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BIBTEX RIS

Interaction of cinnamic acid and methyl cinnamate with bovine serum albumin: A thermodynamic approach

2017; Elsevier BV; Volume: 237; Linguagem: Inglês

10.1016/j.foodchem.2017.05.131

1873-7072

Natália Moreira Nunes, Ana Flávia Coelho Pacheco, Álvaro Javier Patiño‐Agudelo, Luís Henrique Mendes da Silva, Maximiliano Soares Pinto, Maria do Carmo Hespanhol da Silva, Ana Clarissa dos Santos Pires,

Photochemistry and Electron Transfer Studies

Cinnamic 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.