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Impacts of glucosamine/oligochitosan glycation and cross-linking by transglutaminase on the structure and in vitro antigenicity of whey proteins

Journal 2015 · IF 0.943 · 69(2): 169-176 · 发表于 2015 年 9 月 24 日
作者: Ying-Hua Zhang,Jia-Qi Liu,Di Xu,Xin-Huai Zhao
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摘要

With the fixed and selected conditions, whey protein concentrate (WPC) was glucosamine-/oligochitosan-glycated and cross-linked by transglutaminase, resulting in glucosamine conjugation of 4.18–5.88 g/kg. Electrophoretic analysis showed cross-linking and glycation of whey proteins, while circular dichroism analysis indicated that the two reactions contributed less ordered secondary structure to the two products. Enzyme-linked immunosorbent assay results showed that the two products lost 64–95% antigenic responses of WPC, and oligochitosan was more powerful than glucosamine to reduce the responses. Rocket immuno-electrophoretic analysis also evidenced antigenicity loss. This applied treatment is efficient to modify the structure and to decrease the allergenicity of whey proteins.

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