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Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin under physiological conditions

(2018) FOOD CHEMISTRY. 269. p.43-52
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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.
Keywords
C-PHYCOCYANIN, SPIRULINA-PLATENSIS, IN-VITRO, CHROMOPHORE ATTACHMENT, ALLYL ISOTHIOCYANATE, HEAT, AGGREGATION, DENATURATION, PURIFICATION, BILIPROTEIN, beta-lactoglobulin, Phycocyanobilin, Phycocyanin, Covalent, Binding, Spirulina, Fluorescence, Molecular docking

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Citation

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MLA
Minic, Simeon et al. “Covalent Binding of Food-derived Blue Pigment Phycocyanobilin to Bovine Β-lactoglobulin Under Physiological Conditions.” FOOD CHEMISTRY 269 (2018): 43–52. Print.
APA
Minic, S., Radomirovic, M., Savkovic, N., Radibratovic, M., Mihailovic, J., Vasovic, T., Nikolic, M., et al. (2018). Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin under physiological conditions. FOOD CHEMISTRY, 269, 43–52.
Chicago author-date
Minic, Simeon, Mirjana Radomirovic, Nina Savkovic, Milica Radibratovic, Jelena Mihailovic, Tamara Vasovic, Milan Nikolic, Milos Milcic, Dragana Stanic-Vucinic, and Tanja Cirkovic Velickovic. 2018. “Covalent Binding of Food-derived Blue Pigment Phycocyanobilin to Bovine Β-lactoglobulin Under Physiological Conditions.” Food Chemistry 269: 43–52.
Chicago author-date (all authors)
Minic, Simeon, Mirjana Radomirovic, Nina Savkovic, Milica Radibratovic, Jelena Mihailovic, Tamara Vasovic, Milan Nikolic, Milos Milcic, Dragana Stanic-Vucinic, and Tanja Cirkovic Velickovic. 2018. “Covalent Binding of Food-derived Blue Pigment Phycocyanobilin to Bovine Β-lactoglobulin Under Physiological Conditions.” Food Chemistry 269: 43–52.
Vancouver
1.
Minic S, Radomirovic M, Savkovic N, Radibratovic M, Mihailovic J, Vasovic T, et al. Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin under physiological conditions. FOOD CHEMISTRY. 2018;269:43–52.
IEEE
[1]
S. Minic et al., “Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin under physiological conditions,” FOOD CHEMISTRY, vol. 269, pp. 43–52, 2018.
@article{8573715,
  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.},
  author       = {Minic, Simeon and Radomirovic, Mirjana and Savkovic, Nina and Radibratovic, Milica and Mihailovic, Jelena and Vasovic, Tamara and Nikolic, Milan and Milcic, Milos and Stanic-Vucinic, Dragana and Cirkovic Velickovic, Tanja},
  issn         = {0308-8146},
  journal      = {FOOD CHEMISTRY},
  keywords     = {C-PHYCOCYANIN,SPIRULINA-PLATENSIS,IN-VITRO,CHROMOPHORE ATTACHMENT,ALLYL ISOTHIOCYANATE,HEAT,AGGREGATION,DENATURATION,PURIFICATION,BILIPROTEIN,beta-lactoglobulin,Phycocyanobilin,Phycocyanin,Covalent,Binding,Spirulina,Fluorescence,Molecular docking},
  language     = {eng},
  pages        = {43--52},
  title        = {Covalent binding of food-derived blue pigment phycocyanobilin to bovine β-lactoglobulin under physiological conditions},
  url          = {http://dx.doi.org/10.1016/j.foodchem.2018.06.138},
  volume       = {269},
  year         = {2018},
}

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