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Campo DC | Valor | Idioma |
---|---|---|
dc.creator | Hudson, Eliara Acipreste | - |
dc.creator | Paula, Hauster Maximiler Campos de | - |
dc.creator | Ferreira, Guilherme Max Dias | - |
dc.creator | Ferreira, Gabriel Max Dias | - |
dc.creator | Hespanhol, Maria do Carmo | - |
dc.creator | Silva, Luis Henrique Mendes da | - |
dc.creator | Pires, Ana Clarissa dos S. | - |
dc.date.accessioned | 2019-04-26T10:54:54Z | - |
dc.date.available | 2019-04-26T10:54:54Z | - |
dc.date.issued | 2018-03 | - |
dc.identifier.citation | HUDSON, E. A. et al. Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding. Food Chemistry, [S.l.], v. 242, p. 505-512, Mar. 2018. | pt_BR |
dc.identifier.uri | https://www.sciencedirect.com/science/article/pii/S0308814617315674?via%3Dihub | pt_BR |
dc.identifier.uri | http://repositorio.ufla.br/jspui/handle/1/33889 | - |
dc.description.abstract | Bovine serum albumin (BSA)/curcumin binding and dye photodegradation stability were evaluated. BSA/curcumin complex showed 1:1 stoichiometry, but the thermodynamic binding parameters depended on the technique used and BSA conformation. The binding constant was of the order of 105 L·mol−1 by fluorescence and microcalorimetric, and 103 and 104 L·mol−1 by surface plasmon resonance (steady-state equilibrium and kinetic experiments, respectively). For native BSA/curcumin, fluorescence indicated an enthalpic and entropic driven process based on the standard enthalpy change (ΔH○F = −8.67 kJ·mol−1), while microcalorimetry showed an entropic driven binding process (ΔH○cal = 29.11 kJ·mol−1). For the unfolded BSA/curcumin complex, it was found thatp ΔH○F = −16.12 kJ·mol−1 and ΔH○cal = −42.63 kJ·mol−1. BSA (mainly native) increased the curcumin photodegradation stability. This work proved the importance of using different techniques to characterize the protein-ligand binding. | pt_BR |
dc.language | en_US | pt_BR |
dc.publisher | Elsevier | pt_BR |
dc.rights | restrictAccess | pt_BR |
dc.source | Food Chemistry | pt_BR |
dc.subject | Curcumin | pt_BR |
dc.subject | Intermolecular interaction | pt_BR |
dc.subject | Analytical technique | pt_BR |
dc.subject | Bovine serum albumin (BSA) | pt_BR |
dc.subject | Photodegradation | pt_BR |
dc.title | Thermodynamic and kinetic analyses of curcumin and bovine serum albumin binding | pt_BR |
dc.type | Artigo | pt_BR |
Aparece nas coleções: | DQI - Artigos publicados em periódicos |
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