Abstract
Previously, we have demonstrated that Gly m 4, one of the major soybean allergens, could pass through the Caco-2 epithelial barrier and have proposed a mechanism of sensitization. However, it is not known yet whether Gly m 4 can reach the intestine in its intact form after digestion in stomach. In the present work, we studied an influence of various factors including lipids (fatty acids and lysolipids) on digestibility of Gly m 4. Using fluorescent and CD spectroscopies, we showed that Gly m 4 interacted with oleic acid and LPPG (lyso-palmitoyl phosphatidylglycerol), but its binding affinity greatly decreased under acidic conditions, probably due to the protein denaturation. The mimicking of gastric digestion revealed that Gly m 4 digestibility could be significantly reduced with the change of pH value and pepsin-to-allergen ratio, as well as by the presence of LPPG. We suggested that the protective effect of LPPG was unlikely associated with the allergen binding, but rather connected to the pepsin inhibition due to the lipid interaction with its catalytic site. As a result, we assumed that, under certain conditions, the intact Gly m 4 might be able to reach the human intestine and thereby could be responsible for allergic sensitization.
Funder
Russian Science Foundation
Subject
Filtration and Separation,Chemical Engineering (miscellaneous),Process Chemistry and Technology
Cited by
3 articles.
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