Binding affinity between dietary polyphenols and β-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
2012; Elsevier BV; Volume: 136; Issue: 3-4 Linguagem: Inglês
10.1016/j.foodchem.2012.09.040
ISSN1873-7072
AutoresMarija Stojadinović, Jelena Radosavljević, Jana Ognjenović, Jelena Vesić, Ivana Prodić, Dragana Stanić-Vučinić, Tanja Ćirković Veličković,
Tópico(s)Biochemical effects in animals
ResumoNon-covalent interactions between β-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 β-sheet to α-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 (R2 = 0.85), (b) masking of total antioxidant capacity of protein–polyphenol complexes (R2 = 0.95).
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