Add time:08/04/2019         Source:sciencedirect.com

The research was aimed at defining the impact of non-enzymatic glycosylation of pea globulin 7S on its biological properties. Glycation of pea globulin 7S was carried out at the temperature of 37 °C for 7 days and at 60 °C for 3 days. No glycation of the of the pea globulin 7S was observed when using high pressure of 500 MPa. Polyclonic rabbit antibodies were produced for immunochemical studies. The immunologic activity of non- and glycated pea globulin 7S was examined with the ELISA and Western blot. Also, excretion of IL-5, -10 and 13 as well as INF-γ by human peripheral blood lymphocytes along with symptoms of allergy to soy proteins under the influence of non- and glycated pea globulin 7S was assessed, as well their apoptosis and necrosis. Moreover, transportation of those proteins by the Caco-2 monolayer and their cytotoxicity were also studied. The results have proved that pea globulin 7S glycated in various physiochemical conditions is characterized by different properties to those of non-glycated ones. Lysine glycation entails a decrease in its nutritional value. Glycated pea globulin 7S manifests lowered affinity to antibodies, which suggests a limitation of its immunoallergic properties. On the other hand, the fact that glycated pea globulin 7S stimulates maturing of Th0 cells to Th2 ones, confirms its role in the process of food allergy induction. Decreased cytotoxicity of glycated pea globulin 7S and its transportation through the Caco-2 monolayer may stand for its allergenicity caused by its limited transportation to the cells of the immune system.

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