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

DOI 日本農学文献記事索引 Web Site Web Site 被引用文献4件 参考文献24件

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

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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.

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