TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3186
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - DATA
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3187
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3187
ER  - 

@misc{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3187"
}

Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. in Food Chemistry
Elsevier Sci Ltd, Oxford..
https://hdl.handle.net/21.15107/rcub_cherry_3187

Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138. in Food Chemistry. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3187 .

Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Supplementary material for the article: Minic, S.; Radomirovic, M.; Savkovic, N.; Radibratovic, M.; Mihailovic, J.; Vasovic, T.; Nikolic, M.; Milcic, M.; Stanic-Vucinic, D.; Cirkovic Velickovic, T. Covalent Binding of 
Food-Derived Blue Pigment Phycocyanobilin to Bovine β-Lactoglobulin under Physiological Conditions. Food Chemistry 2018, 269, 43–52. https://doi.org/10.1016/j.foodchem.2018.06.138" in Food Chemistry (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3187 .

TY  - CONF
AU  - Minić, Simeon
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6041
AB  - Objective. Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin (C-PC),  the major chromoprotein of cyanobacteria Spirulina platensis. It is covalently attached to cysteine residues of C-PC via thioether bond. β-lactoglobulin, the major whey protein, is frequently used as an additive in food products due to its various techno-functional properties. This study aimed to investigate covalent binding of bioactive PCB to bovine β-lactoglobulin.

Material and Methods. Combination of fluoresence spectroscopy, mass spectrometry and electrophoretic techniques was employed in order to examine covalent binding of PCB to BLG. Effects of PCB binding on secondary and tertiary structure of BLG were studied by CD spectroscopy.

Results. SDS-PAGE with Zn2+ staining and fluorescence spectroscopy have revealed that PCB covalently binds to BLG via free cysteine residue, with binding constant of 4 x 105 M-1. BLG-PCB covalent adduct has been detected by mass spectrometry, with both isoforms of BLG being modified to similar extent. Binding of PCB influences secondary and tertiary structure of BLG, while BLG-PCB adduct has altered secondary and tertiary structure in comparison to native BLG.

Conclusions. Our results indicate that BLG, modified by PCB, could serve as suitable oral delivery system of bioactive tetrapyrrole chromophore. Covalent modification of BLG at the same time represents a feasible strategy to impart new functionalities to this important food protein.
PB  - Beograd : Srpsko udruženje za proteomiku
C3  - IV SePA symposium: Interactomics and glycoproteomics: new approaches in large-scale protein analysis, Belgrade, Serbia, 25th May, 2018. In: Book of Abstracts
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin detected by mass spectrometry
SP  - 11
EP  - 11
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6041
ER  - 

@conference{
author = "Minić, Simeon and Radomirović, Mirjana Ž. and Savković, Nina and Vasović, Tamara and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "Objective. Phycocyanobilin (PCB) is a blue tetrapyrrole chromophore of C-phycocyanin (C-PC),  the major chromoprotein of cyanobacteria Spirulina platensis. It is covalently attached to cysteine residues of C-PC via thioether bond. β-lactoglobulin, the major whey protein, is frequently used as an additive in food products due to its various techno-functional properties. This study aimed to investigate covalent binding of bioactive PCB to bovine β-lactoglobulin.

Material and Methods. Combination of fluoresence spectroscopy, mass spectrometry and electrophoretic techniques was employed in order to examine covalent binding of PCB to BLG. Effects of PCB binding on secondary and tertiary structure of BLG were studied by CD spectroscopy.

Results. SDS-PAGE with Zn2+ staining and fluorescence spectroscopy have revealed that PCB covalently binds to BLG via free cysteine residue, with binding constant of 4 x 105 M-1. BLG-PCB covalent adduct has been detected by mass spectrometry, with both isoforms of BLG being modified to similar extent. Binding of PCB influences secondary and tertiary structure of BLG, while BLG-PCB adduct has altered secondary and tertiary structure in comparison to native BLG.

Conclusions. Our results indicate that BLG, modified by PCB, could serve as suitable oral delivery system of bioactive tetrapyrrole chromophore. Covalent modification of BLG at the same time represents a feasible strategy to impart new functionalities to this important food protein.",
publisher = "Beograd : Srpsko udruženje za proteomiku",
journal = "IV SePA symposium: Interactomics and glycoproteomics: new approaches in large-scale protein analysis, Belgrade, Serbia, 25th May, 2018. In: Book of Abstracts",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin detected by mass spectrometry",
pages = "11-11",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6041"
}

Minić, S., Radomirović, M. Ž., Savković, N., Vasović, T., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin detected by mass spectrometry. in IV SePA symposium: Interactomics and glycoproteomics: new approaches in large-scale protein analysis, Belgrade, Serbia, 25th May, 2018. In: Book of Abstracts
Beograd : Srpsko udruženje za proteomiku., 11-11.
https://hdl.handle.net/21.15107/rcub_cherry_6041

Minić S, Radomirović MŽ, Savković N, Vasović T, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin detected by mass spectrometry. in IV SePA symposium: Interactomics and glycoproteomics: new approaches in large-scale protein analysis, Belgrade, Serbia, 25th May, 2018. In: Book of Abstracts. 2018;:11-11.
https://hdl.handle.net/21.15107/rcub_cherry_6041 .

Minić, Simeon, Radomirović, Mirjana Ž., Savković, Nina, Vasović, Tamara, Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin detected by mass spectrometry" in IV SePA symposium: Interactomics and glycoproteomics: new approaches in large-scale protein analysis, Belgrade, Serbia, 25th May, 2018. In: Book of Abstracts (2018):11-11,
https://hdl.handle.net/21.15107/rcub_cherry_6041 .

TY  - JOUR
AU  - Minić, Simeon L.
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Radibratović, Milica
AU  - Mihailović-Vesić, Jelena
AU  - Vasović, Tamara
AU  - Nikolić, Milan
AU  - Milčić, Miloš K.
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2197
AB  - In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.
PB  - Elsevier Sci Ltd, Oxford
T2  - Food Chemistry
T1  - Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions
VL  - 269
SP  - 43
EP  - 52
DO  - 10.1016/j.foodchem.2018.06.138
ER  - 

@article{
author = "Minić, Simeon L. and Radomirović, Mirjana Ž. and Savković, Nina and Radibratović, Milica and Mihailović-Vesić, Jelena and Vasović, Tamara and Nikolić, Milan and Milčić, Miloš K. and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
abstract = "In this study, we investigated structural aspects of covalent binding of food derived blue pigment phycocyanobilin (PCB) to bovine beta-lactoglobulin (BLG), major whey protein, by spectroscopic, electrophoretic, mass spectrometry and computational methods. At physiological pH (7.2), we found that covalent pigment binding via free cysteine residue is slow (k(a)=0.065 min(-1)), of moderate affinity (K-a=4x10(4) M-1), and stereo-selective. Binding also occurs at a broad pH range and under simulated gastrointestinal conditions. Adduct formation rises with pH, and in concentrated urea (k(a)=0.101 min(-1)). The BLG-PCB adduct has slightly altered secondary and tertiary protein structure, and bound PCB has higher fluorescence and more stretched conformation than free chromophore. Combination of steered molecular dynamic for disulfide exchange, non-covalent and covalent docking, favours Cys119 residue in protein calyx as target for covalent BLG-PCB adduct formation. Our results suggest that this adduct can serve as delivery system of bioactive PCB.",
publisher = "Elsevier Sci Ltd, Oxford",
journal = "Food Chemistry",
title = "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions",
volume = "269",
pages = "43-52",
doi = "10.1016/j.foodchem.2018.06.138"
}

Minić, S. L., Radomirović, M. Ž., Savković, N., Radibratović, M., Mihailović-Vesić, J., Vasović, T., Nikolić, M., Milčić, M. K., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry
Elsevier Sci Ltd, Oxford., 269, 43-52.
https://doi.org/10.1016/j.foodchem.2018.06.138

Minić SL, Radomirović MŽ, Savković N, Radibratović M, Mihailović-Vesić J, Vasović T, Nikolić M, Milčić MK, Stanić-Vučinić D, Ćirković-Veličković T. Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions. in Food Chemistry. 2018;269:43-52.
doi:10.1016/j.foodchem.2018.06.138 .

Minić, Simeon L., Radomirović, Mirjana Ž., Savković, Nina, Radibratović, Milica, Mihailović-Vesić, Jelena, Vasović, Tamara, Nikolić, Milan, Milčić, Miloš K., Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Covalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditions" in Food Chemistry, 269 (2018):43-52,
https://doi.org/10.1016/j.foodchem.2018.06.138 . .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Minić, Simeon L.
AU  - Savković, Nina
AU  - Vasović, T.
AU  - Nikolić, Milan
AU  - Stanić-Vučinić, Dragana
AU  - Ćirković-Veličković, Tanja
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2175
PB  - Wiley, Hoboken
C3  - FEBS OPEN BIO
T1  - Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects
VL  - 8
SP  - 97
EP  - 97
UR  - https://hdl.handle.net/21.15107/rcub_cherry_2175
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Minić, Simeon L. and Savković, Nina and Vasović, T. and Nikolić, Milan and Stanić-Vučinić, Dragana and Ćirković-Veličković, Tanja",
year = "2018",
publisher = "Wiley, Hoboken",
journal = "FEBS OPEN BIO",
title = "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects",
volume = "8",
pages = "97-97",
url = "https://hdl.handle.net/21.15107/rcub_cherry_2175"
}

Radomirović, M. Ž., Minić, S. L., Savković, N., Vasović, T., Nikolić, M., Stanić-Vučinić, D.,& Ćirković-Veličković, T.. (2018). Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. in FEBS OPEN BIO
Wiley, Hoboken., 8, 97-97.
https://hdl.handle.net/21.15107/rcub_cherry_2175

Radomirović MŽ, Minić SL, Savković N, Vasović T, Nikolić M, Stanić-Vučinić D, Ćirković-Veličković T. Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects. in FEBS OPEN BIO. 2018;8:97-97.
https://hdl.handle.net/21.15107/rcub_cherry_2175 .

Radomirović, Mirjana Ž., Minić, Simeon L., Savković, Nina, Vasović, T., Nikolić, Milan, Stanić-Vučinić, Dragana, Ćirković-Veličković, Tanja, "Beta-lactoglobulin covalent modification by phycocyanobilin under physiological conditions: structural and functional effects" in FEBS OPEN BIO, 8 (2018):97-97,
https://hdl.handle.net/21.15107/rcub_cherry_2175 .

TY  - CONF
AU  - Radomirović, Mirjana Ž.
AU  - Savković, Nina
AU  - Minić, Simeon
AU  - Stanić-Vučinić, Dragana
AU  - Nikolić, Milan
AU  - Ćirković-Veličković, Tanja
PY  - 2017
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6042
AB  - Bovine β-lactoglobulin (BLG) is the major whey protein, with significant techno-functional properties and big potential for application in food industry. A blue tetrapyrrole chromophore with exceptional antioxidant activity, phycocyanobilin (PCB) is covalently bound to cysteine (Cys) residues of C-phycocyanin, major protein of cyanobacteria. This paper characterized covalent binding of PCB to BLG, under physiological conditions, using spectroscopic and electrophoretic techniques. It was shown that PCB is bound to Cys-121 residue of BLG as P conformer, with binding constant of 105 M-1. In comparison to free BLG, the covalently modified protein has an altered tertiary structure, as well as the content of secondary structures. Upon heating, modified protein is less susceptible to oligomerization and the amyloid formation. Furthermore, obtained BLG-PCB covalent adduct (blue neo-chromoprotein) has increased antioxidant potential, as well as higher resistance to pepsin and pancreatin digestion than the unmodified protein. Our findings indicate that the covalent BLG-PCB adduct has improved bioactive and techno-functional properties in comparison to the free protein.
PB  - Beograd : Srpsko hemijsko društvo
C3  - 54th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 29th-30th September, 2017. In: Book of Abstracts and Proceedings
T1  - Characterization and effects of covalent binding of phycocyanobilin to bovine β-lactoglobulin
SP  - 59
EP  - 59
UR  - https://hdl.handle.net/21.15107/rcub_cherry_6042
ER  - 

@conference{
author = "Radomirović, Mirjana Ž. and Savković, Nina and Minić, Simeon and Stanić-Vučinić, Dragana and Nikolić, Milan and Ćirković-Veličković, Tanja",
year = "2017",
abstract = "Bovine β-lactoglobulin (BLG) is the major whey protein, with significant techno-functional properties and big potential for application in food industry. A blue tetrapyrrole chromophore with exceptional antioxidant activity, phycocyanobilin (PCB) is covalently bound to cysteine (Cys) residues of C-phycocyanin, major protein of cyanobacteria. This paper characterized covalent binding of PCB to BLG, under physiological conditions, using spectroscopic and electrophoretic techniques. It was shown that PCB is bound to Cys-121 residue of BLG as P conformer, with binding constant of 105 M-1. In comparison to free BLG, the covalently modified protein has an altered tertiary structure, as well as the content of secondary structures. Upon heating, modified protein is less susceptible to oligomerization and the amyloid formation. Furthermore, obtained BLG-PCB covalent adduct (blue neo-chromoprotein) has increased antioxidant potential, as well as higher resistance to pepsin and pancreatin digestion than the unmodified protein. Our findings indicate that the covalent BLG-PCB adduct has improved bioactive and techno-functional properties in comparison to the free protein.",
publisher = "Beograd : Srpsko hemijsko društvo",
journal = "54th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 29th-30th September, 2017. In: Book of Abstracts and Proceedings",
title = "Characterization and effects of covalent binding of phycocyanobilin to bovine β-lactoglobulin",
pages = "59-59",
url = "https://hdl.handle.net/21.15107/rcub_cherry_6042"
}

Radomirović, M. Ž., Savković, N., Minić, S., Stanić-Vučinić, D., Nikolić, M.,& Ćirković-Veličković, T.. (2017). Characterization and effects of covalent binding of phycocyanobilin to bovine β-lactoglobulin. in 54th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 29th-30th September, 2017. In: Book of Abstracts and Proceedings
Beograd : Srpsko hemijsko društvo., 59-59.
https://hdl.handle.net/21.15107/rcub_cherry_6042

Radomirović MŽ, Savković N, Minić S, Stanić-Vučinić D, Nikolić M, Ćirković-Veličković T. Characterization and effects of covalent binding of phycocyanobilin to bovine β-lactoglobulin. in 54th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 29th-30th September, 2017. In: Book of Abstracts and Proceedings. 2017;:59-59.
https://hdl.handle.net/21.15107/rcub_cherry_6042 .

Radomirović, Mirjana Ž., Savković, Nina, Minić, Simeon, Stanić-Vučinić, Dragana, Nikolić, Milan, Ćirković-Veličković, Tanja, "Characterization and effects of covalent binding of phycocyanobilin to bovine β-lactoglobulin" in 54th Meeting of the Serbian Chemical Society, Belgrade, Serbia, 29th-30th September, 2017. In: Book of Abstracts and Proceedings (2017):59-59,
https://hdl.handle.net/21.15107/rcub_cherry_6042 .