Metabolism of glycosylsucrose by oral microorganisms and its hydrolysis by Streptococcus salivarius fructosyltransferase.

S Hojo, M Mitsutomi, T Yamada

Index: Infect. Immun. 55(3) , 698-703, (1987)

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Abstract

Resting-cell suspensions of oral microorganisms grown in sucrose were studied for the production of acid from glucosylsucrose and maltosylsucrose. Most oral microorganisms fermented these sugars to only a limited extent. Streptococcus salivarius, however, metabolized glucosylsucrose as well as sucrose. We therefore looked for a specific enzyme in S. salivarius which was capable of hydrolyzing glucosylsucrose. Fructosyltransferase and invertase were purified from S. salivarius 13419, and the substrate specificities and hydrolytic activities of these enzymes were determined. Purified fructosyltransferase catalyzed fructan synthesis from glucosylsucrose or maltosylsucrose, whereas purified invertase barely hydrolyzed these sugars. These results suggest that the high fermentative efficiency of glycosylsucrose by S. salivarius is due to the hydrolysis of these sugars by fructosyltransferase, but not by invertase. The partially purified fructosyltransferases of Actinomyces viscosus NY1 and Streptococcus mutans NCIB 11723 catalyzed fructan synthesis from glucosylsucrose or maltosylsucrose. The fructosyltransferases of these oral microorganisms are also responsible for the hydrolysis of glycosylsucrose.