Abstract
The extracellular collagenase, produced by Bacillus licheniformis F11.4, was purified by ammonium sulfate precipitation followed by DEAE Sephadex A-50. The purified collagenase showed a 26.3-fold increase in specific activity being 1.0 U/mg and 2.6% recovery. The collagenase has an apparent molecular weight of 124 and 26 kD as analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and zymography. The optimal temperature and pH were 50°C and pH 7.0, respectively. The collagenase activity was inhibited by Fe2+ (1 mM), Mg2+ (1 mM), Mn2+ (1 mM), Co2+ (1 mM), EDTA (1 mM), and β-mercaptoetanol (1 mM). However, Ca2+ (1 mM) and Cu2+ (1 mM) increased its activity. The collagenase from B. licheniformis F11.4 was capable of hydrolyzing other protein substrates such as casein, gelatin, and fibrin. The Km and Vmax of the enzyme for collagen were 0.26 mg/ml and 0.27 U, respectively. Key words: Collagenase, Bacillus licheniformis F11.4, purification, characterization.
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