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 α-1, 6- and α-1, 4-Glucosidic Linkages
复制标题
异麦芽糖葡聚糖酶单一活性位点具有 α-1, 6- 和 α-1, 4-糖苷键水解活性的证据
DOI:
10.5458/jag.48.55
复制
发表时间:
2001
影响因子:
1.1
通讯作者:
S. Chiba
中科院分区:
文献类型:
--
作者:
T. Takayanagi;A. Kimura;H. Matsui;G. Okada;S. Chiba
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.
影响因子:
4.1
作者:
A. Dahlqvist
通讯作者:
A. Dahlqvist