Reactivities of D-glucose and D-fructose during glycation of bovine serum albumin.

Glycation of bovine serum albumin by D-glucose and D-fructose under dry-heating conditions was studied. The reactivities of D-glucose and D-fructose, with respect to their ability to utilize primary amino groups of proteins, to cross-link proteins, to develop Maillard fluorescence, and to reduce protein solubility in the presence and absence of air (molecular oxygen) were investigated. D-Glucose showed a higher initial rate of utilization of primary amino groups than D-fructose, both in the presence and in the absence of oxygen. Subsequent reactions of the Amadori and Heyns rearrangement products, cross-linking, development of Maillard fluorescence, oxidation, and fragmentation, indicated that the alpha-hydroxy carbonyl group of Amadori products is more reactive than the aldehydo group of Heyns products. D-Fructose showed a greater sensitivity than D-glucose toward the presence of oxygen at the initial stages of the Maillard reaction. The presence or absence of oxygen in the glycation mixture did not seem to have an influence on the nature of products generated in the glycation mixtures during the advanced stages of the Maillard reaction.