[Enzymatic activity of chymopsin of various origin]

A number of enzymatic properties of fish pylochymopsin and bull chymopsin have been studied. Hydrolysis of synthetic ethers of N-benzoyl-L-tyrosine and N-benzoyl-L-arginine by these chymopsins depending at the time and concentration of preparations has been studied. It was found that bull chymopsin is the most active one. It was shown that concentrations of 2 to 6 micrograms/ml of bull chymopsin and of 15 to 20 micrograms/ml of fish enzyme were optimal for synthetic substrate BTME hydrolysis. The significant trypsin activity was revealed in the both preparations on a number of synthetic amides. In contrast to the bull chymopsin the treatment of fish pylochymopsin by TPCK did not completely remove the chymotryptic activity of pylochymopsin. It was shown that tryptic activity in the both preparations was completely removed with TLCK. The time and concentration dependence of the autolysis in both chymopsins has been studied. It should be noted that this process is negligible for fish pylochymopsin in contrast to bull chymopsin. Stabilization of both proteases in aqueous solution at room temperature has been studied. Stabilization of the chymopsins in solution is achieved by the addition of various protein preparations including casein and serum albumin. The degree of stabilization by these proteins was achieved at 2% concentration.