녹맥아로부터 $endo-{eta}-1,3-glucanase$를 추출하여 각종 수지로써 정제하여 glucanase I과 glucanase II의 존재를 확인하였고, 정제한 두 효소의 특성에 대하여 실험한 결과, 두 정제 효소의 분자량은 각각 35,000과 28,000으로 추정되었으며 최적 pH는 5.5이었고 pH 안정 범위는 각각 달랐다. 두 정제효소의 최적 온도는 glucanase I, II 다 같이 $40^{circ}C$이었으며 glucanase I에 비해 glucanase II가 열에 다소 안정하였다. 그리고 $AgNO_3$와 $HgCl_2$와 같은 화합물은 효소활성을 저해하였다. Laminarin을 기질로 하여 측정한 Km값은 glucanase I, II 각각 1.03 mg/ml, 1.20 mg/ml이었다.
Two types of $endo-{eta}-1,3-glucanases$ were purified from green malt and their basic characteristics were studied. Molecular weights of glucanase I and glucanase II were estimated, by electrophoresis, to be 35,000 and 28,000, respectively. Purified glucanase I and II showed the highest activity at pH $5.0{sim}7.0$ and $5.0{sim}8.0$, respectively. The optimal temperature of purified glucanase I and II was $40^{circ}C$. Purified glucanase I and glucanase II were stable at $40^{circ}$ for 60 min and at $50^{circ}$ for 30 min. All enzymes were inactivited by $AgNO_3$ and $HgCl_2$ while those were not activated by various compounds tried. Km values of glucanase I and II were 1.03 mg/ml, 1.20 mg/ml, respectively.
