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

Streptomyces 속균(屬菌)이 생성하는 Metal Protease - 제 1 보 : 균(菌)의 분리(分離) 및 효소학적(酵素學的) 성질(成質) -

  • Yi, Dong-Heui (Department of Agricultural Chemistry, Kyungpook National University) ;
  • Yu, Choon-Bal (Department of Food Technology, Junior College, Korea Social Work College)
  • 이동희 (경북대학교 농과대학, 농화학과) ;
  • 유춘발 (한국 사회 사업 대학, 병설 실업 전문 대학, 식품 공업과)
  • Published : 1980.03.30


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 $45^{\circ}C$, respectively. The stable pH range of the enzyme was between pH 6.0 to 8.0. The enzyme was stable at $45^{\circ}C$, but it lost the activity about 75 % for 5 min and completely for 30 min when it was treated at $60^{\circ}C$. The activity of the enzyme was inhibited by $Hg^{++},\;Cu^{++},\;Ag^{+}$ and activated by $Mg^{++},\;Mn^{++},\;Co^{++},\;but\;Fe^{++},\;Ca^{++},\;Pb^{++}\;and\;Al^{3+}$ did not affect enzyme activity. This enzyme was strongly inhibited by EDTA, but was not inhibited by 2, 4-DNP, ${\rho}$-CMB, ${\varepsilon}$-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.