With the advancement of food biotechnology both soy and pea proteins become present in various products in the form of a textured proteins or a “protein filler”. 7S globulins – vicilin (Pis s1) from pea and b-conglycinin from soy – are one of the major seed storage proteins and known food allergens.

Glycation (non-enzymatic glycosylation) is a spontaneous reaction that occurs during food processing, storage and preparation of food. Changes caused by glycation itself and reactions following it are highly complex and not easily predictable, but there are a number of major chemical pathways that lead to distinct patterns of modifications. Each one of intentional and unintentional modification is able to change immunogenicity or allergenicity of proteins, however both extension and direction (decrease or increase) of those changes have not been fully assessed.

The aim of this research was to investigate the influence of glycation on antigenicity of soy and pea 7S globulin.

After extraction from soy and pea flour, 7S globulins were purified by cold and acid fractionation (soy) or ammonium sulphate fractionation (pea), followed by Con A Sepharose lectin affinity chromatography and Superdex 200 gel filtration. Glycation with glucose was carried out for three days at 50°C, followed by dialysis against DI water to remove glucose. Rabbit polyclonal antibodies against native protein were used for competitive ELISA for quantitative assessment of antigenicity. Both native and glycated proteins were hydrolyzed with trypsin and resulting polypeptides were submitted to Western-immunoblotting for qualitative assessment.

It was found that thermal processing of soy and pea 7S globulins has significant influence on their antigenic properties.

Acknowledgements – this research was funded through the EU Sixth Framework Programme “The Prevalence, Cost, and Basis of Food Allergy across Europe (EuroPrevall)”.

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