Boiling and frying peanuts decreases soluble peanut (Arachis Hypogaea) allergens Ara h 1 and Ara h 2 but does not generate hypoallergenic peanuts

Authors: COMSTOCK, SARA - University Of Michigan; Maleki, Soheila; TEUBER, SUZANNE - University Of California

Submitted to: PLOS ONE
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 6/6/2016
Publication Date: 6/16/2016
Citation: Comstock, S.S., Maleki, S.J., Teuber, S.S. 2016. Boiling and frying peanuts decreases soluble peanut (Arachis Hypogaea) allergens Ara h 1 and Ara h 2 but does not generate hypoallergenic peanuts. PLoS One. doi:10.1371/journal.pone.0157849.

Interpretive Summary: Peanut allergy continues to be a problem in most developed countries of the world. We sought a processing method that would alter allergenic peanut proteins, such that allergen recognition by IgE from allergic individuals would be significantly reduced or eliminated. Such a method would render accidental exposures to trace amounts of peanuts safer. A combination of boiling and frying decreased recovery of Ara h 1 and Ara h 2. In contrast, treatment with high pressures under varying temperatures had no effect on protein extraction profiles. Antibodies specific for Ara h 1, Ara h 2, and Ara h 6, the major peanut allergens, bound proteins extracted from raw samples but not in boiled/fried samples. However, boiled/fried extracts were able to prevent serum immunoglobulin E (IgE, an allergen specific antibody) from binding to raw peanut. Thus, this method of processing is unlikely to generate a peanut product tolerated by peanut allergic patients. Importantly, variability in individual patients' IgE repertoires may mean that some patients' IgE would bind fewer polypeptides in the sequentially processed seed.

Technical Abstract: Peanut allergy continues to be a problem in most developed countries of the world. We sought a processing method that would alter allergenic peanut proteins, such that allergen recognition by IgE from allergic individuals would be significantly reduced or eliminated. Such a method would render accidental exposures to trace amounts of peanuts safer. A combination of boiling and frying decreased recovery of Ara h 1 and Ara h 2 at their expected MWs. In contrast, treatment with high pressures under varying temperatures had no effect on protein extraction profiles. Antibodies specific for Ara h 1, Ara h 2, and Ara h 6 bound proteins extracted from raw samples but not in boiled/fried samples. However, pre-incubation of serum with boiled/fried extract removed most raw peanut-reactive IgE from solution, including IgE directed to Ara h 1 and 2. Thus, this method of processing is unlikely to generate a peanut product tolerated by peanut allergic patients. Importantly, variability in individual patients' IgE repertoires may mean that some patients' IgE would bind fewer polypeptides in the sequentially processed seed.