Penicillium 속 균주가 분비하는 알칼리성 Protease에 관한 연구

국문 초록 (Abstract)

알칼리성 protease 강력 분비 균주로써 Penicillium 속 1균주를 분리 선별하여 그 정체 및 기본적 성질을 검토한 결과 이 효소는 Sephadex-G 200에 의해서 비교적 순수하게 정제가능하며 최적 pH는 8.0~11.0 최적온도는 $50^{\circ}C$이었다. 또 pH 6.0~12.0에서 비교적 안정하였으며 $50^{\circ}C$에서 60분 이상 경과하였을때 약 10%정도의 실활을 나타내었다. 효소활성이 $Cu^{+2}$, $Hg^{+2}$에 의해서 저해되며 $Pb^{+2}$는 다소 보호작용을 나타내나 $Li^{+2}$, $Ca^{+2}$, $Ni^{+2}$, $Mg^{+2}$, $Zn^{+2}$, $Co^{+2}$, $Mn^{+2}$, $Ba^{+2}$, $Fe^{+2}$등의 금속이온은 아무런 영향을 미치지 않았다. 또 EDTA-2Na가 아무런 영향을 미치지 않음을 볼 때 이 효소는 비금속 효소이며 그 Km 치는 casein에 작용했을때 0.147%이었다.

다국어 초록 (Multilingual Abstract)

This alkaline protease was isolated from the culture of Penicillium sp. on the wheat bran culture. The crude form of this enzyme was extracted with distilled water and precipitated with ammonium sulfate saturation. This crude enzyme was easily separated from other ninhydrine-positive materials by Sephadex column chromatography. The activity of this alkaline enzyme was determined by Folin's colorimetric method. The optimal pH of this enzyme ranged from 8 to 11 and the optimal temperature was $50^{\circ}C$. The pH stability ranged from pH 6 to 12 and the enzyme was not inactivated by heat treatment at lower temperatures than $40^{\circ}C$. The enzyme was protected from heat denaturation by the treatment of $Pb^{++}$, but was inactivated with $Cu^{++}$, $Mg^{++}$ and it was not affected by treatment of EDTA. And the Km value of the enzyme was 0.083% on casein.