کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
7585430 | 1492037 | 2018 | 40 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Spectroscopic and docking studies on the interaction between caseins and β-carotene
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کلمات کلیدی
موضوعات مرتبط
مهندسی و علوم پایه
شیمی
شیمی آنالیزی یا شیمی تجزیه
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چکیده انگلیسی
Natural occurrence of β-carotene in bovine milk and the leading role of milk proteins in low-fat or fat-free dairy products necessitate investigating the possibility of interaction between β-carotene and casein constituting up to 80% of bovine milk proteins. In this study, molecular interaction of caseins and β-carotene was analyzed using fluorescence, UV-Vis absorption, circular dichroism (CD), and computer-aided molecular modeling. Casein and its fractions were bound to β-carotene with a binding constant of the order 104â¯Mâ1 and a 1:1 binding stoichiometry. The binding was favored at alkaline pHs, low ionic strength and temperatures. κ-Casein had the highest binding affinity to β-carotene, among casein fractions. The negative values of entropy and enthalpy changes and docking studies proved Van der Waals interactions are predominant forces in the binding process. The casein conformation was also altered through inducing a more folded structure in β-casein and a looser conformation in α- and κ-casein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 255, 30 July 2018, Pages 187-196
Journal: Food Chemistry - Volume 255, 30 July 2018, Pages 187-196
نویسندگان
Zahra Allahdad, Mehdi Varidi, Reza Zadmard, Ali Akbar Saboury,