The alkaline protease was isolated from the culture material of monascus sp. on wheat bran culture. The crude purification of this enzyme was extracted with distilled water and precipitated with ammonium sulfate of 0.5 saturation. And, the activity of this enzyme was determined very strongly by folin´s colorimetric method.
The optimal pH of this enzyme was ranging from pli 10 to 12 and the optimal temperature was 50℃. The pH stability was ranging from pH 5 to 12 and the enzyme activity was not inactivated by heat treatment in lower temperature than 40℃. The enzyme was protected from heat denature by the treatment of Pb^(++), Ba^(++), Co^(++), Zn^(++), and Cu^(++), but was inactivated with Hg^(++), Fe^(++) strongly. Moreover, one of these metal ions, the copper ion, has a strung protective activity on enzyme heat denature. And, it was not effected by treatment of EDTA.
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