**5. Chemical and biological properties of food allergens**

For Jedrychowski and Wichers [21], most of the allergens have a protein; they are usually glycoproteins dissolved in water and resistant to digestion. The immune system recognizes them, and as a result, specific IgEs are produced (type I allergy) or specific T-cell antigen receptors (TCRs) are produced (type IV allergy).

Harder et al. [11] treated the debate on the effect of radiation in proteins formed on the study of the radiation chemistry of amino acids. Started responses with hydrated electrons are the main route in the radiolysis of amino acids and proteins. When proteins are irradiated in the attendance of water, all of the retroactions that are possible with amino acids are also practicable with proteins holding these amino acids. With 20 component amino acids and proteins with three reactive kinds of water radiolysis, many complicated interactions are practical. Further, the effects are exercised by the spatial shape of the protein current, determined by hydrogen links, disulfide links, hydrophobic links, and ionic links. Lonely, amino acids, which are likely to attack by radicals when irradiated, are less susceptible when they are part of the protein structure and they are more or less inaccessible to responses with radicals. Another factor that probably contributes to the increased force compared with the proteinisolated amino acid sequence is owing to a greater or lesser hardness of the spatial structure of the protein; radicals created as a result of irradiation molecule are safe in the stance and have a high chance of recombination.

The authors also said that a great proportion of radiant energy laid up in irradiated proteins seemingly promotes denaturation, and modifies in secondary and tertiary current, before the destruction of the amino acid components. This denaturation is much less longer than that caused by warmth. This is because sterilizing radiation in food for much time housing combines with warm treatment. Enzymes are more sensible to warmth.
