Binding of resveratrol with sodium caseinate in aqueous solutions

被引：133
作者：
Acharya, Durga P.
Sanguansri, Luz
Augustin, Mary Ann
机构：
[1] CSIRO Preventat Hlth Natl Res Flagship Food & Hlt, Werribee, Vic 3030, Australia
[2] CSIRO Div Anim Food & Hlth Sci, Werribee, Vic 3030, Australia
来源：
FOOD CHEMISTRY | 2013年 / 141卷 / 02期
关键词：
Resveratrol; Polyphenol; Casein; Protein-polyphenol binding; Fluorescence quenching; HUMAN SERUM-ALBUMIN; ANTIOXIDANT FLAVONOIDS; HEART-DISEASE; CANCER; PROTEINS; FLUORESCENCE; TRANSPORT;
D O I：
10.1016/j.foodchem.2013.03.037
中图分类号：
O69 [应用化学];
学科分类号：
081704 ;
摘要：
The interaction between resveratrol (Res) and sodium caseinate (Na-Cas) has been studied by measuring fluorescence quenching of the protein by resveratrol. Quenching constants were determined using Stern-Volmer equation, which suggests that both dynamic and static quenching occur between Na-Cas and Res. Binding constants for the complexation between Na-Cas and Res were determined at different temperatures. The large binding constants (3.7-5.1 x 10(5) M-1) suggest that Res has strong affinity for Na-Cas. This affinity decreases as the temperature is raised from 25 to 37 degrees C. The binding involves both hydrogen bonding and hydrophobic interaction, as suggested by negative enthalpy change and positive entropy change for the binding reaction. The present study indicates that Na-Cas, a common food protein, may be used as a carrier of Res, a bioactive polyphenol which is insoluble in both water and oils. (C) 2013 Elsevier Ltd. All rights reserved.
引用
收藏
页码：1050 / 1054
页数：5
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