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dc.creatorRosa, Lívia Neves Santa-
dc.creatorRezende, Jaqueline de Paula-
dc.creatorCoelho, Yara Luiza-
dc.creatorMendes, Tiago Antônio Oliveira-
dc.creatorSilva, Luis Henrique Mendes da-
dc.creatorPires, Ana Clarissa dos Santos-
dc.date.accessioned2022-08-01T20:37:04Z-
dc.date.available2022-08-01T20:37:04Z-
dc.identifier.citationROSA, 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.urihttps://doi.org/10.1016/j.fbio.2021.101418pt_BR
dc.identifier.urihttp://repositorio.ufla.br/jspui/handle/1/50785-
dc.description.abstractCaffeine 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.languageen_USpt_BR
dc.publisherElsevierpt_BR
dc.rightsrestrictAccesspt_BR
dc.sourceFood Biosciencept_BR
dc.subjectBioactive compoundspt_BR
dc.subjectProtein thermodynamic bindingpt_BR
dc.subjectIsothermal titration calorimetrypt_BR
dc.subjectMolecular dockingpt_BR
dc.subjectCompostos bioativospt_BR
dc.subjectLigação termodinâmica de proteínaspt_BR
dc.subjectCalorimetria de titulação isotérmicapt_BR
dc.titleβ-lactoglobulin conformation influences its interaction with caffeinept_BR
dc.typeArtigopt_BR
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