大豆胰蛋白酶抑制剂对南极磷虾类胰蛋白酶的抑制动力学 [中文引用][英文引用]

To study thekinetics of inhibition of trypsin-like protease from Euphausia superba by soybean trypsin inhibitor (STI), the kinetic theory by Tsou of irreversible inactivation was applied to measure its microscopic rate constants. The values of K_m and V_max were 0.155 mmol/L and 8.44 μmol/(L·min), respectively. As the concentration of STI was increased, the activity decreased with IC­₅₀ of 2.8 μg/mL. STI slowly, reversibly and competitively inhibited the enzyme activity at low concentration. The rate constant of the forward inactivation (k₊₀) was 0.184 min^-1, which was about five times higher than the value of 0.039 4 min^-1 for the reverse reactivation (k₋₀). Therefore, at sufficiently high STI concentrations, the enzyme would be completely inactivated. This study provides experimental data for further research into the inhibition technology of the trypsin-like protease from E. superba.