Oolong tea extract (OTE) was found to inhibit the water-insoluble glucan- synthesizing enzyme, glucosyltransferase I (GTase-I), of Streptococcus sobrinus 6715. The GTase-inhibitory substance in the OTE was purified by successive adsorption chromatography on Diaion HP-21 and HP-20 columns; this was followed by further purification by Sephadex LH-20 column chromatography. A major fraction that inhibited GTase activity (fraction OTF10) was obtained, and the chemical analysis of OTF10 indicated that it was a novel polymeric polyphenol compound that had a molecular weight of approximately 2,000 and differed from other tea polyphenols. Catechins and all other low-molecular- weight polyphenols except theaflavin derived from black tea did not show significant GTase-inhibitory activities. It was found that OTE and OTF10 markedly inhibit GTase-I and yeast α-glucosidase, but not salivary α- amylase. Various GTases purified from S. sobrinus and Streptococcus mutans were examined for inhibition by OTE and OTF10. It was determined that S. sobrinus GTase-I and S. mutans cell-free GTase synthesizing water-soluble glucan were most susceptible to the inhibitory action of OTF10, while S. sobrinus GTase-Sa and S. mutans cell-associated GTase were moderately inhibited; no inhibition of S. sobrinus GTase-Sb was observed. Inhibition of a specific GTase or specific GTases of mutants streptococci resulted in decreased adherence of the growing cells of these organisms. The inhibitory effect of OTF10 on cellular adherence was significantly stronger than that of OTE.
CITATION STYLE
Nakahara, K., Kawabata, S., Ono, H., Ogura, K., Tanaka, T., Ooshima, T., & Hamada, S. (1993). Inhibitory effect of oolong tea polyphenols on glucosyltransferases of mutans streptococci. Applied and Environmental Microbiology, 59(4), 968–973. https://doi.org/10.1128/aem.59.4.968-973.1993
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