Glucoamylase (EC 3.2.1.3) from Endomyces sp. IFO 0111 was bound with CM-cellulose at pH 4. The amylase activity in the bound form was found to be less than 2.5% of that in soluble state, and the bound enzyme was more labile to heat- and urea-treatment. However, the bound enzyme could be quantitatively liberated into solution at pH 6. Thus, the enzyme which had acted in solution at pH 6 could be recovered simply bylowering the pH and repeatedly used for another action at pH 6. When the glucoamylase was adsorbed on hydroxyapatite, it showed 10% of the amylase activity and 45% of the maltase activity, as compared with the corresponding amount of the enzyme in solution. K_m and V_max values of both states of the enzyme were determined for soluble starch and maltose. The enzyme increased its heat-stability upon being adsorbed on hydroxyapatite. Both types of the bound enzyme could be dried to stable powders in the presence of a high concentration of sugar.