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. 1987 Mar;55(3):698–703. doi: 10.1128/iai.55.3.698-703.1987

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

S Hojo, M Mitsutomi, T Yamada
PMCID: PMC260396  PMID: 3818092

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. DAVIS B. J. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS. Ann N Y Acad Sci. 1964 Dec 28;121:404–427. doi: 10.1111/j.1749-6632.1964.tb14213.x. [DOI] [PubMed] [Google Scholar]
  2. DISCHE Z., DEVI A. A new colorimetric method for the determination of ketohexoses in presence of aldoses, ketoheptoses and ketopentoses. Biochim Biophys Acta. 1960 Mar 25;39:140–144. doi: 10.1016/0006-3002(60)90129-3. [DOI] [PubMed] [Google Scholar]
  3. Ebert K. H., Schenk G. Mechanisms of biopolymer growth: the formation of dextran and levan. Adv Enzymol Relat Areas Mol Biol. 1968;30:179–221. doi: 10.1002/9780470122754.ch4. [DOI] [PubMed] [Google Scholar]
  4. Garszczynski S. M., Edwards J. R. Synthesis of a broth levan by a cell-bound levansucrase from Streptococcus salivarius (SS2). Arch Oral Biol. 1973 Feb;18(2):239–251. doi: 10.1016/0003-9969(73)90144-1. [DOI] [PubMed] [Google Scholar]
  5. Ikeda T., Shiota T., McGhee J. R., Otake S., Michalek S. M., Ochiai K., Hirasawa M., Sugimoto K. Virulence of Streptococcus mutans: comparison of the effects of a coupling sugar and sucrose on certain metabolic activities and cariogenicity. Infect Immun. 1978 Feb;19(2):477–480. doi: 10.1128/iai.19.2.477-480.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Walker G. J., Hare M. D., Morrey-Jones J. G. Activity of fructanase in batch cultures of oral streptococci. Carbohydr Res. 1983 Feb 16;113(1):101–112. doi: 10.1016/0008-6215(83)88222-6. [DOI] [PubMed] [Google Scholar]
  8. Weber K., Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J Biol Chem. 1969 Aug 25;244(16):4406–4412. [PubMed] [Google Scholar]
  9. Whitaker E. J., Edwards J. R. Purification and properties of a cell-associated levan-sucrase from Streptococcus salivarius SS2. Arch Oral Biol. 1976;21(10):565–570. doi: 10.1016/0003-9969(76)90025-x. [DOI] [PubMed] [Google Scholar]
  10. Yamada T., Carlsson J. Regulation of lactate dehydrogenase and change of fermentation products in streptococci. J Bacteriol. 1975 Oct;124(1):55–61. doi: 10.1128/jb.124.1.55-61.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Yamada T., Takahashi-Abbe S., Abbe K. Effects of oxygen on pyruvate formate-lyase in situ and sugar metabolism of Streptococcus mutans and Streptococcus sanguis. Infect Immun. 1985 Jan;47(1):129–134. doi: 10.1128/iai.47.1.129-134.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Zacharius R. M., Zell T. E., Morrison J. H., Woodlock J. J. Glycoprotein staining following electrophoresis on acrylamide gels. Anal Biochem. 1969 Jul;30(1):148–152. doi: 10.1016/0003-2697(69)90383-2. [DOI] [PubMed] [Google Scholar]

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