Stability and immunogenicity of hypoallergenic peanut protein–polyphenol complexes during in vitro pepsin digestion

Abstract

Allergenic peanut proteins are relatively resistant to digestion, and if digested, metabolized peptides tend to remain large and immunoreactive, triggering allergic reactions in sensitive individuals. In this study, the stability of hypoallergenic peanut protein-polyphenol complexes was evaluated during simulated in vitro gastric digestion. When digested with pepsin, the basic subunit of the peanut allergen Ara h 3 was more rapidly hydrolyzed in peanut protein-cranberry or green tea polyphenol complexes compared to uncomplexed peanut flour. Ara h 2 was also hydrolyzed more quickly in the peanut protein-cranberry polyphenol complex than in uncomplexed peanut flour. Peptides from peanut protein-cranberry polyphenol complexes and peanut protein-green tea polyphenol complexes were substantially less immunoreactive (based on their capacity to bind to peanut-specific IgE from patient plasma) compared to peptides from uncomplexed peanut flour. These results suggest that peanut protein-polyphenol complexes may be less immunoreactive passing through the digestive tract in vivo, contributing to their attenuated allergenicity.

Peanut Allergy: Characteristics and Approaches for Mitigation

“…Besides IgE epitopes, protein structure also plays a critical role and functions in the allergenic potential of proteins (Chruszcz et al, 2011, Nesbit et al, 2012, Dyer et al, 2018Maleki, Kopper et al, 2000;Maleki et al, 2003, Maleki, 2004, Maleki & Hurlburt, 2004. Therefore, the alteration in allergen structure subsequently alters its physicochemical properties such as solubility and digestibility, which in turn plays a significant role in altering the immunoreactivity (Apostolovic et al, 2013;Mikiashvili & Yu, 2018;Plundrich et al, 2015;Szymkiewicz & Jędrychowski, 2009;Vanga et al, 2016). The degree of alteration of allergens depends on the types and conditions of processing.…”

Influence of peanut matrix on stability of allergens in gastric‐simulated digesta: 2S albumins are main contributors to the IgE reactivity of short digestion‐resistant peptides

“…Only 2 studies have dealt with peanut protein digestibility within their real food matrix. Plundrich et al investigated digestibility of light‐roasted peanut flour (12% fat) by pepsin and monitored degradation of allergens using 1‐dimensional sodium dodecyl sulphate polyacrylamide gel electrophoresis (1D SDS‐PAGE). The study of Di Stasio et al investigated digestibility of proteins from the whole peanut by complete oral‐gastric‐intestinal‐brush border membrane proteases, but it did not report the gastric digestion products.…”

Protein-bound polyphenols create “ghost” band artifacts during chemiluminescence-based antigen detection

“…The phenomenon was also observed with other aggregate particles including whey protein isolate-green tea polyphenol and whey protein isolate-blueberry polyphenol aggregate particles (see Figure S1) indicating that “ghosting” was not dependent on specific EWPs. “Ghost” bands also occurred on a few blots in our previously published work, however, this did not affect data interpretation 3, 9 . The same treatments were re-tested by fluorescence-based Western blotting and the data was consistent with that previously reported.…”