Characteristics of M-Gtfi, A New Inhibitor of Streptococcus Mutans Glucosyltransferase

Abstract

M-GTFI, originally screened as an inhibitor of Streptococcus mutans glucosyltransferase, strongly inhibited α-glucosidase, in a non-competitive manner especially when the synthetic substrate p-nitrophenyl-α-D-glucopyranoside was used. It also inhibited β-glucosidase, β-amylase and, to a lesser extent, β-glu-curonidase.

The inhibitor was stable in neutral and alkaline pH ranges and dependency of the inhibition on pH and temperature was not observed. Some proteinases and polysaccharides-hydrolyzing enzymes as well as human saliva did not inactivate the inhibitor.

There was a correlation between the release of sulfate anions from the inhibitor molecule on incubation with HCI (0.2 N) at 100°c and loss of inhibitory properties of the molecule. It is suggested that the presence of sulfate ester linkages in the inhibitor molecule play an important role in the inhibition process.

Key Words: :

• Glucosyltransferase inhibitor
• enzyme inhibitor
• M-GTFI
• Streptococcus mutans
• dental caries