期刊
JOURNAL OF DAIRY SCIENCE
卷 98, 期 7, 页码 4255-4265出版社
ELSEVIER SCIENCE INC
DOI: 10.3168/jds.2014-9010
关键词
antigenicity; shear; heat; pH; conformation
Structural modifications influence the immune-reactivity of food proteins. We investigated effects of pH (3, 5, 7), temperature (80, 100, 120 degrees C), and shear (100, 500, and 1,000 s(-1)) on conformational changes (monitored by surface hydrophobicity, total thiol content, Fourier transform infrared spectroscopy, and gel electrophoresis) and their relation to antigenicity (determined by indirect ELISA) of P-lactoglobulin (beta-LG). Overall, heating at low pH (3) caused unfolding of proteins and fragmentation due to partial acid hydrolysis and thereby exposed. beta-strands that contributed to appearance of some hidden epitopes, resulting in higher antigenicity. Heating at pH 5 and 7 decreased the allergenic response due to covalently bonded molecular polymerization and aggregation, which destroyed or masked some epitopes. Shear alone had no effect on the antigenic response of beta-LG but may have an effect in combination with pH or temperature. Overall, heating P-LG solutions to 120 degrees C at pH 5 with shearing (100-1,000 s(-1)) resulted in minimal antigenicity. Structural modifications of beta-LG via denaturation or disulfide- or thiol-mediated interactions can either enhance or decrease its antigenicity.
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