Abstract
Results Heating Ara h 2/6 at 110°C resulted in extensive denaturation whilst Ara h 2/6 extracted from roasted peanut retained its native conformation. Allergen stimulation of PBMC from peanut allergic patients induced proliferation of mainly CD4+ T-cells and induction of Th2 cytokine secretion which was unaffected by thermal processing. 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 2/6 purified from roasted peanut demonstrated the same IgE reactivity as unheated, native Ara h 2/6.
Highlights
Native Ara h 2/6 was purified from raw peanuts and heated in solution (15 min, 110°C) in either the presence or absence of glucose, or purified from roasted peanut
Heating Ara h 2/6 at 110°C resulted in extensive denaturation whilst Ara h 2/6 extracted from roasted peanut retained its native conformation
Allergen stimulation of PBMC from peanut allergic patients induced proliferation of mainly CD4+ T-cells and induction of Th2 cytokine secretion which was unaffected by thermal processing
Summary
From Food Allergy and Anaphylaxis Meeting 2011 Venice, Italy. Aim To study the effect of heating and glycation on the IgEbinding properties and biological activity of 2S albumins (Ara h 2/6) from peanut
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