Abstract
Stability at neutral pH, proteolytic activity measured by various assay methods, and course of digestion of casein and gelatin were compared between crystalline proteinase of Bac. subtilis, BPN', and crystalline trypsin. The time required to decrease 0.1 per cent solution of BPN' was about 30 times longer than that of trypsin. Activity of BPN' measured by casein or hemoglobin digestion methods, gelatin liquefying method and formol titration method using casein and gelatin as substrate, was 1.9-3.3 times stronger than that of trypsin, and milk clotting activity of BPN' was about 10 times stronger than trypsin.