Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin detected by mass spectrometry
Autori
Minić, SimeonRadomirović, Mirjana Ž.
Savković, Nina
Vasović, Tamara
Nikolić, Milan
Stanić-Vučinić, Dragana
Ćirković-Veličković, Tanja
Konferencijski prilog (Objavljena verzija)
Metapodaci
Prikaz svih podataka o dokumentuApstrakt
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.
Izvor:
IV SePA symposium: Interactomics and glycoproteomics: new approaches in large-scale protein analysis, Belgrade, Serbia, 25th May, 2018. In: Book of Abstracts, 2018, 11-11Izdavač:
- Beograd : Srpsko udruženje za proteomiku
Finansiranje / projekti:
- Molekularne osobine i modifikacije nekih respiratornih i nutritivnih alergena (RS-MESTD-Basic Research (BR or ON)-172024)
Kolekcije
Institucija/grupa
Hemijski fakultet / Faculty of ChemistryTY - 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 .