Partial purification and properties of extracellular proteolytic activity ofBacteroides nodosus

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Abstract
Extracellular proteolytic activity from broth cultures of a virulent strain of B. nodosus, the chief causative agent of foot rot in sheep, was purified about 3000-fold. The activity of the preparation was maximal between pH 8.8 and 10.0 was inhibited EDTA and was unaffected by trypsin and chymotrypsin inhibitors. Few proteins were hydrolyzed by the preparation. No esterase, di- or tripeptidase activity was detected. The preparation partially solubilized powdered ovine hoof that was modified by dry-grinding, but no action on native or denatured wool keratin could be demonstrated.

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