221
Views
6
CrossRef citations to date
0
Altmetric
Original Articles

A Novel Glucanotransferase from a Bacillus circulans Strain That Produces a Cyclomaltopentaose Cyclized by an α-1,6-Linkage

, , , , &
Pages 1954-1960 | Received 10 Mar 2006, Accepted 11 Apr 2006, Published online: 22 May 2014

  • 1) Tabuchi, A., Mandai, T., Shibuya, T., Fukuda, S., Sugimoto, T., and Kurimoto, M., Formation of trehalose from starch by novel enzymes. J. Appl. Glycosci. (in Japanese), 42, 401–406 (1995).
  • 2) Mukai, K., Tabuchi, A., Nakada, T., Shibuya, T., Chaen, H., Fukuda, S., Kurimoto, M., and Tsujisaka, Y., Production of trehalose from starch by thermostable enzymes from Sulfolobus acidcaldarius. Starch/Stärke, 49, 26–30 (1997).
  • 3) Chaen, H., Production of trehalose by a novel enzymatic method and its applications. J. Appl. Glycosci. (in Japanese), 44, 115–120 (1997).
  • 4) French, D., The Schardinger dextrins. Advan. Carbohydr. Chem., 12, 189–260 (1957).
  • 5) Loftsson, T., and Brewster, M. E., Pharmaceutical applications of cyclodextrins. 1. Drug solubilization and stabilization. J. Pharm. Sci., 85, 1017–1025 (1996).
  • 6) Goubet, I., Dahout, C., Semon, E., Guichard, E., Le Quere, J. L., and Voilley, A., Competitive binding of aroma compounds by beta-cyclodextrin. J. Agric. Food Chem., 49, 5916–5922 (2001).
  • 7) Tran, C. D., and De Paoli Lacerda, S. H., Determination of binding constants of cyclodextrins in room-temperature ionic liquids by near-infrared spectrometry. Anal. Chem., 74, 5337–5341 (2002).
  • 8) Côté, G. L., and Biely, P., Enzymically produced cyclic α-1,3-linked and α-1,6-linked oligosaccharides of D-glucose. Eur. J. Biochem., 226, 641–648 (1994).
  • 9) Misaki, A., Torii, M., Sawai, T., and Goldstein, I. J., Structure of the dextran of Leuconostoc mesenteroides B-1355. Carbohydr. Res., 84, 273–285 (1980).
  • 10) Biely, P., Côté, G. L., and Burgess-Cassler, A., Purification and properties of alternanase, a novel endo-α-1,3-α-1,6-D-glucanase. Eur. J. Biochem., 226, 633–639 (1994).
  • 11) Nishimoto, T., Aga, H., Mukai, K., Hashimoto, T., Watanabe, H., Kubota, M., Fukuda, S., Kurimoto, M., and Tsujisaka, Y., Purification and characterization of glucosyltransferase and glucanotransferase involved in the production of cyclic tetrasaccharide in Bacillus globisporus C11. Biosci. Biotechnol. Biochem., 66, 1806–1818 (2002).
  • 12) Aga, H., Higashiyama, T., Watanabe, H., Sonoda, T., Nishimoto, T., Kubota, M., Fukuda, S., Kurimoto, M., and Tsujisaka, Y., Production of cyclic tetrasaccharide from starch using a novel enzyme system from Bacillus globisporus C11. J. Biosci. Bioeng., 94, 336–342 (2002).
  • 13) Aga, H., Nishimoto, T., Kuniyoshi, M., Maruta, K., Yamashita, H., Higashiyama, T., Nakada, T., Kubota, M., Fukuda, S., Kurimoto, M., and Tsujisaka, Y., 6-α-Glucosyltransferase and 3-α-isomaltosyltransferase from Bacillus globisporus N75. J. Biosci. Bioeng., 95, 215–224 (2003).
  • 14) Mukai, K., Watanabe, H., Oku, K., Nishimoto, T., Kubota, M., Chaen, H., Fukuda, S., and Kurimoto, M., An enzymatically produced novel cyclic tetrasaccharide, cyclo-{→6)-α-D-Glcp-(1→4)-α-D-Glcp-(1→6)-α-D-Glcp-(1→4)-α-D-Glcp-(1→} (cyclic maltosyl-(1→6)-maltose), from starch. Carbohydr. Res., 340, 1469–1474 (2005).
  • 15) Mukai, K., Watanabe, H., Kubota, M., Chaen, H., Fukuda, S., and Kurimoto, M., Purification, characterization, and gene cloning of a novel maltosyltransferase from an Arthrobacter globiformis strain that produces an alternating α-1,4- and α-1,6-cyclic tetrasaccharide from starch. Appl. Environ. Microbiol., 72, 1065–1071 (2006).
  • 16) Watanabe, H., Nishimoto, T., Sonoda, T., Kubota, M., Chaen, H., and Fukuda, S., An enzymatically produced novel cyclomaltopentaose cyclized from amylose by an α-(1→6)-linkage, cyclo-{→6)-α-D-Glcp-(1→4)-α-D-Glcp-(1→4)-α-D-Glcp-(1→4)-α-D-Glcp-(1→4)-α-D-Glcp-(1→}. Carbohydr. Res., 341, 957–963 (2006).
  • 17) Lowry, O. H., Rosebrough, N. J., Farr, A. L., and Randall, R. J. Y., Protein measurement with the Folin phenol reagent. J. Biol. Chem., 193, 265–275 (1951).
  • 18) Davis, B. J., Disk-electrophoresis. II. Method and application to human serum proteins. Ann. NY Acad. Sci., 121, 404–427 (1964).
  • 19) Laemmli, U. K., Cleavage of structural proteins during the assembly of the head of bacteriopharge T4. Nature, 227, 680–685 (1970).
  • 20) Somogyi, S., Notes on sugar determination. J. Biol. Chem., 195, 19–23 (1952).
  • 21) Nelson, N., A photometric adaptation of the Somogyi method for the determination of glucose. J. Biol. Chem., 153, 375–380 (1944).
  • 22) Chaen, H., Nishimoto, T., Yamamoto, T., Nakada, T., Fukuda, S., Sugimoto, T., Kurimoto, M., and Tsujisaka, Y., Formation of a nonreducing trisaccharide, selaginose, from trehalose by a cell-free system of Thermoanaerobium brokii. J. Appl. Glycosci., 46, 129–134 (1999).
  • 23) Henrissat, B., and Davies, G., Structural and sequence-based classification of glycoside hydrolases. Curr. Opin. Struct. Biol., 7, 637–644 (1997).
  • 24) Uitdehaag, J. C., Kalk, K. H., van der Veen, B. A., Dijkhuizen, L., and Dijkstra, B. W., The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-Å resolution. J. Biol. Chem., 274, 34868–34876 (1999).
  • 25) van der Veen, B. A., Leemhuis, H., Kralj, S., Uitdehaag, J. C., Dijkstra, B. W., and Dijkhuizen, L., Hydrophobic amino acid residues in the acceptor binding site are main determinants for reaction mechanism and specificity of cyclodextrin-glycosyltransferase. J. Biol. Chem., 276, 44557–44562 (2001).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.