다공성 섬유소 업자를 제조하고, $alpha$-amylase와 glucoamylase를 각각 효과적으로 고정화 시키기 위하여 섬유소 담체를 활성화 시키고 그 최적 조건을 조사하였으며 그것의 효소학적 성질에 관하여 연구하였다. 가장 효과적 인 $alpha$-amylase와 glucoamylase의 고정화는 다공성 섬유소 담체를 0.1M p-benzoquinone으로 활성화 시킨 후 3% gallotannin으로 재활성화 시켰을 때 잔여 활성도가 가장 높았으며 이때 $CaCl_2$를 첨가함으로써 고정화율이 증가되었다. 유리의 $alpha$-amylase와 고정화 $alpha$-amylase의 반응 최적 pH는 차이가 없었으며, 반응 최적 온도는 모두 $55^{circ}C$이었다. 유리의 glucoamylase와 고정화 glucoamylase의 반응 최적 pH에도 차이가 없었으나 반응 최적 온도는 유리의 glucoamylase는 $55^{circ}C$, 고정화 glucoamylase는 $50^{circ}C$로 나타났다. Starch에 대한 $alpha$-amylase와 gucoamylase의 Km 값은 고정화시킴으로써 증가되었고 저장성 또한 증가되었다.
For the immobilization of $alpha$-amylase and glucoamylase effectively on porous cellulose beads, the optimal activation methods were studied. And their enzymatic properties were investigated. The results obtained were as follows; 1) The most effective method of enzyme immobilization was obtained when the 3% gallotannin, pH 4, was used as activation reagent after 0.1M p-benzoquinone. pH 12, activation in case of $alpha$-amylase and when the 3% gallotannin, pH 9, was used as activation reagent after 0.1M p-benzoquinone, pH 12, activation in case of glucoamylase. 2) The immobilized enzymes activities were increased by the addition of $CaCl_2$ to immobilizing mixture. The immobilized $alpha$-amylase activity was increased from 69.17u/g to 77.18u/g by addition of $5{ imes}10^{-4}M$ $CaCl_2$ to the immobilizing mixture. The immobilized glucoamylase activity was increased from 157.37u/g to 189.31u/g by addition of $5{ imes}10^{-3}M$ $CaCl_2$ to the immobilizing mixture. The maximum immobilization rate of $alpha$-amylase was 5.07% and glucoamylase was 47.33%. 3) The optimum pH of $alpha$-amylase was 4.5-5 for native enzyme and also 4. 5-5 for immobilized enzyme. The optimum pH of glucoamylase was 4.5 in both cases. 4) The optimum temperatures for the native and immobilized $alpha$-amylase were both $55^{circ}C$. The optimum temperature was $55^{circ}C$ for the native glucoamylase and $50^{circ}C$ for the immobilized glucoamylase. 5) The Km value of native $alpha$-amylase was 0.48% and that of immobilized $alpha$-amylase was 1.43% while Vmax (1.52mg hydrolyzed soluble starch/min) was unaltered. The Km value of native glucoamylase was 0.83% and that of immobilized glucoamylase was 2.0%.
