Metal Protease from Streptomyces spp. - I. Isolation of the Strain and the Enzymatic Properties -

A Streptomyces spp. strain SY 79-1 which was capable of producing metal protease was isolated from soil. The optimal pH and temperature of the protease were around pH 8.0 and , respectively. The stable pH range of the enzyme was between pH 6.0 to 8.0. The enzyme was stable at , but it lost the activity about 75 % for 5 min and completely for 30 min when it was treated at . The activity of the enzyme was inhibited by and activated by did not affect enzyme activity. This enzyme was strongly inhibited by EDTA, but was not inhibited by 2, 4-DNP, -CMB, -aminocaproic acid, cysteine, thiourea, citric acid, oxalic acid and sodium arsenate. When cobalt was added to the EDTA-denatured enzyme, the activity of the enzyme was restored.