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ARS Home » Southeast Area » New Orleans, Louisiana » Southern Regional Research Center » Food Processing and Sensory Quality Research » Research » Publications at this Location » Publication #264222
Title: Influence of enzymatic hydrolysis on the allergenicity of roasted peanut protein

Author
item CABANILLAS, BEATRIZ - Instituto Nacional De Investigacion Y Technologia Agraria Y Alimentaria
item RODRIGUEZ, JULIA - Instituto Nacional De Investigacion Y Technologia Agraria Y Alimentaria
item CRESPO, JESUS - Instituto Nacional De Investigacion Y Technologia Agraria Y Alimentaria
item PEDROSA, MERCEDES - Instituto Nacional De Investigacion Y Technologia Agraria Y Alimentaria
item CUADRADO, CARMEN - Instituto Nacional De Investigacion Y Technologia Agraria Y Alimentaria
item BURBANO, CARMEN - Instituto Nacional De Investigacion Y Technologia Agraria Y Alimentaria
item Maleki, Soheila

Submitted to: International Archives of Allergy and Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 3/12/2011
Publication Date: 10/1/2011
Citation: Cabanillas, B., Rodriguez, J., Crespo, J.F., Pedrosa, M.M., Cuadrado, C., Burbano, C., Maleki, S.J. 2011. Influence of enzymatic hydrolysis on the allergenicity of roasted peanut protein. International Archives of Allergy and Immunology. 157:41-50.

Interpretive Summary: Peanut allergy is recognized as one of the most severe food allergies. Some studies have investigated the effects of enzymatic treatments on the in vitro immunological reactivity of members of the Leguminosae family; such as, soybean, chickpea, and lentil. Nevertheless, there are only a few studies carried out with sera from patients with well-documented allergy. Roasted peanut protein extract was hydrolyzed by sequential and individual action of two food-grade enzymes. Immunoreactivity to roasted peanut extract and hydrolyzed samples was evaluated using immunoglobulin E (IgE) antibody from the serum of five patients with clinical allergy to peanut and allergenic proteins. These assays showed an important decrease of IgE reactivity and major allergen levels in the first 30 minutes of hydrolyzation with one of the enzymes. In contrast, individual treatment with the second enzyme caused an increase in IgE reactivity at 30 minutes, and led to a 65% inhibition of IgE reactivity at the end of the assay (300 minutes). Two of the major peanut allergens were still recognized after treatment with the second enzyme for 300 minutes. Hydrolysis with the first enzyme decreases IgE reactivity in the soluble protein fraction of roasted peanut better than hydrolysis with the second enzyme.

Technical Abstract: Peanut allergy is recognized as one of the most severe food allergies. Some studies have investigated the effects of enzymatic treatments on the in vitro immunological reactivity of members of the Leguminosae family; such as, soybean, chickpea, and lentil. There are only a few studies carried out with sera from patients with well-documented allergy. Roasted peanut protein extract was hydrolyzed by sequential and individual action of two food-grade enzymes; an endoprotease (Alcalase) and an exoprotease (Flavourzyme). Immunoreactivity to roasted peanut extract and hydrolyzed samples was evaluated by means of IgE immunoblot, ELISA, and 2-dimensional electrophoresis, using sera from five patients with clinical allergy to peanut and anti-Ara h 1, anti-Ara h 2, and anti-Ara h 3 immunoblots. Immunoblot and ELISA assays showed an important decrease of IgE reactivity, and Ara h 1, Ara h 2, and Ara h 3 levels in the first 30 minutes of hydrolyzation with Alcalase. In contrast, individual treatment with Flavourzyme caused an increase in IgE reactivity detected by ELISA at 30 minutes, and led to a 65% inhibition of IgE reactivity at the end of the assay (300 min). Ara h 1 and the basic subunit of Ara h 3 were still recognized after treatment with Flavourzyme for 300 minutes. Hydrolysis with endoprotease Alcalase decreases IgE reactivity in the soluble protein fraction of roasted peanut better than hydrolysis with exoprotease Flavourzyme.