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The determination of peanut proteins is based on their immunochemical reaction with a specific antibody. A polyclonal antibody specific to peanuts proteins has been pre-coated into a microtiter plate. During the first step, calibrators and samples are pipetted into the wells and peanuts proteins are bound by the immobilized antibody. After a washing step removing any unbound antigen, another peanut protein-specific antibody conjugated with an enzyme horseradish peroxidase is applied. This antibody reacts with the complex of the first antibody-peanut protein via another epitope on the protein. After an incubation period, a chromogenic substrate is added to the wells and color develops in proportion to the amount of peanut proteins bound in the initial step. The color development is stopped and the intensity of the color is measured.

Peanut (Arachyshypogea), a member of the Fabaceae family, is a frequent cause of food allergic reaction. The prevalence of the peanut allergy is estimated between 0,5 - 1,1 % in the adult population of some American and European countries (Becker et al., 2004). Several peanut proteins have been identified to introduce allergic reaction. Ara h1 and Ara h2 are considered to be major allergens (Muelenauer et al., 2005). Ara h1 - conarachin, vicilin - is 7S globulin, a peanut storage protein. The Ara h2 - conglutin - belongs to the 2S albumins. Ara h1 and Ara h2 cause the majority of adverse reactions. Thearachin Ara h3 and very similar protein Ara h4 are 11-12S globulins (Szymkiewicz, 2010, Koppelman et al., 1999). These peanut allergens are heat-resistant and their allergenicity is enhanced by roasting, possibly because of structural modification of the protein molecules (Becker et al., 2004).