Proteolytic enzymes of Clostridium welchii

Publisher Website
Google Scholar
Abstract
The partial purification and properties of the [lambda]-enzyme of C. welchii Type B are described. In a special medium (pancreatic digest of casein) C-welchii Type B produced high yields of [lambda]-enzyme and [epsilon]-toxin, but little or no [beta]-toxin. Purification of [lambda]-enzyme led to parallel purification of [lambda]-antigen, and the 2 are considered to be identical. [lambda]-Enzyme was purified about 40 times in terms of the non-dialyzable N in the crude filtrate from the casein medium in which it was already about 40 times as pure as in ordinary meat broth media. The enzyme prepns. attacked hide powder, gelatin, casein, hemoglobin and seracin, but had no effect on native collagen. The optimum pH was pH 6-7.5. The enzyme was destroyed at values below pH 5 or above 9 or by heating to 60[degree] for 10 min. Citrate inhibited the enzyme strongly, but there was no evidence for activation by Ca or Mg ions. The enzyme was slightly inhibited by iodoacetic acid and cyanide and strongly inhibited by cysteine. Its properties were compared with those of collagenase and the "secondary" enzyme of C. welchii Type A.