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Impacts of glucosamine/oligochitosan glycation and cross‐linking by transglutaminase on the structure and in vitro antigenicity of whey proteins
Author(s) -
Zhang YingHua,
Liu JiaQi,
Xu Di,
Zhao XinHuai
Publication year - 2016
Publication title -
international journal of dairy technology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.061
H-Index - 53
eISSN - 1471-0307
pISSN - 1364-727X
DOI - 10.1111/1471-0307.12246
Subject(s) - antigenicity , glycation , chemistry , glucosamine , whey protein , tissue transglutaminase , biochemistry , in vitro , circular dichroism , glycosylation , electrophoresis , food science , enzyme , antigen , immunology , biology , receptor
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.