Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed

被引：217

作者：

Stojadinovic, Marija ^{[1
]}

Radosavljevic, Jelena ^{[1
]}

Ognjenovic, Jana ^{[1
]}

Vesic, Jelena ^{[1
]}

Prodic, Ivana ^{[1
]}

Stanic-Vucinic, Dragana ^{[1
]}

Velickovic, Tanja Cirkovic ^{[1
]}

机构：

[1] Univ Belgrade, Fac Chem, Belgrade 11000, Serbia

来源：

FOOD CHEMISTRY | 2013年 / 136卷 / 3-4期

关键词：

Antioxidant; beta-Lactoglobulin; Digestion; Interaction; Quenching; Polyphenol; GREEN TEA; FLUORESCENCE SPECTROSCOPY; PHENOLIC-COMPOUNDS; SERUM-ALBUMIN; TANNIC-ACID; PH; FLAVONOIDS; BOVINE; CAPACITY; COFFEE;

D O I：

10.1016/j.foodchem.2012.09.040

中图分类号：

O69 [应用化学];

学科分类号：

081704 ;

摘要：

Non-covalent interactions between beta-lactoglobulin (BLG) and polyphenol extracts of teas, coffee and cocoa were studied by fluorescence and CD spectroscopy at pH values of the gastrointestinal tract (GIT). The biological implications of non-covalent binding of polyphenols to BLG were investigated by in vitro pepsin and pancreatin digestibility assay and ABTS radical scavenging activity of complexes formed. The polyphenol-BLG systems were stable at pH values of the GIT. The most profound effect of pH on binding affinity was observed for polyphenol extracts rich in phenolic acids. Stronger non-covalent interactions delayed pepsin and pancreatin digestion of BLG and induced beta-sheet to alpha-helix transition at neutral pH. All polyphenols tested protected protein secondary structure at an extremely acidic pH of 1.2. A positive correlation was found between the strength of protein-polyphenol interactions and (a) half time of protein decay in gastric conditions (R-2 = 0.85), (b) masking of total antioxidant capacity of protein-polyphenol complexes (R-2 = 0.95). (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：1263 / 1271

页数：9

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[1] Modulation of the antioxidant activity of phenols by non-covalent interactions [J].