Degradation products of the artificial azo dye, Allura red, inhibit esterase activity of carbonic anhydrase II: A basic in vitro study on the food safety of the colorant in terms of enzyme inhibition

Food Chem. 2016 Dec 15:213:494-504. doi: 10.1016/j.foodchem.2016.06.078. Epub 2016 Jun 24.

Abstract

Allura red is a widely used food colorant, but there is debate on its potential security risk. In the present study, we found that degradation products of the dye were more potent agents with higher carbonic anhydrase inhibitory action than the parent dye. The mechanism by which the compounds inhibit the enzyme activity has been determined as competitive mode. In addition, the enzyme binding properties of the compounds were investigated employing different spectroscopic techniques and molecular docking. The analyses of fluorescence quenching data revealed the existence of the same binding site for the compounds on the enzyme molecule. The thermodynamic parameters of ligand binding were not similar, which indicates that different interactions are responsible in binding of the parent dye and degradation products to the enzyme. It appears that enzyme inhibition should be considered, more seriously, as a new opened dimension in food safety.

Keywords: Allura red; Carbonic anhydrase; Colorant; Degradation products; Enzyme inhibition; Food safety.

MeSH terms

  • Azo Compounds / pharmacology*
  • Binding Sites
  • Carbonic Anhydrase II / antagonists & inhibitors*
  • Esterases / antagonists & inhibitors*
  • Food Coloring Agents / pharmacology
  • Food Safety*
  • Humans
  • Molecular Docking Simulation*
  • Protein Binding
  • Spectrum Analysis
  • Thermodynamics

Substances

  • Azo Compounds
  • Food Coloring Agents
  • Esterases
  • Carbonic Anhydrase II