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dc.creatorMinic, Simeon
dc.creatorRadomirović, Mirjana
dc.creatorSavkovic, Nina
dc.creatorRadibratović, Milica
dc.creatorMihailović, Jelena
dc.creatorVasovic, Tamara
dc.creatorNikolić, Milan
dc.creatorMilčić, Miloš
dc.creatorStanic-Vucinic, Dragana
dc.creatorĆirković Veličković, Tanja
dc.date.accessioned2019-01-30T18:00:07Z
dc.date.available2019-01-30T18:00:07Z
dc.date.issued2018
dc.identifier.issn0308-8146
dc.identifier.urihttp://cer.ihtm.bg.ac.rs/handle/123456789/2420
dc.description.abstractIn 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.en
dc.publisherElsevier Sci Ltd, Oxford
dc.relationinfo:eu-repo/grantAgreement/MESTD/Basic Research (BR or ON)/172024/RS//
dc.relationinfo:eu-repo/grantAgreement/EC/FP7/256716/EU//
dc.rightsrestrictedAccess
dc.sourceFood Chemistry
dc.subjectbeta-lactoglobulinen
dc.subjectPhycocyanobilinen
dc.subjectPhycocyaninen
dc.subjectCovalenten
dc.subjectBindingen
dc.subjectSpirulinaen
dc.subjectFluorescenceen
dc.subjectMolecular dockingen
dc.titleCovalent binding of food-derived blue pigment phycocyanobilin to bovine beta-lactoglobulin under physiological conditionsen
dc.typearticle
dc.rights.licenseARR
dcterms.abstractСтаниц-Вуциниц, Драгана; Николиц, Милан; Михаиловиц, Јелена; Радибратовић, Милица; Милциц, Милос; Васовиц, Тамара; Савковиц, Нина; Миниц, Симеон; Велицковиц, Тања Цирковиц; Радомировиц, Мирјана;
dc.citation.volume269
dc.citation.spage43
dc.citation.epage52
dc.citation.other269: 43-52
dc.citation.rankaM21
dc.description.otherThe peer-reviewed version: [http://cer.ihtm.bg.ac.rs/handle/123456789/3022]
dc.identifier.pmid30100456
dc.identifier.doi10.1016/j.foodchem.2018.06.138
dc.identifier.rcubConv_3976
dc.identifier.scopus2-s2.0-85049319228
dc.identifier.wos000441142100006
dc.type.versionpublishedVersion


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