Lipase from Pseudomonas sp.

Research area: Cell Signaling

Lipases are part of the α/β-hydrolase fold superfamily of enzymes and are expressed in various tissues. For instance, hepatic lipases are found in the liver, lipoprotein lipase is located on the vascular endothelial surface, hormone-sensitive lipases are present in adipocytes, and pancreatic lipase is situated in the small intestine.

Isoelectric point : 5.95 -/+0.05
Inhibitors : Hg^++, Ag⁺, ionic detergents
Optimum pH : 7.0 - 9.0
Optimum temperature : 45 - 50^oC
pH Stability : pH 7.0 - 9.0 (25^oC, 20hr)
Thermal stability : below 55^oC (pH 7.0, 10min)

Lipase from Pseudomonas sp. has been used:

• for enzymatic determination of triglyceride in serum when coupled with L-α- glycerophosphate oxidase (G3O-301, G3O-311, G3O-321) and glycerol kinase (GYK-301, GYK-311).
• in a study to assess enzymatic synthesis of biodiesel from palm oil assisted by microwave irradiation.
• in determining the triglyceride content for identifying the role of gut bacteria in host health.
• to determine the effect of lipase on high-density lipoprotein 2 (HDL2) and plasma in vitro.

Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).

Lipase from Pseudomonas was shown to inhibit monocyte chemotaxis in human peripheral blood. It functions by employing chymotrypsin-like hydrolysis, involving a histidine base, a serine nucleophile, and aspartic acid. Lipases are also crucial for lipid transport. Elevated serum lipase levels are often observed in pancreatitis. Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols.

Lyophilized powder containing Mg⁺², sodium cholate, and bovine serum albumin as stabilizers

Protein determined by biuret.

One unit will produce 1.0 μmole of glycerol from a triglyceride per min at pH 7.0 at 37 °C in the presence of bovine serum albumin.