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Please use this identifier to cite or link to this item: http://hdl.handle.net/1843/41155
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dc.creatorPaulo Henrique Costa Paivapt_BR
dc.creatorYara Luiza Coelhopt_BR
dc.creatorLuís Henrique Mendes da Silvapt_BR
dc.creatorMaximiliano Soares Pintopt_BR
dc.creatorMárcia Cristina Teixeira Rodrigues Vidigalpt_BR
dc.creatorAna Clarissa dos Santos Pirespt_BR
dc.date.accessioned2022-04-26T14:59:54Z-
dc.date.available2022-04-26T14:59:54Z-
dc.date.issued2020-02-
dc.citation.volume305pt_BR
dc.citation.spage125463pt_BR
dc.identifier.doihttps://doi.org/10.1016/j.foodchem.2019.125463pt_BR
dc.identifier.issn0308-8146pt_BR
dc.identifier.urihttp://hdl.handle.net/1843/41155-
dc.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 bindingpt_BR
dc.description.sponsorshipCNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológicopt_BR
dc.description.sponsorshipFAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Geraispt_BR
dc.description.sponsorshipCAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superiorpt_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 Chemistrypt_BR
dc.rightsAcesso Abertopt_BR
dc.subject.otherAlbuminapt_BR
dc.subject.otherEspectroscopia de fluorescênciapt_BR
dc.subject.otherTermodinâmicapt_BR
dc.titleInfluence of protein conformation and selected Hofmeister salts on bovine serum albumin/lutein complex formationpt_BR
dc.typeArtigo de Periódicopt_BR
dc.url.externahttps://www.sciencedirect.com/science/article/pii/S030881461931578X?via%3Dihub#!pt_BR
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