Abstract
Soybean is a high-quality plant protein resource and also a major food allergen. Glycation is widely used to modify protein allergens. In the current report, the influences of different saccharides on soybean protein structure and antigenicity through glycation were investigated. Soybean protein isolate (SPI) and saccharides (glucose, galactose, maltose, lactose, and dextran), at 1:1 weight ratio, were dry-heated at 60 °C and 79 % relative humidity for different times. The content of free amino group in glycated products was decreased by trinitrobenzene sulfonic acid method. In addition, high-molecular aggregates were generated in the glycated SPI, indicating that glycation reaction occurred in SPI–saccharide conjugates. Moreover, the structure of SPI in conjugates changed with exposure to aromatic side chains. Of all the SPI–saccharide conjugates, with time increased from 0 to 72 h, the antigenicity inhibition rate of β-conglycinin in SPI–glucose complexes declined from 83.55 (0 h) to 29.80 % (48 h), suggesting that introducing saccharides in SPI is an effective method to reduce the antigenicity of β-conglycinin.
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Acknowledgments
This work was supported financially by the National Natural Science Foundation of China (31201293 and 31171790), the National High Technology Research and Development Program of China (863 Program) (2013AA102208-5) and Foundation of Henan Educational Committee (14B550013).
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Bu, G., Zhu, T., Chen, F. et al. Effects of saccharide on the structure and antigenicity of β-conglycinin in soybean protein isolate by glycation. Eur Food Res Technol 240, 285–293 (2015). https://doi.org/10.1007/s00217-014-2326-5
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DOI: https://doi.org/10.1007/s00217-014-2326-5