흰느타리버섯(Pleurotus cormkopiae(pers.) Rolland)중의 protease를 DEAE-sephadex A-50, CM-cellulose, DEAE-cellulose 및 Sephadex G-75를 사용하여 분리정제하고 그 성질을 조사하였다. 이 버섯중에는 bovine serum albumin을 기질로 하였을 때 2종류의 활성분획을 함유하고 있었고, protease(분획 I)의 최적 pH는 4.0, 최적온도는 $50^{circ}C$, pH 안정도는 pH 3.0~4.0 그리고 열안정도는 $40^{circ}C$ 이하에서 안정하였다. 또한$Ca^{++}$, $Cu^{++}$, $Zn^{++}$, $Fe^{++}$ 및 $Mg^{++}$ 이온은 이 효소의 활성도를 저해하였으나, $Co^{++}$ 이온은 효소의 활성을 증가시켰다. 이 효소의 subunit는 1개 였고, 걷보기 분자량은 56,000 daltons이었으며 아미노산 조성은 17종이었다.
The enzyme properties of protease of the Pleurotus Cornucopiae (Pers.) Rolland were investigated by purification with gel filteration using DEAE-sephadex A-50, CM-cellulose, DEAE-cellulose and Sephadex G-75. Two kinds of active fractions were isolated from this mushroom study. The active fraction showed protease activity for the bovine serum albumin substrate, and its optimum pH, optimum temperature, pH stability and thermal stability were 4.0, $50^{circ}C$, 3.0~4.0 and $20{sim}40^{circ}C$, respectively. The activity of the enzyme was inhibited by $Ca^{++}$, $Cu^{++}$, $Zn^{++}$, $Fe^{++}$ and $Mg^{++}$, but increased with $Co^{++}$. The enzyme had one subunits composed of 17 amino acids. The apparent molecular weight was about 56,000 daltons.
