Glucoamylase Immobilization on Bacterial Cellulose Using Periodate Oxidation Method

Abstract

Glucoamylase immobilized to bacterial cellulose beads, which were activated by the periodate oxidation method, was discussed. The immobilized glucoamylase activity increased by about 40% more than the value in previous research. The maximum immobilized activity of 133.3 U/g-BC was achieved when the loading glucoamylase concentration was 1.0%. The results of pH and thermal stability analyses indicated that the activity of immobilized glucoamylase was significantly influenced by the environment. Furthermore, about 46% of the activity remained after 14 repeated usages.