TY  - 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 . .

TY  - JOUR
AU  - Al-Hanish, Ayah
AU  - Stanić-Vučinić, Dragana
AU  - Mihailović-Vesić, Jelena
AU  - Prodić, Ivana
AU  - Minić, Simeon L.
AU  - Stojadinović, Marija M.
AU  - Radibratović, Milica
AU  - Milčić, Miloš K.
AU  - Ćirković-Veličković, Tanja
PY  - 2016
UR  - http://intor.torlakinstitut.com/handle/123456789/759
AB  - Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Hydrocolloids
T1  - Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate
EP  - 250
SP  - 241
VL  - 61
DO  - 10.1016/j.foodhyd.2016.05.012
ER  - 

@article{
author = "Al-Hanish, Ayah and Stanić-Vučinić, Dragana and Mihailović-Vesić, Jelena and Prodić, Ivana and Minić, Simeon L. and Stojadinović, Marija M. and Radibratović, Milica and Milčić, Miloš K. and Ćirković-Veličković, Tanja",
year = "2016",
abstract = "Bovine alpha-lactalbumin (ALA) is an important Ca-binding protein of milk. Epigallocatechin-3-gallate (EGCG) is the major and the most biologically active catechin of green tea, which has the highest binding affinity to whey proteins due to galloyl functional group. In this study experimental and computational methods were used to investigate noncovalent interactions of EGCG and ALA. Binding affinity of EGCG for ALA, determined by fluorescence quenching analysis, was in the range described for complexes of EGCG and other dietary proteins, and lower than affinity of some phenolic compounds to ALA. Based on circular dichroism and Fourier transform infrared spectroscopy spectra, binding of EGCG change ALA conformation inducing alpha-helix to beta-structures transition. The isothermal titration calorimetry results suggest that the binding of EGCG to ALA is enthalpically favorable. The docking analysis shows that EGCG binds in the hydrophobic pocket at the entrance of cleft between alpha-helical and beta-sheetrich domains and includes residues of aromatic cluster II. Uptake of ALA by monocytes proceeds at a slower rate in the presence of EGCG suggesting that EGCG binding may impair uptake of ALA by antigen-presenting cells. ALA, being of low cost and widely available protein, can serve as suitable delivery system for EGCG, as well as for food fortification with this bioactive catechin. (C) 2016 Elsevier Ltd. All rights reserved.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Hydrocolloids",
title = "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate",
pages = "250-241",
volume = "61",
doi = "10.1016/j.foodhyd.2016.05.012"
}

Al-Hanish, A., Stanić-Vučinić, D., Mihailović-Vesić, J., Prodić, I., Minić, S. L., Stojadinović, M. M., Radibratović, M., Milčić, M. K.,& Ćirković-Veličković, T.. (2016). Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids
Elsevier Sci Ltd, Oxford., 61, 241-250.
https://doi.org/10.1016/j.foodhyd.2016.05.012

Al-Hanish A, Stanić-Vučinić D, Mihailović-Vesić J, Prodić I, Minić SL, Stojadinović MM, Radibratović M, Milčić MK, Ćirković-Veličković T. Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate. in Food Hydrocolloids. 2016;61:241-250.
doi:10.1016/j.foodhyd.2016.05.012 .

Al-Hanish, Ayah, Stanić-Vučinić, Dragana, Mihailović-Vesić, Jelena, Prodić, Ivana, Minić, Simeon L., Stojadinović, Marija M., Radibratović, Milica, Milčić, Miloš K., Ćirković-Veličković, Tanja, "Noncovalent interactions of bovine alpha-lactalbumin with green tea polyphenol, epigalocatechin-3-gallate" in Food Hydrocolloids, 61 (2016):241-250,
https://doi.org/10.1016/j.foodhyd.2016.05.012 . .