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Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity
Author(s) -
van Boxtel Evelien L.,
van den Broek Lambertus A. M.,
Koppelman Stef J.,
Gruppen Harry
Publication year - 2008
Publication title -
molecular nutrition and food research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.495
H-Index - 131
eISSN - 1613-4133
pISSN - 1613-4125
DOI - 10.1002/mnfr.200700299
Subject(s) - legumin , chemistry , allergen , denaturation (fissile materials) , digestion (alchemy) , immunoglobulin e , food science , food allergens , pepsin , hydrolysis , food allergy , storage protein , allergy , biochemistry , chromatography , immunology , enzyme , antibody , biology , nuclear chemistry , gene
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.