This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dols, M.
Right arrow Articles by Monsan, P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dols, M.
Right arrow Articles by Monsan, P.
Agricola
Right arrow Articles by Dols, M.
Right arrow Articles by Monsan, P.

 Previous Article  |  Next Article 

Appl Environ Microbiol, April 1998, p. 1298-1302, Vol. 64, No. 4
0099-2240/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Characterization of the Different Dextransucrase Activities Excreted in Glucose, Fructose, or Sucrose Medium by Leuconostoc mesenteroides NRRL B-1299

Marguerite Dols,* M. Remaud-Simeon, R. M. Willemot, M. Vignon, and P. Monsan

Centre de Bioingénierie Gilbert Durand, U.M.R. C.N.R.S. 5504 and Laboratoire Associeé I.N.R.A., D.G.B.A., I.N.S.A., Complexe Scientifique de Rangueil, 31 077 Toulouse Cedex 4, France

Received 30 October 1997/Accepted 5 February 1998

When grown in glucose or fructose medium in the absence of sucrose, Leuconostoc mesenteroides NRRL B-1299 produces two distinct extracellular dextransucrases named glucose glucosyltransferase (GGT) and fructose glucosyltransferase (FGT). The production level of GGT and FGT is 10 to 20 times lower than that of the extracellular dextransucrase sucrose glucosyltransferase (SGT) produced on sucrose medium (traditional culture conditions). GGT and FGT were concentrated by ultrafiltration before sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. Their molecular masses were 183 and 186 kDa, respectively, differing from the 195 kDa of SGT. The structural analysis of the dextran produced from sucrose and of the oligosaccharides synthesized by acceptor reaction in the presence of maltose showed that GGT and FGT are two different enzymes not previously described for this strain. The polymer synthesized by GGT contains 30% alpha (1right-arrow2) linkages, while FGT catalyzes the synthesis of a linear dextran only composed of alpha (1right-arrow6) linkages.

* Corresponding author. Mailing address: Centre de Bioingénierie G. Durand, D.G.B.A., I.N.S.A., Complexe Scientifique de Rangueil, 31 077 Toulouse Cedex 4, France. Phone: 33 (0) 5 61 55 94 46. Fax: 33 (0) 5 61 55 94 00. E-mail: remaud{at}insa-tlse.fr.




This article has been cited by other articles:

  • Bozonnet, S., Dols-Laffargue, M., Fabre, E., Pizzut, S., Remaud-Simeon, M., Monsan, P., Willemot, R.-M. (2002). Molecular Characterization of DSR-E, an {alpha}-1,2 Linkage-Synthesizing Dextransucrase with Two Catalytic Domains. J. Bacteriol. 184: 5753-5761 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»