Title
Legumin allergens from peanuts and soybeans: Effects of denaturation and aggregation on allergenicity
Author
van Boxtel, E.L.
van den Broek, L.A.M.
Koppelman, S.J.
Gruppen, H.
TNO Kwaliteit van Leven
Publication year
2008
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.
Subject
Healthy for Life
Health
Healthy Living
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
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DOI
https://doi.org/10.1002/mnfr.200700299
TNO identifier
240832
ISSN
1613-4125
Source
Molecular Nutrition and Food Research, 52 (6), 674-682
Document type
article