کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10975220 | 1108032 | 2015 | 11 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Conformational changes of β-lactoglobulin induced by shear, heat, and pH-Effects on antigenicity
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موضوعات مرتبط
علوم زیستی و بیوفناوری
علوم کشاورزی و بیولوژیک
علوم دامی و جانورشناسی
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چکیده انگلیسی
Structural modifications influence the immune-reactivity of food proteins. We investigated effects of pH (3, 5, 7), temperature (80, 100, 120°C), and shear (100, 500, and 1,000 sâ1) 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 β-lactoglobulin (β-LG). Overall, heating at low pH (3) caused unfolding of proteins and fragmentation due to partial acid hydrolysis and thereby exposed β-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 β-LG but may have an effect in combination with pH or temperature. Overall, heating β-LG solutions to 120°C at pH 5 with shearing (100-1,000 sâ1) resulted in minimal antigenicity. Structural modifications of β-LG via denaturation or disulfide- or thiol-mediated interactions can either enhance or decrease its antigenicity.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Journal of Dairy Science - Volume 98, Issue 7, July 2015, Pages 4255-4265
Journal: Journal of Dairy Science - Volume 98, Issue 7, July 2015, Pages 4255-4265
نویسندگان
Toheder Rahaman, Todor Vasiljevic, Lata Ramchandran,