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dc.creatorJovanović, Zorana
dc.creatorVeličković, Luka
dc.creatorGligorijević, Nikola
dc.creatorŠunderić, Miloš
dc.creatorZoumpanioti, Maria
dc.creatorMinić, Simeon L.
dc.creatorNikolić, Milan
dc.date.accessioned2023-01-31T11:59:29Z
dc.date.available2023-01-31T11:59:29Z
dc.date.issued2022
dc.identifier.isbn978-86-7220-124-6
dc.identifier.urihttp://cherry.chem.bg.ac.rs/handle/123456789/5785
dc.description.abstractTo minimize the impact of artificial food colouring (e.g., in drinks) on health, chemical dyes are increasingly replaced by natural ones. C-phycocyanin (C-PC), hexameric light-harvesting phycobiliprotein from cyanobacteria Artrhorspira platensis, has been proposed as an alternative. The intensive blue colour of C-PC arises from phycocyanobilin (PCB), the covalently attached tetrapyrrole chromophores. The presence of PCB chromophores gives C-PC a broad range of bioactive effects (antioxidant, anticancer, and immunomodulatory ones), substantially increasing their potential for applications in the food industry. However, C-PC issensitive to temperature, and its colour significantly diminishes by thermal treatment, limiting its use in the food industry. Hence, improving C-PC stability is the major challenge for successful application in food and beverage colouring. It is well known that binding small, high-affinity ligands significantly improve protein stability. Therefore, selecting food-derived ligands (such as vitamins, polyphenols, sugars, etc.) with the ability to bind C-PC firmly could be a promising strategy to increase the C-PC stability and preserve its colour, which should increase its application potential in the food industry. The main aim of this study is to characterize the binding of selected food-derived ligands (including quercetin, coenzyme Q10, gallic acid, vanillic acid, vanillin, resveratrol, glucose, fructose, sucrose, vitamin K, menthol, and dihydrolipoic acid) to C-PC by standard spectroscopic methods (UV/VIS absorption spectroscopy, spectrofluorimetry, and CD spectroscopy). Quercetin has the strongest binding affinity to C-PC (Ka~3.7x105 M-1 ), and its effects on C-PC structure and stability have been further investigated. CD spectroscopy revealed that quercetin induces stabilization of the protein secondary structure under simulated physiological conditions, while the conformation of the PCB chromophore is altered upon quercetin binding. Furthermore, quercetin binding increases the thermal stability of C-PC. Overall, our study revealed the ability of high-affinity, food-derived ligands to increase the stability of C-PC, which may enhance its application potential in the food industry.sr
dc.language.isoensr
dc.publisherBelgrade : Faculty of Chemistrysr
dc.relationinfo:eu-repo/grantAgreement/MESTD/inst-2020/200288/RS//sr
dc.relationANSO, Project No. ANSO-CR-PP-2021-01sr
dc.rightsopenAccesssr
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceSerbian Biochemical Society, Eleventh Conference, Scientific meeting of an international character: "Amazing Biochemistry"; 2022 Sep 22-23; Novi Sad, Serbiasr
dc.subjectC-phycocyaninsr
dc.subjectcoloursr
dc.subjectfood-derived ligandssr
dc.subjectQuercetinsr
dc.titleC-Phycocyanin from cyanobacteria Artrhorspira platensis: Binding of selected food-derived ligandssr
dc.typeconferenceObjectsr
dc.rights.licenseBYsr
dc.citation.spage165
dc.citation.epage165
dc.type.versionpublishedVersionsr
dc.identifier.fulltexthttp://cherry.chem.bg.ac.rs/bitstream/id/32398/C-Phycocyanin_from_pub_2022.pdf
dc.identifier.rcubhttps://hdl.handle.net/21.15107/rcub_cherry_5785


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