Evidence for a Single Active Site on Isomalto-dextranase with Hydrolysis Activities of .ALPHA.-1,6- and .ALPHA.-1,4-Glucosidic Linkages.

• Takayanagi Tsutomu

  Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University

• Kimura Atsuo

  Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University

• Matsui Hirokazu

  Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University

• Okada Gentaro

  Department of Biology, Faculty of Education, Shizuoka University

• Chiba Seiya

  Division of Applied Bioscience, Graduate School of Agriculture, Hokkaido University

Bibliographic Information

Other Title

• α-1,6およびα-1,4-グルコシド結合に加水分解活性を有するイソマルトデキストラナーゼの活性部位の検討
• Evidence for a Single Active Site on Isomalto-dextranase with Hydrolysis Activities of α-1,6- and α-1,4-Glucosidic Linkages
• Evidence for a Single Active Site on Isomalto dextranase with Hydrolysis Activities of アルファ 1 6 and アルファ 1 4 Glucosidic Linkages

Abstract

An isomalto-dextranase from Arthrobacter globiformis T6 was kinetically elucidated to be capa ble of splitting α-1, 4-glucosidic linkage of panose as well as α-1, 6-glucosidic linkage of isomalt otriose. The kinetic features of the experiments with the mixed substrates of isomaltotriose and panose, the linearity of Lineweaver-Burk plots, the dependence of the apparent maximal velocities on the mole fraction (f) of isomaltotriose in the mixed substrates, f = [isomaltotriose]/([isomaltotriose]+ [panose]) were in good agreement with those expected for a single catalytic site mecha nism. The enzyme is accompanied by isopullulanase activity, by which pullulan is endolytically hy drolyzed to release isopanose mainly. The isomalto-dextranase expressed by the recombinant E. coli cells also produced isopanose from pullulan. It was for the first time confirmed genetically that the enzyme had inherently isopullulanase activity.

Journal

• Journal of Applied Glycoscience

  Journal of Applied Glycoscience 48 (1), 55-61, 2001

  The Japanese Society of Applied Glycoscience

Details

• CRID: 1390001206292219904
• NII Article ID: 10008252385
• NII Book ID: AN10453916
• ISSN: 13403494
• ISSN: 18807291
• ISSN: 13447882
• DOI: 10.5458/jag.48.55
• NDL BIB ID: 5648269
• Web Site: https://agriknowledge.affrc.go.jp/RN/2030621840
• Web Site: https://ndlsearch.ndl.go.jp/books/R000000004-I5648269
• Web Site: http://www.jstage.jst.go.jp/article/jag1999/48/1/48_1_55/_pdf
• Text Lang: en
• Data Source:
  • JaLC
  • IRDB
  • NDL
  • Crossref
  • CiNii Articles
• Abstract License Flag: Disallowed