Portal de Periódicos da CAPES

Artigo Acesso aberto Produção Nacional Revisado por pares

BIBTEX RIS

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

2020; Elsevier BV; Volume: 331; Linguagem: Inglês

10.1016/j.foodchem.2020.127337

1873-7072

Natália Moreira Nunes, Yara Luíza Coelho, José Severiche Castro, Márcia Cristina Teixeira Ribeiro Vidigal, Tiago Antônio de Oliveira Mendes, Luís Henrique Mendes da Silva, Ana Clarissa dos Santos Pires,

Lipid Membrane Structure and Behavior

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.