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Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
dc.creator | Stojadinović, Marija M. | |
dc.creator | Radosavljević, Jelena | |
dc.creator | Ognjenović, Jana | |
dc.creator | Mihailović-Vesić, Jelena | |
dc.creator | Prodić, Ivana | |
dc.creator | Stanić-Vučinić, Dragana | |
dc.creator | Ćirković-Veličković, Tanja | |
dc.date.accessioned | 2018-11-22T00:25:11Z | |
dc.date.available | 2018-11-22T00:25:11Z | |
dc.date.issued | 2013 | |
dc.identifier.issn | 0308-8146 | |
dc.identifier.uri | https://cherry.chem.bg.ac.rs/handle/123456789/1577 | |
dc.description.abstract | 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). | en |
dc.publisher | Elsevier Sci Ltd, Oxford | |
dc.relation | info:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS// | |
dc.relation | info:eu-repo/grantAgreement/EC/FP7/256716/EU// | |
dc.rights | restrictedAccess | |
dc.source | Food Chemistry | |
dc.subject | Antioxidant | en |
dc.subject | beta-Lactoglobulin | en |
dc.subject | Digestion | en |
dc.subject | Interaction | en |
dc.subject | Quenching | en |
dc.subject | Polyphenol | en |
dc.title | Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed | en |
dc.type | article | |
dc.rights.license | ARR | |
dcterms.abstract | Михаиловић Весић, Јелена; Огњеновиц, Јана; Радосављевић, Јелена; Стојадиновиц, Марија; Ћирковић-Величковић, Тања; Станић-Вучинић, Драгана; Продић, Ивана; | |
dc.citation.volume | 136 | |
dc.citation.issue | 3-4 | |
dc.citation.spage | 1263 | |
dc.citation.epage | 1271 | |
dc.identifier.wos | 000313924900021 | |
dc.identifier.doi | 10.1016/j.foodchem.2012.09.040 | |
dc.citation.other | 136(3-4): 1263-1271 | |
dc.citation.rank | aM21 | |
dc.identifier.pmid | 23194522 | |
dc.description.other | Supplementary material: [http://cherry.chem.bg.ac.rs/handle/123456789/2905] | |
dc.type.version | publishedVersion | en |
dc.identifier.scopus | 2-s2.0-84867896149 |