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The structural properties and antigenicity of soybean glycinin by glycation with xylose
Author(s) -
Bu Guanhao,
Zhu Tingwei,
Chen Fusheng
Publication year - 2017
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.8036
Subject(s) - glycation , antigenicity , maillard reaction , chemistry , xylose , biochemistry , glycosylation , melanoidin , food science , antibody , biology , receptor , fermentation , immunology
BACKGROUND Soybean glycinin is considered a major allergenic protein, and glycation is widely used to reduce the allergenic potential of present allergens. Glycation of soybean glycinin with xylose at 55 °C for different lengths of time was investigated. The extent of Maillard reaction was reflected through the content changing of free amino groups, color analysis and sodium dodecyl sulfate–polyacrylamide gel electrophoresis. Alteration in the structural properties of glycinin was characterized by Fourier transform infrared spectroscopy, and antigenicity was evaluated by indirect competitive enzyme‐linked immunosorbent assay. RESULTS The changes in the color of glycinin–xylose samples and the reduction of free amino group content in proteins indicated that the Maillard reaction occurred. The degree of glycation increased in glycated samples with the increase in reaction time. Glycation induced the changes in the secondary structure of glycinin and the ordered structure of proteins increased during the glycation reaction. The antigenicity of glycinin was reduced with the increase in reaction time. After glycation for 12 h, the antigenicity of glycinin declined about 18% compared with native glycinin. CONCLUSION The application of glycation may be an efficient method to reduce the antigenicity of soybean glycinin. © 2016 Society of Chemical Industry