Transglucosylation and Hydrolysis Activity of Gluconobacter oxydans Dextran Dextrinase with Several Donor and Acceptor Substrates

  • Myriam Naessens
  • Erick J. Vandamme


In this paper the reactivity of Gluconobacter oxydans dextran dextrinase (DDase) towards several glucosyl donor and acceptor molecules was studied. The donor/acceptor assay reflecting most accurately the DDase transglucosylation activity, could then be used as an evaluation tool for the optimization of the DDase production by G. oxydans. Different combinations of glucosyl donors (maltodextrin or maltose) and glucosyl acceptors (glucose, maltose or cellobiose) were incubated with a crude G. oxydans cell extract as a biocatalyst. The synthesis of panose revealed to be the most reliable indicator for DDase transglucosylation activity. Measurements of increasing glucose concentrations or decreasing maltose concentrations were less suitable for the quantification of DDase activity, since maltose seemed to be subjected to some hydrolysis during the enzymatic assays. In order to determine whether the hydrolytic activity, revealed in the donor/acceptor assays, originated from the DDase enzyme itself or from another enzyme present in the DDase preparation, the G. oxydans cell extract was subjected to native PAGE and zymogram analysis. The cell extract contained a number of proteins, the majority being smaller than 140 kDa. One protein band could be detected between the MW markers of catalase and ferritin (with a MW of 232 kDa and 440 kDa resp.), corresponding to DDase, which has a MW of 300 kDa, according to Yamamoto et al 1. The zymogram showed an uncoloured zone with the same Rf value as DDase, leading to the conclusion that DDase itself was most probably the enzyme displaying the hydrolytic activity observed in the donor/acceptor assays.


Native Page Acceptor Substrate Zymogram Analysis Increase Glucose Concentration Glucosyl Unit 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Yamamoto, K., Yoshikawa, K., Kitahata, S., Okada, S. , 1992, Purification and some properties of dextrin dextranase from Acetobacter capsulatus ATCC 11894. Bioscience, Biotechnology and Biochemistry, 56: 169–173CrossRefGoogle Scholar
  2. 2.
    Shimwell, J.L., 1947, A study of ropiness in beer. Journal of the Institute of Brewing, 53: 280–294Google Scholar
  3. 3.
    Hehre, H., Hamilton, D.M., 1949, Bacterial conversion of dextrin into a polysaccharide with the serological properties of dextran. Proceedings of the Society for Experimental Biology and Medicine, 71: 336–339Google Scholar
  4. 4.
    Yamamoto, K., Yoshikawa, K., Okada, S., 1993, Detailed action mechanism of dextrin dextranase from Acetobacter capsulatus ATCC 11894. Bioscience, Biotechnology and Biochemistry, 57: 47–50CrossRefGoogle Scholar
  5. 5.
    Lobov, S.V., Ohtani, R.K.K., Tanaka, O., Yamasaki, K., 1991, Enzymic production of sweet stevioside derivatives: Transglucosylation by glucosidases. Agricultural and Biological Chemistry, 55: 2959–2965CrossRefGoogle Scholar
  6. 6.
    Japanese patent: Preparation of food additives palatinose derivatives with sugars. JP 92–123945 920515Google Scholar
  7. 7.
    Japanese patent: Food product based on soybean glycosides. JP 83–64183 830411Google Scholar
  8. 8.
    Yamamoto, K., Yoshikawa, K., Okada, S., 1994, Substrate specificity of dextrin dextranase from Acetobacter capsulatus ATCC 11894. Bioscience, Biotechnology and Biochemistry, 58: 330–333CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2001

Authors and Affiliations

  • Myriam Naessens
    • 1
  • Erick J. Vandamme
    • 1
  1. 1.Department of Biochemical and Microbial Technology, Faculty of Agricultural and Applied Biological SciencesUniversity of GentGentBelgium

Personalised recommendations