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Campo DC | Valor | Idioma |
---|---|---|
dc.creator | Rosa, Lívia Neves Santa | - |
dc.creator | Rezende, Jaqueline de Paula | - |
dc.creator | Coelho, Yara Luiza | - |
dc.creator | Mendes, Tiago Antônio Oliveira | - |
dc.creator | Silva, Luis Henrique Mendes da | - |
dc.creator | Pires, Ana Clarissa dos Santos | - |
dc.date.accessioned | 2022-08-01T20:37:04Z | - |
dc.date.available | 2022-08-01T20:37:04Z | - |
dc.identifier.citation | ROSA, L. N. S. et al. β-lactoglobulin conformation influences its interaction with caffeine. Food Bioscience, [S. l.], v. 44, 101418, Dec. 2021. Part A. DOI: 10.1016/j.fbio.2021.101418. | pt_BR |
dc.identifier.uri | https://doi.org/10.1016/j.fbio.2021.101418 | pt_BR |
dc.identifier.uri | http://repositorio.ufla.br/jspui/handle/1/50785 | - |
dc.description.abstract | Caffeine is a molecule with bioactive properties related to increased mental performance. Its use in food products is limited by its bitterness and self-association behavior. The complex formed by β-lactoglobulin and caffeine was characterized by fluorescence spectroscopy, isothermal titration calorimetry, and molecular docking. Fluorescence spectroscopy revealed that β-lactoglobulin interacted with caffeine to form a 1:1 stoichiometric complex. Isothermal titration calorimetry characterization of β-lactoglobulin-caffeine binding revealed a different stoichiometry (1:3). Molecular docking analysis confirmed the information obtained by the two thermodynamic evaluation techniques, showing that the best interaction occurred in the hydrophobic cavity of β-lactoglobulin. The effect of protein conformation was also evaluated by fluorescence spectroscopy. The complex stoichiometry and binding constants were from the same order as those obtained for native β-lactoglobulin. However, in contrast to the complex formation with native protein, the flexibility increase observed in the thermal unfolded protein promoted a great temperature effect on the standard enthalpy and entropy changes of interaction, indicating the presence of a balance between hydrophobic and hydrophilic forces. | pt_BR |
dc.language | en_US | pt_BR |
dc.publisher | Elsevier | pt_BR |
dc.rights | restrictAccess | pt_BR |
dc.source | Food Bioscience | pt_BR |
dc.subject | Bioactive compounds | pt_BR |
dc.subject | Protein thermodynamic binding | pt_BR |
dc.subject | Isothermal titration calorimetry | pt_BR |
dc.subject | Molecular docking | pt_BR |
dc.subject | Compostos bioativos | pt_BR |
dc.subject | Ligação termodinâmica de proteínas | pt_BR |
dc.subject | Calorimetria de titulação isotérmica | pt_BR |
dc.title | β-lactoglobulin conformation influences its interaction with caffeine | pt_BR |
dc.type | Artigo | pt_BR |
Aparece nas coleções: | DCA - Artigos publicados em periódicos |
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