Naringenin-lactoferrin binding: Impact on naringenin bitterness and thermodynamic characterization of the complex

Food Chem. 2020 Nov 30:331:127337. doi: 10.1016/j.foodchem.2020.127337. Epub 2020 Jun 18.

Abstract

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.

Keywords: Bioactive compounds; Bitterness; Bovine lactoferrin, PubChem CID: 126456119; Computer modeling; Flavonoids; ITC; Naringenin, PubChem CID: 932; Protein thermodynamic binding; Time-intensity analysis.

MeSH terms

  • Adult
  • Animals
  • Calorimetry / methods
  • Cattle
  • Entropy
  • Female
  • Flavanones / chemistry
  • Flavanones / metabolism*
  • Flavanones / pharmacology*
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Lactoferrin / chemistry*
  • Lactoferrin / metabolism*
  • Male
  • Molecular Docking Simulation
  • Molecular Dynamics Simulation
  • Taste*
  • Thermodynamics

Substances

  • Flavanones
  • Lactoferrin
  • naringenin