Abstract

Lipase from the hepatopancreas of Tra catfish (Pangasius) was precipitated by ammonium sulfate fractionation, purified by ion-exchange chromatography on DEAE cellulose and gel filtration on Sephadex G- 75. On substrate triolein, purified lipase has K_m= 1.381 mM and V_max= 0.063 mM/min. The lipase was stable at a pH range of 7.0- 9.0 and in temperatures of 35-50°C. At 50⁰C the enzyme loosed 44,7% activity after 120 min. The enzyme was specific for the α- positions (1, 3) of triglyceride. In bile salt solution of 0.015M NaTC, lipase activity of the enzyme increased in 3.08 folds in comparison of sample without NaTC.