초록
토양에서 분리한 Streptomyces 속 중에 금속을 함유하고 있는 protease를 강하게 분필하는 균일 주를 선별하여 그 효소학적 성질 멸가지를 알아본 결과는 다음과 같다. 1 본 효소의 작용 최적 pH는 중성부근이며 최적온도는 37$^{\circ}C$ 부근이다. 2. 본 효소는 중성부근에서 비교적 안정하며 열에는 비교적 불안정하며 37$^{\circ}C$에서 100분간 열처리했을때 약 50% 가량 실활하였다. 3. Hg$^{＋＋}$, Cu$^{＋＋}$, Cd$^{＋＋}$, Ag$^{＋}$ 등에 의하여 강하게 조해되며, Mn$^{＋＋}$, $Mg^{＋＋}$, $Ca^{＋＋}$, Pb$^{＋＋}$, $Ba^{＋＋}$ 등에는 별 영향을 받지 않는다. 4. oxalate, citrate, 2-4-dinitrophenol, $\varepsilon$-amino caproic acid, thiourea, cysteine에 의해서는 강하게 조해되었다.
A strain of Streptomyces sp. which producing a metal containing proteolytic enzyme was isolated from soil and some properties of this enzyme were investigated. The following results were obtained. 1. Optimal pH and temperature of this enzyme were pH7.0 and 37$^{\circ}C$ 2. This enzyme was easily inactivated with heat treatment: for example, by the treatmentat 37$^{\circ}C$ for 100 minutes the activity of the enzyme was decreased to about 50 per cent of intial actively but this enzyme was stable at neutral pH. 3. The activity of this enzyme was not inhibited by $Mg^{＋＋}$, $_Mn^{＋＋}$, $Ca^{＋＋}$, Pb$^{＋＋}$, or $Ba^{＋＋}$ ect. but strongly inhibited by Hg$^{＋＋}$, Co$^{＋＋}$, Ag$^{＋}$, Cu$^{＋＋}$, or Cd$^{＋＋}$. 4. This enzyme was strongly inhibited by EDTA but was not inhibited by oxalic acid, citric acid, 2, 4-dinitrophenol, $\varepsilon$-aminocaproic acid, cysteine, or thiourea.