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

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2018
Authors
Minic, Simeon
Radomirović, Mirjana
Savkovic, Nina
Radibratović, Milica
Mihailović, Jelena
Vasovic, Tamara
Nikolić, Milan
Milčić, Miloš
Stanić-Vučinić, Dragana
Ćirković Veličković, Tanja
Article (Published version)
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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 th...is adduct can serve as delivery system of bioactive PCB.

Keywords:
beta-lactoglobulin / Phycocyanobilin / Phycocyanin / Covalent / Binding / Spirulina / Fluorescence / Molecular docking
Source:
Food Chemistry, 2018, 269, 43-52
Publisher:
  • Elsevier Sci Ltd, Oxford
Projects:
  • Molecular properties and modifications of some respiratory and nutritional allergens (RS-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-256716)
Note:
  • The peer-reviewed version: http://cer.ihtm.bg.ac.rs/handle/123456789/3022

DOI: 10.1016/j.foodchem.2018.06.138

ISSN: 0308-8146

PubMed: 30100456

WoS: 000441142100006

Scopus: 2-s2.0-85049319228
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URI
http://cer.ihtm.bg.ac.rs/handle/123456789/2420
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