Gliadins are major allergens responsible
for wheat allergies. Food
processing is an effective strategy to reduce the allergenicity of
gluten. In the present study, we determined the secondary and tertiary
structures of gluten and gliadins treated by chemical, physical, and
enzymatic means through FTIR, surface hydrophobicity, intrinsic fluorescence
spectra, and UV absorption spectra. The results showed that the three
treatments of phosphorylation and alcalase and papain hydrolyses significantly
changed the conformational structures of gliadins, especially the
secondary structure. Then, the potential allergenicity of the phosphorylated
and alcalase and papain hydrolyzed gliadins were further characterized,
and we observed a significant decrease in the allergenicity through
the results of the index of spleen, serum total IgE, gliadin-specific
IgE, histamine, and serum cytokine concentrations. An elevation of
Th17 cells, the absence of Treg cells, and an imbalance in Treg/Th17
are associated with allergy. On the basis of the expression levels
of related cytokines and key transcription factors, we also confirmed
that phosphorylation and alcalase and papain hydrolysis could effectively
reduce the allergenicity of gliadins by improving the imbalance of
both Th1/Th2 and Treg/Th17 in the spleens of sensitized mice. This
study suggested that the changes in conformational structure contribute
to gliadin hyposensitization and that phosphorylation and alcalase
and papain hydrolysis may be promising strategies for the production
of wheat products with low allergenicity.