Please use this identifier to cite or link to this item:
http://hdl.handle.net/1843/41155
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.creator | Paulo Henrique Costa Paiva | pt_BR |
dc.creator | Yara Luiza Coelho | pt_BR |
dc.creator | Luís Henrique Mendes da Silva | pt_BR |
dc.creator | Maximiliano Soares Pinto | pt_BR |
dc.creator | Márcia Cristina Teixeira Rodrigues Vidigal | pt_BR |
dc.creator | Ana Clarissa dos Santos Pires | pt_BR |
dc.date.accessioned | 2022-04-26T14:59:54Z | - |
dc.date.available | 2022-04-26T14:59:54Z | - |
dc.date.issued | 2020-02 | - |
dc.citation.volume | 305 | pt_BR |
dc.citation.spage | 125463 | pt_BR |
dc.identifier.doi | https://doi.org/10.1016/j.foodchem.2019.125463 | pt_BR |
dc.identifier.issn | 0308-8146 | pt_BR |
dc.identifier.uri | http://hdl.handle.net/1843/41155 | - |
dc.description.resumo | Protein 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 | pt_BR |
dc.description.sponsorship | CNPq - Conselho Nacional de Desenvolvimento Científico e Tecnológico | pt_BR |
dc.description.sponsorship | FAPEMIG - Fundação de Amparo à Pesquisa do Estado de Minas Gerais | pt_BR |
dc.description.sponsorship | CAPES - Coordenação de Aperfeiçoamento de Pessoal de Nível Superior | pt_BR |
dc.description.sponsorship | Outra Agência | pt_BR |
dc.language | eng | pt_BR |
dc.publisher | Universidade Federal de Minas Gerais | pt_BR |
dc.publisher.country | Brasil | pt_BR |
dc.publisher.department | ICA - INSTITUTO DE CIÊNCIAS AGRÁRIAS | pt_BR |
dc.publisher.initials | UFMG | pt_BR |
dc.relation.ispartof | Food Chemistry | pt_BR |
dc.rights | Acesso Aberto | pt_BR |
dc.subject.other | Albumina | pt_BR |
dc.subject.other | Espectroscopia de fluorescência | pt_BR |
dc.subject.other | Termodinâmica | pt_BR |
dc.title | Influence of protein conformation and selected Hofmeister salts on bovine serum albumin/lutein complex formation | pt_BR |
dc.type | Artigo de Periódico | pt_BR |
dc.url.externa | https://www.sciencedirect.com/science/article/pii/S030881461931578X?via%3Dihub#! | pt_BR |
Appears in Collections: | Artigo de Periódico |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
Influence of protein conformation and selected hofmeister salts on bovine serum albuminlutein complex formation.pdf | 592.94 kB | Adobe PDF | View/Open |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.