The kinetic comparison of purified trypsin enzyme from common kilka (Clupeonella cultriventris caspia) pyloric caeca using the amidolytic and esterolytic synthetic substrate

In present study, the kinetic parameters of purified trypsin from pyloric caeca of common kilka (C.cultriventris caspia) were measured using the amidolytic (BAPNA) and esterolytic (TAME) substrates. The results of the kinetic comparison between BAPNA and TAME substrates showed that kinetic parameters including maximum velocity (Vmax), catalytic constant (kcat) and catalytic efficiency (kcat/Km) were in TAME higher than those from BAPNA while Michaelis-Menten constant (Km) showed the lower value in TAME than that from BAPNA. The Vmax value of TAME was significantly higher than that from BAPNA (p0.05). The kcat and kcat /Km values of TAME were also significantly higher than those from BAPNA (P < 0.05). The findings reveals that purified trypsin from common Kilka pyloric caeca has a higher affinity for TAME than dose that from BAPNA and so TAME can be used as substrate for trypsin activity assessment.