title: Kinetic evaluation of the inhibition of protein glycation during heating.
abstract: 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 °C for different times in dry state or in solution. Heated samples were analysed for furosine, acid derivative of N-ε-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.
authors.affiliation: Department of Food Engineering, Hacettepe University, Beytepe Campus, 06800 Ankara, Turkey.
authors.forename: H Gül
authors.initials: HG
authors.lastname: Akıllıoğlu
authors.affiliation: Department of Food Engineering, Hacettepe University, Beytepe Campus, 06800 Ankara, Turkey. Electronic address: vgokmen@hacettepe.edu.tr.
authors.forename: Vural
authors.initials: V
authors.lastname: Gökmen
mesh_terms: D006031:Glycosylation; D006361:Heating / Q000379:methods*; D007700:Kinetics; D011506:Proteins / Q000378:metabolism*
chemical_list: D011506:Proteins
keywords: Anti-glycation agents; Inhibition of glycation; Inhibition type; Kinetic analysis; Protein glycation