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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.

M-GTFI, an inhibitor of glucosyltransferase from S. mutans was produced by Micromonospora narashinoensis strain No. 731. The isolation procedure for M-GTFI was improved and established for spectro-scopic analyses, and some properties of the inhibitor were investigated. The structure of M-GTFI was shown to be trisodium [2-sulphonato-9-undecenyll-oxacyclotriacont-3-en-2-one, 16, 18-his sulp-honate. The chemical structure of M-GTFI was therefore similar to that of izumenolide which is a β-lactamase inhibitor containing sulfate ester groups in its molecule.The inhibitory characteristics of M-GTFI were parallel to that of other inhibitory compounds containing sulphate esters but the spectrum of activity was wider.