Lipase PLfrom Alcaligenes sp.
Triacylglycerol lipase EC 3.1.1.3
| Lipase PL from Alcaligenes sp. Triacylglycerol lipase EC 3.1.1.3 |
| Lipase PL is active and stable in various organic solvents and suitable for synthesis of esters and transesterification. The activity of Lipase PL is remarkably stimulated in the presence of bile salts like pancreatic lipases. |
| Appearance | Beige powder | |
| Activity | ca. 100,000 U/g powder | |
| Molecular weight | 30,000 (SDS-PAGE) | |
| Isoelectric point | 4.5 | |
| Optimum pH | 8 - 9.5 | |
| pH stability | 7 - 10 | |
| Optimum temperature | 50 ºC | |
| Thermal stability | Below 40 ºC | |
| Inhibitors | Cationic detergents | |
| Specificities | Positional specificity | preferentially hydrolyzing the sn-1 and sn-3 positions of triacylglycerols. |
| Activity on esters | ca. 75 U/g (p-Nitrophenyl acetate as a substrate) | |
| Storage | Desiccate and store below 25 ºC | |
| Lipase PLC, PLG |
| Lipase PLC and PLG are immobilized enzymes designed for various reactions in organic solvents or with no solvents. Lipase PLC is produced by immobilizing Lipase PL on diatomaceous earth, while Lipase PLG is prepared by immobilizing the same enzyme on granulated diatomaceous earth. Lipase PLC and PLG are applicable to synthesis of optically active substances in organic solvents and transesterification of fats and oils with no solvents. |
| Activity | ca. 100,000 U/g *1 |
| Loss on drying | 1 % or less |
| Storage | Desiccate and store below 25 ºC |
| *1 : Activity of immobilized lipases is expressed as the hydrolytic activity adsorbed on the support materials. |