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Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity

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Author: Boxtel, E.L. van · Broek, L.A.M. van den · Koppelman, S.J. · Gruppen, H.
Type:article
Date:2008
Institution: TNO Kwaliteit van Leven
Source:Molecular Nutrition and Food Research, 6, 52, 674-682
Identifier: 240832
doi: doi:10.1002/mnfr.200700299
Keywords: Health · Ara h 3 · Food allergy · Glycinin · Heat processing · Pepsin digestion · Ara · Arachis hypogaea · Glycine max · allergen · allergen Ara h3 · globulin · glycinin · immunoglobulin E · legumin protein, plant · pepsin A · soybean protein · vegetable protein · article · blood · chemistry · drug stability · food allergy · heat · human · immunology · metabolism · peanut · peanut allergy · plant seed · protein denaturation · protein quaternary structure · soybean · structure activity relation · Allergens · Arachis hypogaea · Drug Stability · Food Hypersensitivity · Globulins · Heat · Humans · Immunoglobulin E · Peanut Hypersensitivity · Pepsin A · Plant Proteins · Protein Denaturation · Protein Structure, Quaternary · Seeds · Soybean Proteins · Soybeans · Structure-Activity Relationship · Healthy for Life · Healthy Living

Abstract

Legumin proteins Ara h 3 from peanuts and glycinin from soybeans are increasingly described as important allergens. The stability of an allergen's IgE binding capacity towards heating and digestion is considered an important characteristic for food allergens. We investigated the effects of heating and digestion on the IgE binding of Ara h 3 and glycinin. Both proteins are relatively stable to denaturation, having denaturation temperatures ranging from 70 to 92°C, depending on their quaternary structure and the ionic strength. Aggregates were formed upon heating, which were partly soluble for glycinin. Heating slightly decreased the pepsin digestion rate of both allergens. However, heating did not affect the IgE binding capacity of the hydrolyzates, as after only 10 min of hydrolysis no IgE binding could be detected any more in all samples. Peanut allergen Ara h 1, when digested under equal conditions, still showed IgE binding after 2 h of hydrolysis. Our results indicate that the IgE binding capacity of legumin allergens from peanuts and soybeans does not withstand peptic digestion. Consequently, these allergens are likely unable to sensitize via the gastro-intestinal tract and cause systemic food allergy symptoms. These proteins might thus be less important allergens than was previously assumed. © 2008 Wiley-VCH Verlag GmbH & Co. KGaA.