초록
Commerial naringinase from Aspergillus niger was partially purified by various methods, and was immobilized to porous alkylamine silica of 30~40 mesh and 400 $\AA\pm10％$ pore diameter that had been activated with 2.5％ glutaraldehyde. About 50~70％ of initial naringinase activity was recovered after the immobilization process. Some enzymatic properties of the immobilized naringinase was investigated and compared with those of the native enzyme. The optimal temper-ature had moved from $40^{\circ}C$ to $55^{\circ}C$ and the heat stability of the immobilized enzyme was better than that of the native naringinase. But no signi-ficant diference in the pH effect on activity was detected. The activation energy of reaction, Ea, was markedly decreased from 14.9 to 8.64 (Kcal/mole) by immobilization.