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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/40728
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dc.creatorCarini Aparecida Lelispt_BR
dc.creatorGabriel Max Dias Ferreirapt_BR
dc.creatorGuilherme Max Dias Ferreirapt_BR
dc.creatorMaria do Carmo Hespanholpt_BR
dc.creatorMaximiliano Soares Pintopt_BR
dc.creatorLuis Henrique Mendes da Silvapt_BR
dc.creatorAna Clarissa dos Santos Pirespt_BR
dc.date.accessioned2022-04-04T11:49:40Z-
dc.date.available2022-04-04T11:49:40Z-
dc.date.issued2017-09-
dc.citation.volume70pt_BR
dc.citation.spage29pt_BR
dc.citation.epage35pt_BR
dc.identifier.doihttps://doi.org/10.1016/j.foodhyd.2017.03.027pt_BR
dc.identifier.issn0268005Xpt_BR
dc.identifier.urihttp://hdl.handle.net/1843/40728-
dc.description.resumoPonceau 4R (P4R) and bovine serum albumin (BSA) may interact changing food properties. We compared fluorescence spectroscopy and surface plasmon resonance (SPR) for studying, in vitro, the interactions between BSA and P4R at pH 7.4 and 3.5 in different temperatures. Fluorescence data pointed to the formation of a complex where P4R was bound on site I or II of BSA, with a stoichiometry around one and a binding constant (Kb) ranging from 1.37 × 105 to 20.15 × 106 L mol−1. The complex formation at both pH was enthalpically driven (standard enthalpy change, ΔH°F = −60.69 and −63.06 kJ mol−1, for pH 7.4 and 3.5, respectively). Using SPR, we also found the formation of 1:1 BSA-P4R complexes, but the calculated Kb values were much smaller, on the order of 103 L mol−1. Again, we found that the formation of BSA-P4R complex was driven by enthalpy decreasing; however the standard enthalpy change was less negative than that found by fluorescence (ΔH°SPR = −15.05 and −40.55 kJ mol−1, at pH 7.4 and 3.5, respectively). Our results show that these distinct techniques provided different thermodynamic binding parameters for the BSA-P4R interaction, especially regarding ΔH° values, indicating that BSA-P4R binding was a multisite phenomenon, and that sites far from tryptophan residues were the main responsible by electrostatic interaction. Thus, this work clearly shows the importance of using complementary techniques for a complete thermodynamic characterization of complexes formed between azo-colorants and proteins; which is directly related to physicochemical properties of systems containing both molecules together.pt_BR
dc.description.sponsorshipOutra Agênciapt_BR
dc.languageengpt_BR
dc.publisherUniversidade Federal de Minas Geraispt_BR
dc.publisher.countryBrasilpt_BR
dc.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIASpt_BR
dc.publisher.initialsUFMGpt_BR
dc.relation.ispartofFood Hydrocolloidspt_BR
dc.rightsAcesso Restritopt_BR
dc.subject.otherAlbuminapt_BR
dc.subject.otherRessonânciapt_BR
dc.subject.otherEspectroscopia de fluorescênciapt_BR
dc.subject.otherEntropiapt_BR
dc.subject.otherEntalpiapt_BR
dc.subject.otherCorantes sintéticospt_BR
dc.titleDetermination of driving forces for bovine serum albumin-Ponceau4R binding using surface plasmon resonance and fluorescence spectroscopy: a comparative studypt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S0268005X16306075?via%3Dihubpt_BR
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