dc.creatorNunes, Natália Moreira
dc.creatorPacheco, Ana Flávia Coelho
dc.creatorAgudelo, Álvaro Javier Patiño
dc.creatorSilva, Luis Henrique Mendes da
dc.creatorPinto, Maximiliano Soares
dc.creatorHespanhol, Maria do Carmo
dc.creatorPires, Ana Clarissa dos Santos
dc.date2018-05-17T14:12:33Z
dc.date2018-05-17T14:12:33Z
dc.date2017-05-26
dc.date.accessioned2023-09-27T22:21:47Z
dc.date.available2023-09-27T22:21:47Z
dc.identifier0308-8146
dc.identifierhttps://doi.org/10.1016/j.foodchem.2017.05.131
dc.identifierhttp://www.locus.ufv.br/handle/123456789/19643
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8974138
dc.descriptionCinnamic acid (CA) and methyl cinnamate (MC) have attracted interest of researchers because of their broad therapeutic functions. Here, we investigated the interaction of CA and MC with bovine serum albumin (BSA) at pH 3.5, 5.0, and 7.4 using fluorescence spectroscopy, differential scanning nanocalorimetry, and measurements of interfacial tension, size, and zeta potential. BSA formed a complex with the ligands with stoichiometry of approximately 1.0. At pH 7.4, CA-BSA complex formation was entropically driven. The interaction between MC and BSA was more favorable than with CA and was enthalpically driven under the same conditions. The pH played an important role in BSA conformation, which altered the manner in which it interacts with the ligands. Interestingly, both CA and MC had no effect on the surface tension of BSA/air interfaces. These data contribute to the knowledge of CA/MC-BSA interactions and provide important data for application in the food industry.
dc.formatpdf
dc.formatapplication/pdf
dc.languageeng
dc.publisherFood Chemistry
dc.relationVolume 237, Pages 525-531, December 2017
dc.rightsElsevier Ltd.
dc.subjectFluorescence spectroscopy
dc.subjectProtein conformation
dc.subjectBinding
dc.subjectComplex formation
dc.subjectCinnamic acid
dc.subjectMethyl cinnamate
dc.titleInteraction of cinnamic acid and methyl cinnamate with bovine serum albumin: A thermodynamic approach
dc.typeArtigo


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