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Biophys Chem. 2013 Dec 15;183:19-29. doi: 10.1016/j.bpc.2013.06.009. Epub 2013 Jun 21.

High pressure effects on allergen food proteins.

Author information

1
Department of Biophysics and Radiation Biology, Semmelweis University, Budapest 1094, Tuzolto u. 37-47, Hungary.

Abstract

There are several proteins, which can cause allergic reaction if they are inhaled or ingested. Our everyday food can also contain such proteins. Food allergy is an IgE-mediated immune disorder, a growing health problem of great public concern. High pressure is known to affect the structure of proteins; typically few hundred MPa pressure can lead to denaturation. That is why several trials have been performed to alter the structure of the allergen proteins by high pressure, in order to reduce its allergenicity. Studies have been performed both on simple protein solutions and on complex food systems. Here we review those allergens which have been investigated under or after high pressure treatment by methods capable of detecting changes in the secondary and tertiary structure of the proteins. We focus on those allergenic proteins, whose structural changes were investigated by spectroscopic methods under pressure in correlation with the observed allergenicity (IgE binding) changes. According to this criterion we selected the following allergen proteins: Mal d 1 and Mal d 3 (apple), Bos d 5 (milk), Dau c 1 (carrot), Gal d 2 (egg), Ara h 2 and Ara h 6 (peanut), and Gad m 1 (cod).

KEYWORDS:

Allergen protein; Food allergen; High pressure; IgE-binding; Unfolding

PMID:
23850175
DOI:
10.1016/j.bpc.2013.06.009
[Indexed for MEDLINE]

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