Antigenicity, Allergenicity, and Structural Properties of Soy Protein Isolate-Xylose Conjugates
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Abstract:
Soybean is a high-quality plant protein source, but it is also one of the top eight food allergens. Glycosylation is an effective method to reduce the allergenic potential of food protein allergens. Xylose was conjugated to soy protein isolate (SPI) by means of glycosylation to form SPI-xylose conjugates. The changes in the antigenicity and allergenicity of glycinin in SPI-xylose conjugates at a specific temperature, specific mass ratio of the protein and sugar, and different reaction times were determined by the indirect competitive enzyme-linked immunosorbent assay, and the structural properties of SPI-xylose conjugates were also studied. The results indicate that glycosylation can effectively reduce the antigenicity and allergenicity of glycinin. The antigenicity of glycinin was reduced from 83.01% to 67.43%; the allergenicity of glycinin was reduced from 46.32% to 29.48%, and both immunoreactivities were relatively low after ten hours of reaction. Glycosylation was confirmed by trinitrobenzene sulfonic acid and sodium dodecyl sulfate polyacrylamide gel electrophoresis. The Fourier transform infrared spectroscopy results showed that compared with SPI, the α-helix and β-turn content in SPI-xylose conjugates decreased, while the β-sheet and random coil contents increased.
