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United States Department of Agriculture

Agricultural Research Service

Research Project: Primary and Secondary Prevention of Peanut and Tree Nut Allergy

Location: Food Processing and Sensory Quality Research

Title: Heat and pressure treatments effects on peanut allergenicity

Authors
item Cabanillas, Beatriz -
item MALEKI, SOHEILA
item Rodriguez, Julia -
item Burbano, Carmen -
item Muzquiz, Mercedes -
item Jimenez, Maria -
item Pedrosa, Mercedes -
item Cuadrado, Carmen -
item Crespo, Jesus -

Submitted to: Food Chemistry
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: October 27, 2011
Publication Date: December 15, 2011
Citation: Cabanillas, B., Maleki, S.J., Rodriguez, J., Burbano, C., Muzquiz, M., Jimenez, M., Pedrosa, M., Cuadrado, C., Crespo, J. 2011. Heat and pressure treatments effects on peanut allergenicity. Food Chemistry. 132:360-366.

Interpretive Summary: Peanut allergy is recognized as one of the most severe food allergies. The aim of this study was to investigate the changes in immunoglobulin E (IgE) binding to peanut proteins produced by thermal-processing methods, including a high moisture and high heat treatment called autoclaving. Immunoreactivity to raw and thermally processed peanut extracts was evaluated by IgE immunoblot, and with skin tests in patients with clinical allergy to peanut. Roasted peanut and autoclaved roasted peanut were selected for IgE binding experiments, with serum from peanut allergic patients, immunoblot experiments with antibodies against peanut allergens (Ara h 1, Ara h 2 and Ara h 3), digestion experiments, and structure determination studies. These studies showed IgE immunoreactivity of roasted peanut proteins decreased significantly at extreme conditions of autoclaving. Structure experiments showed unfolding of proteins in autoclave treated samples, which makes them more susceptible to digestion, and caused a significant decrease in the IgE-binding capacity of peanut allergens.

Technical Abstract: Peanut allergy is recognized as one of the most severe food allergies. The aim of this study was to investigate the changes in IgE binding capacity of peanut proteins produced by thermal-processing methods, including autoclaving. Immunoreactivity to raw and thermally processed peanut extracts was evaluated by IgE immunoblot, and skin prick tests in patients with clinical allergy to peanut. Roasted peanut and autoclaved roasted peanut were selected for IgE ELISA experiments, with individual sera, immunoblot experiments with antibodies against peanut allergens (Ara h 1, Ara h 2 and Ara h 3), digestion experiments, and circular dichroism spectroscopy. In vitro and in vivo experiments showed IgE immunoreactivity of roasted peanut proteins decreased significantly at extreme conditions of autoclaving. Circular dichroism experiments showed unfolding of proteins in autoclave treated samples, which makes them more susceptible to digestion. Autoclaving at 2.56 atm for 30 min produces a significant decrease of IgE-binding capacity of peanut allergens.

Last Modified: 7/28/2014