Volume :
2
Issue :
2
Abstract :
The aim of the present study was isolation and characterization of Iranian yellow scorpion Odontobuthus doriae. Scorpion venoms are considered as a rich source of enzymes. Some types of enzymes such as phospholipase A2, proteolytic enzymes and phosphodiesterase are definitely characterized. However, few studies have been done about lipase. In this article, we study the isolation and purification of lipase from Odontobuthus doriae scorpion, belongs to Buthidae family. It can cause dangerous envenoming. A combination of gel filtration on Sephadex G-75, ion exchange chromatography on DEAE-cellulose and Colorimetric Lipase Assay were used respectively. The optimal pH and temperature for maximum activity of isolated lipase were 9 and 37Ä‹, respectively. The km of enzyme was 17 mM at 37Ä‹ and its specific activity was 42.6 U/mg against 10 U/mg/min for the total desiccated venom. The enzyme was meaningfully stable at high pH values, and maintained about 65% of its activity after 4h incubation at pH 11. Lipase enzyme was inactivated after 5min at a temperature higher than 55Ä‹. The sodium dodecyl sulfate-polyacrilamide gel electrophoresis and then Sephadex G-75 techniques showed that enzyme had estimate molecular weight of 50 KDa.