Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
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2017
Authors
Peruško, MarijaAl-Hanish, Ayah
Mihailović-Vesić, Jelena
Minić, Simeon L.
Trifunović, Sara
Prodić, Ivana
Ćirković-Veličković, Tanja
Article (Published version)
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Show full item recordAbstract
Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both ...glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.
Keywords:
Beta-lactoglobulin / Epigallocatechin-3-gallate / Glycation / Maillard reaction / Protein polyphenol interactions / TeaSource:
Food Chemistry, 2017, 232, 744-752Publisher:
- Elsevier Sci Ltd, Oxford
Funding / projects:
- Molecular properties and modifications of some respiratory and nutritional allergens (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)
Note:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3027
DOI: 10.1016/j.foodchem.2017.04.074
ISSN: 0308-8146
PubMed: 28490136
WoS: 000401097700089
Scopus: 2-s2.0-85017657241
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Institution/Community
Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Peruško, Marija AU - Al-Hanish, Ayah AU - Mihailović-Vesić, Jelena AU - Minić, Simeon L. AU - Trifunović, Sara AU - Prodić, Ivana AU - Ćirković-Veličković, Tanja PY - 2017 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2456 AB - Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved. PB - Elsevier Sci Ltd, Oxford T2 - Food Chemistry T1 - Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction VL - 232 SP - 744 EP - 752 DO - 10.1016/j.foodchem.2017.04.074 ER -
@article{ author = "Peruško, Marija and Al-Hanish, Ayah and Mihailović-Vesić, Jelena and Minić, Simeon L. and Trifunović, Sara and Prodić, Ivana and Ćirković-Veličković, Tanja", year = "2017", abstract = "Major green tea catechin, epigallocatechin-3-gallate (EGCG), binds non-covalently to numerous dietary proteins, including beta-lactoglobulin of cow's milk. The effects of glycation of proteins via Maillard reaction on the binding capacity for polyphenols and the antiradical properties of the formed complexes have not been studied previously. Binding constant of BLG glycated by milk sugar lactose to EGCG was measured by the method of fluorophore quenching. Binding of EGCG was confirmed by CD and FTIR. The antioxidative properties of the complexes were examined by measuring ABTS radical scavenging capacity, superoxide anion scavenging capacity and total reducing power assay. Glycation of BLG does not significantly influence the binding constant of EGCG for the protein. Conformational changes were observed for both native and glycated BLG upon complexation with EGCG. Masking effect of polyphenol complexation on the antioxidative potential of the protein was of the similar degree for both glycated BLG and native BLG. (C) 2017 Elsevier Ltd. All rights reserved.", publisher = "Elsevier Sci Ltd, Oxford", journal = "Food Chemistry", title = "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction", volume = "232", pages = "744-752", doi = "10.1016/j.foodchem.2017.04.074" }
Peruško, M., Al-Hanish, A., Mihailović-Vesić, J., Minić, S. L., Trifunović, S., Prodić, I.,& Ćirković-Veličković, T.. (2017). Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry Elsevier Sci Ltd, Oxford., 232, 744-752. https://doi.org/10.1016/j.foodchem.2017.04.074
Peruško M, Al-Hanish A, Mihailović-Vesić J, Minić SL, Trifunović S, Prodić I, Ćirković-Veličković T. Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction. in Food Chemistry. 2017;232:744-752. doi:10.1016/j.foodchem.2017.04.074 .
Peruško, Marija, Al-Hanish, Ayah, Mihailović-Vesić, Jelena, Minić, Simeon L., Trifunović, Sara, Prodić, Ivana, Ćirković-Veličković, Tanja, "Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction" in Food Chemistry, 232 (2017):744-752, https://doi.org/10.1016/j.foodchem.2017.04.074 . .