An Isomalto-dextranase Accompanied by Isopullulanase Activity from Arthrobacter globiformis T6(Biological Chemistry)

概要

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An isomalto-dextranase was highly purified from the cell-free culture broth of Arthrobacter globiformis T6 by consecutive column chromatographies on CM-cellulose. The final purified enzyme was judged to be homogeneous on polyacrylamide gel, SDS-polyacrylamide gel and ampholine electrophoresis. The isopullulanase to G2-dextranase activity ratio was almost the same (ca. 0.18%) at each purification step. The isopullulanase activity appeared at exactly the same position as the G_2-dextranase activity on CM-cellulose column chromatography, analytical polyacrylamide gel electrophoresis and isoelectric focusing. The stabilities of the isopullulanase as to pH and temperature well coincided with those of the G_2-dextranase. Furthermore, the inactivation profiles of the isopullulanase with various metal ions and inhibitors were almost the same as those of the G_2-dextranase. From these results, it was strongly suggested that a single enzyme molecule was responsible for both the G_2-dextranase and isopullulanase activities.
社団法人日本農芸化学会の論文
1988-03-23