Kinetic evaluation of the inhibition of protein glycation during heating


FOOD CHEMISTRY, vol.196, pp.1117-1124, 2016 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 196
  • Publication Date: 2016
  • Doi Number: 10.1016/j.foodchem.2015.10.066
  • Journal Name: FOOD CHEMISTRY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.1117-1124
  • Keywords: Protein glycation, Inhibition of glycation, Anti-glycation agents, Inhibition type, Kinetic analysis, CHLOROGENIC ACID, END-PRODUCTS, TANNIC-ACID, AMINO-ACIDS, AGES, DIGESTION, PREVENT, CASEIN, HEALTH, LYSINE
  • Hacettepe University Affiliated: Yes


This study aimed to investigate the kinetics of early stage of the Maillard reaction by a reversible bimolecular reaction mechanism and also to evaluate the compatibility of enzyme inhibition kinetics for calculating the inhibitory activity of protein anti-glycation agents. Model systems composed of ovalbumin, glucose, and anti-glycation agents (tannic acid or calcium ion) at different molar ratios were heated at 90 degrees C for different times in dry state or in solution. Heated samples were analysed for furosine, acid derivative of N-epsilon-fructoselysine (FL), to monitor the progression of the early glycation stage. Compared to a control, presence of calcium ions and tannic acid decreased FL formation significantly (p < 0.05) during heating in dry state. Evaluation of the kinetic data revealed that calcium inhibited glycation of ovalbumin by a mixed non-competitive mechanism in both dry and in solution conditions; while the mode of inhibition by tannic acid was found to be purely non-competitive in the dry state. (C) 2015 Elsevier Ltd. All rights reserved.