Extractable low mass proteins <30Â kDa from peanut display elevated antigenicity (IgG-binding) and allergenicity (IgE-binding) in vitro and are attenuated by thermal reactivity with non-peanut food ingredients

Human allergic reactions to peanut proteins and the associated risk of life-threatening anaphylaxis requires vigilant management of peanuts in food processing. Processed forms of peanuts with attenuated antigenicity and less severe immunogenic responses may lower the risk. Molecular subfractions of raw (UP), blanched (BP) and roasted (RP) peanuts were prepared including water-insoluble (P1), water-soluble high mass (>30 kDa, P2) and water-soluble low mass (<30 kDa, P3) fractions. Products were screened by measuring binding to IgG (polyclonal antibody against peanut allergen) and IgE (sera from peanut-allergic donors, RAST > 3). The results showed that IgE titres were highest for total extracts of RP, particularly for P3 fractions of UP and RP, and were affected by further heating. Antigenicity was also modulated by heating in the presence of either peanut oil or non-peanut food ingredients (lactose, coconut oil). Results support several alternative methods for regulating peanut antigenicity using food processing approaches but require further substantiation in larger numbers of allergic and control donor sera.