کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
7597546 1492133 2014 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Interaction of flavan-3-ol derivatives and different caseins is determined by more than proline content and number of proline repeats
ترجمه فارسی عنوان
تعامل مشتقات فلان 3-اول و کازئین های مختلف با بیشتر از مقدار پرولین و تعداد تکرار پرولین
کلمات کلیدی
تعامل پروتئین فلاونوئیدها، خنک سازی فلورسنت، فوق العاده تصفیه انعطاف پذیری لیگاند، تصفیه پروسیانیدین،
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی آنالیزی یا شیمی تجزیه
چکیده انگلیسی
Interactions of Type A and B flavan-3-ol dimers (procyanidins) and several monomeric flavan-3-ols, with α-casein and β-casein, were investigated. Binding affinities measured were related to the ligands structure, including several properties (e.g. intrinsic flexibility (number of rotatable bonds) and hydrophobicity), and to the amino-acid composition of the caseins. A monomeric flavan-3-ol esterified with gallic acid (EGCG) had a five to ten times higher affinity to caseins compared to the non-galloylated dimeric flavan-3-ols. In this case, the larger number of rotatable bonds in EGCG might be accountable for this difference. Comparing flavan-3-ol dimers, intrinsic flexibility did not consistently promote interactions, as procyanidin A1 displayed a higher affinity to α-casein than the supposedly more flexible B-type dimers investigated. Despite its higher content of proline, compared to α-casein, β-casein did not always have a higher affinity for the ligands investigated (e.g. no interaction with procyanidin A1 detected). These results suggest that more factors than proline content and the number of proline repeats govern phenolic-casein interactions.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Food Chemistry - Volume 158, 1 September 2014, Pages 408-416
نویسندگان
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