Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed
Само за регистроване кориснике
2013
Аутори
Stojadinović, Marija M.Radosavljević, Jelena
Ognjenović, Jana
Mihailović-Vesić, Jelena
Prodić, Ivana
Stanić-Vučinić, Dragana
Ćirković-Veličković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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).
Кључне речи:
Antioxidant / beta-Lactoglobulin / Digestion / Interaction / Quenching / PolyphenolИзвор:
Food Chemistry, 2013, 136, 3-4, 1263-1271Издавач:
- Elsevier Sci Ltd, Oxford
Финансирање / пројекти:
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-172024)
- Reinforcement of the Faculty of Chemistry, University of Belgrade, towards becoming a Center of Excellence in the region of WB for Molecular Biotechnology and Food research (EU-256716)
Напомена:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/2905
DOI: 10.1016/j.foodchem.2012.09.040
ISSN: 0308-8146
PubMed: 23194522
WoS: 000313924900021
Scopus: 2-s2.0-84867896149
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stojadinović, Marija M. AU - Radosavljević, Jelena AU - Ognjenović, Jana AU - Mihailović-Vesić, Jelena AU - Prodić, Ivana AU - Stanić-Vučinić, Dragana AU - Ćirković-Veličković, Tanja PY - 2013 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1577 AB - 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). PB - Elsevier Sci Ltd, Oxford T2 - Food Chemistry T1 - Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed VL - 136 IS - 3-4 SP - 1263 EP - 1271 DO - 10.1016/j.foodchem.2012.09.040 ER -
@article{ author = "Stojadinović, Marija M. and Radosavljević, Jelena and Ognjenović, Jana and Mihailović-Vesić, Jelena and Prodić, Ivana and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja", year = "2013", 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).", publisher = "Elsevier Sci Ltd, Oxford", journal = "Food Chemistry", title = "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed", volume = "136", number = "3-4", pages = "1263-1271", doi = "10.1016/j.foodchem.2012.09.040" }
Stojadinović, M. M., Radosavljević, J., Ognjenović, J., Mihailović-Vesić, J., Prodić, I., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2013). Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. in Food Chemistry Elsevier Sci Ltd, Oxford., 136(3-4), 1263-1271. https://doi.org/10.1016/j.foodchem.2012.09.040
Stojadinović MM, Radosavljević J, Ognjenović J, Mihailović-Vesić J, Prodić I, Stanić-Vučinić D, Ćirković-Veličković T. Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed. in Food Chemistry. 2013;136(3-4):1263-1271. doi:10.1016/j.foodchem.2012.09.040 .
Stojadinović, Marija M., Radosavljević, Jelena, Ognjenović, Jana, Mihailović-Vesić, Jelena, Prodić, Ivana, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Binding affinity between dietary polyphenols and beta-lactoglobulin negatively correlates with the protein susceptibility to digestion and total antioxidant activity of complexes formed" in Food Chemistry, 136, no. 3-4 (2013):1263-1271, https://doi.org/10.1016/j.foodchem.2012.09.040 . .