Abstract
1) Experiment were conducted on the enzymatic action of the crystalline protease obtained from cultures of Ps myxogenes sp., and results obtained are as given below (2)-(4).
2) The optimum pH for liquefaction of gelatin was found to be 7.0-8.5, and the optimum temperature about 45°
3) The enzyme acted remarkably on gela-tin and hide-powder, but slightly on the other proteins, i.e., gluten, haemoglobin, casein, egg-albumin. The substrate-specificity is clearly differentiable from those of trypsin, papain and pepsin. Consequently, the enzyme may be assumed to be a collagenase.
4) From the mode of digestion of gelatin when the N-terminal residue technique was applied, it can be said that Ps enzyme is more similar to papain, than trypsin and pepsin. The author wishes to express his sincere thanks to Prof. H. Katagiri of Kyoto Univ. for his constant guidance and encouragement in the course of this work, and also to Mr. E. Masuo of this Laboratory.
