Allergens of Arachis hypogaea and the effect of processing on their detection by ELISA

Abstract

Food allergies are an emerging public health problem in industrialized areas of the world. They represent a considerable health problem in these areas because of the relatively high number of reported cases. Usually, food allergens are proteins or glycoproteins with a molecular mass ranging from 10 to 70 kDa. Among the food allergies, peanut is accounted to be responsible for more than 50% of the food allergy fatalities. Threshold doses for peanut allergenic reactions have been found to range from as low as 100 µg to 1 g of peanut protein, which equal to 400 µg to 4 g peanut meal. Allergens from peanut are mainly seed storage proteins that are composed of conglutin, vicilin, and glycinin families. Several peanut proteins have been identified to induce allergic reactions, particularly Ara h 1-11. This review is mainly focused on different classes of peanut allergens, the effect of thermal and chemical treatment of peanut allergens on the IgY binding and detectability of these allergens by enzyme linked immunosorbent assay (ELISA) to provide knowledge for food industry.

Keywords: allergens processing; anaphylaxis; conglutin; glycinin; peanut proteins; vicilin.

Fig. 1

Sequence leading to sensitization and elicitation of a food allergic reaction to a food.

Fig. 2

Detectability of peanut proteins after heat treatment at 80°C and 100°C in PBS (24).

Fig. 3

Detectability of peanut protein after heat treatment at 100°C in PBS buffer at pH 4, pH 7.4 and pH 10 (24).

Fig. 4

Detectability of peanut protein after heat treatment at 80°C in 20 mM glucose solution and 100°C in 20 mM glucose solution (24).