting commonly utilizes a horseradish peroxidase-coupled secondary antibody and enhanced chemiluminescent substrate. We utilized this technique to examine the impact of green tea-derived polyphenols on the binding of egg white protein-specific IgE antibodies from allergic human plasma to their cognate antigens. Our experiments unexpectedly showed that green tea-derived polyphenols, when stably complexed with egg white proteins, caused hyperactivation of horseradish peroxidase resulting in the appearance of white \"ghost\" bands. This study suggests that caution should be taken when evaluating polyphenol-bound proteins by enhanced chemiluminescence Western blotting using horseradish peroxidase and demonstrates that protein-bound polyphenols can be a source of \"ghost\" band artifacts on Western blots.