Abstract
Crude enzyme solution was prepared from the supernate of cultured S. schenckii by filtration and partially purified with DEAE-cellulose column chromatography. The enzyme fraction which degraded azocoll (insoluble denatured collagen) was pooled and characterized. Optimum pH of hydrolytic activity of azocoll was found to be 4.0 and the activity was inhibited by pepstatin. The enzyme also showed degrading activity of native acid soluble calf skin collagen on SDS polyacrylamide gel electrophoresis.
From these studies, it was confirmed that S. schenckii produced collagenolytic proteinase. This suggests that the collagenolytic proteinase may play an important role in the pathogenesis of S. schenckii.
