| Title | Characterization of Bacillus cereus SH-7 Extracellular Protease |
|---|---|
| Author | Hak Kyu Yi, Young Jin Chum 1, and Han Bok Kim * |
| Address | Department of Life Science, Hoseo University, Asan-Si, ChungNam 336-795; 1 College of Pharmacy, Chung-Ang University, Seoul 156-756, Korea |
| Bibliography | Journal of Microbiology, 37(4),213-217, 1999, |
| DOI | |
| Key Words | Bacillus cereus, metalloprotease, extracellular protease |
| Abstract | An extracellular endopeptidase from Bacillus cereus SH-7 was purified to homogeneity. The protease was most active at pH 8 and 40 C, respectively. The molecular mass of the protease was 40 kDa on SDS-PAGE, and 120 kDa by gel filtration, suggesting that the native enzyme is composed of three homogeneous subunits. The K_m and V_max values of the protease for N-succinyl-(Ala)_2-Pro-Phe-p-nitroanilide were 11.11 mM and 170 nmol/mg of protein/min, respectively. The protease was also identified as a metalloprotease. The bioactivity of the SH-7 protease will need further study in the future. |
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