Abstract

PurposeThe purpose of this study was to determine the influence of Maillard reaction (MR, glycation) on biochemical and biological properties of the major peanut allergen Ara h 1.MethodsThree different time/temperature conditions of treatment were applied (37, 60, and 145 °C). The extent of MR was assessed by SDS-PAGE, loss of free amino groups, fluorescence intensity, content of bound sugar and fructosamine. The Caco-2 model system was applied to study effects of hydrolysed and non-hydrolysed Ara h 1 on proliferation and interleukin-8 (IL-8) secretion from Caco-2 cells.ResultsWe demonstrated significant differences in the biochemical properties of Ara h 1 glycated at different time/temperature conditions. Glycation of Ara h 1 at 37 °C was shown to cause least biochemical changes, not limiting pepsin hydrolysis. Loss of free amino groups, increase of fluorescence and brown colour of Ara h 1 glycated at 60 and 145 °C indicated advanced and final stages of MR. Non-treated Ara h 1 inhibited Caco-2 cell proliferation and stimulated IL-8 secretion. This effect was less pronounced for glycated Ara h 1. Incubation of Caco-2 cells with non-hydrolysed Ara h 1, glycated at the temperature of 37 and 60 °C, did not stimulate IL-8 secretion.ConclusionEach applied time/temperature-treatment combination caused different biochemical changes of Ara h 1, underlining diversity of formed MRPs. MR, independently of temperature/time conditions, reduced the pro-inflammatory properties of native Ara h 1, reflected in stimulation of IL-8 secretion from intestinal epithelial cells.

Highlights

  • The allergy to peanuts (Arachis hypogea) is one of the most common in industrialized societies

  • Purpose The purpose of this study was to determine the influence of Maillard reaction (MR, glycation) on biochemical and biological properties of the major peanut allergen Ara h 1

  • Treatment of Ara h 1 in the presence of glucose for each time/ temperature combination resulted in increased levels of bound sugar compared to both non-treated protein and Ara h 1 heated without glucose (Fig. 1b)

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Summary

Introduction

The allergy to peanuts (Arachis hypogea) is one of the most common in industrialized societies. Research on the prevalence of peanut allergy carried out under the integrated project on food allergy EuroPrevall showed the occurrence of sensitization to peanut in adult population to be 9.3 % in USA and between 4.2 and 0.8 % in European countries [1]. Clinical peanut allergy is detectable in 1–2 % of the total population [2] with an increasing prevalence in US [3] and stable tendency in the UK [4]. A trimeric complex of Ara h 1 may protect from digestion of a linear IgE epitopes which are located mainly in the areas of the subunit– subunit contacts [11]. Fragments of Ara h 1 containing several intact IgE-binding epitopes are able to reach the gut mucosa and influence the intestinal homeostasis [11]

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