This study aimed to investigate the effects of hydrophobic and ionic interactions on glycation of native and high-shear treated casein during heating. Casein epicatechin and casein calcium complexes were formed and glycated with glucose at different temperatures ranging from 70 to 150 degrees C in solution and dry states. Furosine, add derivative of N-epsilon-fructoselysine (FL), and N-epsilon-carboxymethyl lysine (CML) were measured as indicators of early and advanced glycation, respectively. CML concentrations of casein epicatechin and casein calcium complexes heated in solution were significantly lower as compared to the control (p < 0.05). For instance, 182 +/- 9.78 mu g/g of CML formed in the control, while CML concentrations were 136 +/- 10.7 and 101 +/- 7.37 mu g/g in casein epicatechin and casein calcium complexes, respectively, heated at 150 degrees C in the solution state. Treatment by high shear microfluidization further decreased the CML formed during heating at 70 degrees C in dry state. The results suggest that interactions with epicatechin molecule and calcium ion could be a useful strategy to limit advanced glycation of casein under certain conditions.