Influence of protein conformation and selected Hofmeister salts on bovine serum albumin/lutein complex formation

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dc.creatorPaulo Henrique Costa Paiva
dc.creatorYara Luiza Coelho
dc.creatorLuís Henrique Mendes da Silva
dc.creatorMaximiliano Soares Pinto
dc.creatorMárcia Cristina Teixeira Rodrigues Vidigal
dc.creatorAna Clarissa dos Santos Pires
dc.date.accessioned2022-04-26T14:59:54Z
dc.date.accessioned2025-09-08T23:40:00Z
dc.date.available2022-04-26T14:59:54Z
dc.date.issued2020-02
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.2019.125463
dc.identifier.issn0308-8146
dc.identifier.urihttps://hdl.handle.net/1843/41155
dc.languageeng
dc.publisherUniversidade Federal de Minas Gerais
dc.relation.ispartofFood Chemistry
dc.rightsAcesso Aberto
dc.subjectAlbumina
dc.subjectEspectroscopia de fluorescência
dc.subjectTermodinâmica
dc.titleInfluence of protein conformation and selected Hofmeister salts on bovine serum albumin/lutein complex formation
dc.typeArtigo de periódico
local.citation.spage125463
local.citation.volume305
local.description.resumoProtein conformation and the 3D water structure play important roles in the ability of bovine serum albumin (BSA) to form stable nanostructures with bioactive molecules. We studied the influence of BSA unfolding and those of two Hofmeister salts, sodium chloride (NaCl) as kosmotrope and sodium thiocyanate (NaSCN) as chaotrope, on BSA/lutein binding at pH 7.4 using fluorescence spectroscopy. The BSA/lutein complex formation was entropically driven and lutein was preferentially bound to site III of BSA. The binding constant (104 L mol−1), complex stoichiometry (1:1), and thermodynamic potential for BSA/lutein binding were independent of protein conformation and Hofmeister salts. However, the enthalpic and entropic components of BSA/lutein binding in the presence of NaSCN decreased as the temperature increased. The opposite was observed for BSA/lutein binding in the presence of NaCl and for denatured BSA/lutein binding. Therefore, the BSA conformation and 3D water structure directly affected the BSA/lutein binding
local.publisher.countryBrasil
local.publisher.departmentICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS
local.publisher.initialsUFMG
local.url.externahttps://www.sciencedirect.com/science/article/pii/S030881461931578X?via%3Dihub#!

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