Recombinant exoinulinase was partially purified form the culture supernatant of S.cerevisiae by(NH4)2SO4 precipitation and PEG treatment. The purfied inulinase was immobilized onto Amino-cellulofine with glutaraldeyde as a cross-linking agent. Immobilization yield based on the enzyme activity was about 15%. Optimal pH and temperature of immobilized enzyme were found to be 5.0 and 6$0^{circ}C$, respectively. The enzyme activity was stably maintained in the pH ranges of 4.5 to 6.0 at 6$0^{circ}C$. 100% of enzyme activity was observed even after incubation for 24 hr at 6$0^{circ}C$. In the operation of a packed-bed reactor containing 412U inulinase, dahalia inulin of 7.5%(w/w) concentration was completely hydrolyzed at flow rate of 2.0mL/min at 6$0^{circ}C$, resulting in a volumetric productivity of 693 g-reducing sugars/L/h. Under the reaction conditions of 1.0mL/min flow rate with 2.5% inulin at 6$0^{circ}C$, the reactor was successfully operated over 30 days without loss ofinulinase activity.