|PLUNDRICH, NATHALIE - North Carolina State University|
|KULIS, MIKE - University Of North Carolina|
|GRACE, MARY - North Carolina State University|
|GUO, RISHU - University Of North Carolina|
|BURKS, A - University Of North Carolina|
|LILA, MARY - North Carolina State University|
Submitted to: Journal of Agricultural and Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 4/23/2014
Publication Date: 4/23/2014
Publication URL: http://DOI 10.1021/jf405773b
Citation: Plundrich, N.J., Kulis, M., White, B.L., Grace, M.H., Guo, R., Birls, A.W., Davis, J.P., Lila, M.A. 2014. Novel Strategy to Create Hypoallergenic Peanut Protein. Journal of Agricultural and Food Chemistry. 2014: 140502094247005.
Interpretive Summary: Chemical compounds called polyphenols are responsible for some of the health effects of fruits and vegetables. These compounds are also know to bind proteins. Proteins in foods such as peanuts are responsible for the reactions that are often severe in persons who are allergic. The polyphenols from fruits such as cranberries can be used to bind the peanut proteins when juices from the fruits are added to flours made by removing the fat from peanuts. These polyphenol fortified flours were found to lessen, but not eliminate the reactions that peanut allergy sufferers have when fed to peanut allergic mice and when added to a chemical test using human blood. This change was attributed to changes in protein structure that occur in the peanut making the specific sites of the allergy triggers unavailable for binding.
Technical Abstract: Peanut allergy is an IgE-mediated hypersensitivity. Upon peanut consumption by an allergic individual, epitopes on peanut proteins bind and cross-link peanut-specific IgE on mast cell and basophil surfaces triggering the cells to release inflammatory mediators responsible for allergic reactions. Polyphenolic phytochemicals have high affinity to bind proteins and form soluble and insoluble complexes with unique functionality. This study investigated the allergenicity of polyphenol-fortified peanut matrices prepared by complexing various polyphenol-rich plant juices and extracts with peanut flour. Polyphenol-fortified peanut matrices reduced IgE binding to one or more peanut allergens (Ara h 1, Ara h 2, Ara h3, and Ara h 6). Attenuated total reflectance-Fourier transform infrared spectroscopy (ATR-FTIR) suggested changes in secondary protein structure. Peanut protein-cranberry polyphenol fortified matrices triggered significantly less basophil degranulation than unmodified flour in an ex vivo assay using human blood and less mast cell degranulation when used to orally challenge peanut-allergic mice. Polyphenol fortification of peanut flour resulted in a hypoallergenic matrix with reduced IgE binding and degranulation capacity, likely due to changes in protein secondary structure or masking of epitopes, suggesting potential application for oral immunotherapy.