Binding thermodynamics of synthetic dye Allura Red with bovine serum albumin

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dc.creatorCarini Aparecida Lelis
dc.creatorEliara Acipreste Hudson
dc.creatorGuilherme Max Dias Ferreira
dc.creatorGabriel Max Dias Ferreira
dc.creatorLuis Henrique Mendes da Silva
dc.creatorMaria do Carmo Hespanhol da Silva
dc.creatorMaximiliano Soares Pinto
dc.creatorAna Clarissa dos Santos Pires
dc.date.accessioned2022-03-29T12:01:01Z
dc.date.accessioned2025-09-08T23:40:22Z
dc.date.available2022-03-29T12:01:01Z
dc.date.issued2017-02-15
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Gerais
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior
dc.description.sponsorshipOutra Agência
dc.identifier.doihttps://doi.org/10.1016/j.foodchem.2016.08.080
dc.identifier.issn03088146
dc.identifier.urihttps://hdl.handle.net/1843/40549
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofFood Chemistry
dc.rightsAcesso Restrito
dc.subjectAlbumina
dc.subjectTermodinâmica
dc.subjectFluorescência
dc.subjectEntalpia
dc.subjectCorantes em alimentos
dc.subjectCorantes sintéticos
dc.titleBinding thermodynamics of synthetic dye Allura Red with bovine serum albumin
dc.typeArtigo de periódico
local.citation.epage58
local.citation.spage52
local.citation.volume217
local.description.resumoThe interaction between Allura Red and bovine serum albumin (BSA) was studied in vitro at pH 7.4. The fluorescence quenching was classified as static quenching due to the formation of AR–BSA complex, with binding constant (K) ranging from 3.26 ± 0.09 to 8.08 ± 0.06 104 L.mol−1, at the warfarin binding site of BSA. This complex formation was driven by increasing entropy. Isothermal titration calorimetric measurements also showed an enthalpic contribution. The Allura Red diffusion coefficient determined by the Taylor-Aris technique corroborated these results because it reduced with increasing BSA concentration. Interfacial tension measurements showed that the AR–BSA complex presented surface activity, since interfacial tension of the water-air interface decreased as the colorant concentration increased. This technique also provided a complexation stoichiometry similar to those obtained by fluorimetric experiments. This work contributes to the knowledge of interactions between BSA and azo colorants under physiological conditions.
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S0308814616313206?via%3Dihub

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