Abstract
A glucodextranase was highly purified from a cell-free culture broth of Arthrobacter globiformis 142. The glucoamylase to glucodextranase activity ratio was almost the same (ca. 0.88 %) at each purification step. The activity profiles of the stabilities of the glucoamylase to pH and temperature coincided well with those of the glucodextranase. Furthermore, the inactivation profiles of the glucoamylase with various metal ions and inhibitors were almost the same as those of the glucodextranase. From these results, it was strongly suggested that a single enzyme molecule was responsible for both the glucodextranase and glucoamylase activities.
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