Catalytic elevation effect of methylglyoxal on invertase and characterization of MGO modification products.

Reactive carbonyl species can modify digestive enzymes upon intake due to their electrophilic nature. This study evaluated the effects of methylglyoxal (MGO), glyoxal, acrolein, and formaldehyde on invertase, an enzyme presents in digestive tract. Unexpectedly, MGO enhanced, rather than inhibited, invertase activity. Moreover, MGO counteracted the inhibitory effects of the other three carbonyls on invertase activity. Kinetic analyses revealed that 150 mmolLexp.-1 MGO resulted in a 2-fold increase in the Km and a 3.3-fold increase in Vmax, indicating that MGO increased the turnover rate of sucrose while reducing the substrate binding affinity of invertase. Additionally, MGO induced dynamic quenching of fluorescence, reduced free amino groups, increased hydrophobicity, the content of Amadori products, fluorescent and nonfluorescent AGEs, and amyloid fibrils of invertase. The specific modifications responsible for the elevated activity of MGO on invertase require further investigation.