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Naringenin (NG) is a flavonoid with many bioactive properties, however, its bitterness limits its use in foods. It is known that complex formation with proteins can mask this undesirable sensory property. Therefore, a trained panel evaluated the effect of bovine lactoferrin (LF) on NG bitterness using time-intensity analysis. LF reduced the maximum bitterness intensity and overall bitterness perception for NG by 27% and 33%, respectively. Isothermal titration nanocalorimetry (ITC), molecular docking (DC), and molecular dynamics (MD) were used to characterize NG-LF binding. These techniques provided similar values of ΔG ° for binding ( [Formula: see text]  = -33.42 kJ mol -1 ; [Formula: see text]  = -32.22 kJ mol -1 ; [Formula: see text]  = -31.84 kJ mol -1 ). ITC showed that the complex formation is primarily entropy driven and DC suggested that NG binds at a hydrophobic site in LF. Here are presented strategic tools for promoting NG incorporation in food and health products., Competing Interests: Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2020 Elsevier Ltd. All rights reserved.)

Lactoferrin (LF) is a glycoprotein that serves as a potential vehicle for small bioactive molecules in food. In an effort to improve this functionality, the kinetic and thermodynamic interaction of LF with naringin (NR) was studied by surface plasmon resonance (SPR). The results demonstrated that the association rate constant between LF and NR was 5.00 × 10 4  M -1  s -1 , while the dissociation rate of the complex was 0.36 s -1 , at 25 °C. The stable complex predominated over free molecules (ΔG 25°C 0 =-29.35 kJ mol -1 ), and the binding constant was 1.39 × 10 5  M -1 , at 25 °C. The association of LF and NR to form an intermediate complex occurred in multi-steps. Nevertheless, the intermediate complex formation from the dissociation of the stable complex occurred in a single step with the activation energy independent of temperature. This study provides an important basis to explore LF as a vehicle for bioactive molecules., (Copyright © 2019 Elsevier Ltd. All rights reserved.)

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., (Copyright © 2017 Elsevier Ltd. All rights reserved.)