Effect of Heating and Glycation on the Allergenicity of 2S Albumins (Ara h 2/6) from Peanut

Y.M. Vissers, F. Blanc, P. Stahl Skov, P.E. Johnson, N.M. Rigby, L. Przybylski-Nicaise, H. Bernhard, J.M. Wal, B. Ballmer-Weber, L. Zuidmeer-Jongejan, Z. Szepfalusi, J. Ruinemans-Koerts, A.P.H. Jansen, H.F.J. Savelkoul, H.J. Wichers, A.R. Mackie, E.N.C. Mills, K. Adel-Patient

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74 Citations (Scopus)


Background Peanut allergy is one of the most common and severe food allergies, and processing is known to influence the allergenicity of peanut proteins. We aimed to establish the effect of heating and glycation on the IgE-binding properties and biological activity of 2S albumins (Ara h 2/6) from peanut. Methodology/Principal Findings Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in the presence or absence of glucose. Ara h 2 and 6 were also purified from roasted peanut. Using PBMC and sera from peanut-allergic patients, the cellular proliferative potency and IgE reactivity (reverse EAST inhibition) and functionality (basophil degranulation capacity) of allergens were assessed. Heating Ara h 2/6 at 110°C resulted in extensive denaturation, hydrolysis and aggregation of the protein, whilst Ara h 2 and 6 isolated from roasted peanut retained its native conformation. Allergen stimulation of PBMC induced proliferation and Th2 cytokine secretion which was unaffected by thermal processing. Conversely, IgE reactivity and functionality of Ara h 2/6 was decreased by heating. Whilst heating-glycation further reduced the IgE binding capacity of the proteins, it moderated their loss of histamine releasing capacity. Ara h 2 and 6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6. Conclusions/Significance Although no effect of processing on T-cell reactivity was observed, heat induced denaturation reduced the IgE reactivity and subsequent functionality of Ara h 2/6. Conversely, Ara h 2 and 6 purified from roasted peanut retained the structure and IgE reactivity/functionality of the native protein which may explain the allergenic potency of this protein. Through detailed molecular study and allergenicity assessment approaches, this work then gives new insights into the effect of thermal processing on structure/allergenicity of peanut proteins.
Original languageEnglish
Article numbere23998
Number of pages9
JournalPLoS ONE
Issue number8
Publication statusPublished - 2011


  • ige-binding epitopes
  • t-cell responses
  • lipid transfer protein
  • in-vitro assay
  • maillard reaction
  • food allergens
  • cytokine production
  • major allergen
  • b-cell
  • digestion

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