Antioxidative capacity and binding affinity of the complex of green tea catechin and beta-lactoglobulin glycated by the Maillard reaction
Само за регистроване кориснике
2017
Аутори
Perusko, MarijaAl-Hanish, Ayah
Mihailović, Jelena
Minić, Simeon
Trifunović, Sara
Prodić, Ivana
Cirkovic Velicković, Tanja
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Кључне речи:
Tea / Protein polyphenol interactions / Maillard reaction / Glycation / Epigallocatechin-3-gallate / Beta-lactoglobulinИзвор:
Food Chemistry, 2017, 232, 744-752Издавач:
- Elsevier Sci Ltd, Oxford
Финансирање / пројекти:
- Молекуларне особине и модификације неких респираторних и нутритивних алергена (RS-MESTD-Basic Research (BR or ON)-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-FP7-256716)
DOI: 10.1016/j.foodchem.2017.04.074
ISSN: 0308-8146
PubMed: 28490136
WoS: 000401097700089
Scopus: 2-s2.0-85017657241
Институција/група
TorlakTY - JOUR AU - Perusko, Marija AU - Al-Hanish, Ayah AU - Mihailović, Jelena AU - Minić, Simeon AU - Trifunović, Sara AU - Prodić, Ivana AU - Cirkovic Velicković, Tanja PY - 2017 UR - http://intor.torlakinstitut.com/handle/123456789/757 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. 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 EP - 752 SP - 744 VL - 232 DO - 10.1016/j.foodchem.2017.04.074 ER -
@article{ author = "Perusko, Marija and Al-Hanish, Ayah and Mihailović, Jelena and Minić, Simeon and Trifunović, Sara and Prodić, Ivana and Cirkovic Velicković, 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.", 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", pages = "752-744", volume = "232", doi = "10.1016/j.foodchem.2017.04.074" }
Perusko, M., Al-Hanish, A., Mihailović, J., Minić, S., Trifunović, S., Prodić, I.,& Cirkovic Velicković, 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
Perusko M, Al-Hanish A, Mihailović J, Minić S, Trifunović S, Prodić I, Cirkovic Velicković 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 .
Perusko, Marija, Al-Hanish, Ayah, Mihailović, Jelena, Minić, Simeon, Trifunović, Sara, Prodić, Ivana, Cirkovic Velicković, 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 . .