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Title: Stability and Immunogenicity of Hypoallergenic Peanut Protein-Polyphenol Complexes During In Vitro Pepsin Digestion

Author
item PLUNDRICH, NATHALIE - North Carolina State University
item WHITE, BRITTANY - Former ARS Employee
item Dean, Lisa
item DAVIS, JACK - Jla Global
item FOEGEDING, EDWARD - North Carolina State University
item LILA, MARYANN - North Carolina State University

Submitted to: Food & Function
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 5/18/2015
Publication Date: 5/26/2015
Citation: Plundrich, N.J., White, B.L., Dean, L.L., Davis, J.P., Foegeding, E.A., Lila, M.A. 2015. Stability and Immunogenicity of Hypoallergenic Peanut Protein-Polyphenol Complexes During In Vitro Pepsin Digestion. Food & Function. Ill:28. doi: 10.1039/c5fo00162e 6:2145-2154.

Interpretive Summary: Allergic reactions from eating peanuts is due to the activity of peanut proteins such as Ara h 2 and Ara h 3. When certain fruit juices and teas containing high levels of polyphenols are mixed with flour made by removing the fat from roasted peanuts, these proteins are bound up with the polyphenols and their ability to cause an allergic reaction should be lessened. When ingested, the treated peanut flours are subjected to enzymes in the stomach such as pepsin. These enzymes could break the bonds between the peanut proteins and the polyphenols. This study found that proteins complexed to the polyphenols were less broken down than the uncomplexed peanut proteins lessening their potential for causing allergic responses.

Technical 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.