L9518
Lipase from Pseudomonas sp.
Type XIII, lyophilized powder, ≥15 units/mg solid
Synonym(s):
Extracellular lipase, Triacylglycerol ester hydrolase, lip, Triacylglycerol acylhydrolase, Triacylglycerol lipase
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About This Item
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type
Type XIII
form
lyophilized powder
specific activity
≥15 units/mg solid
mol wt
~134 kDa
composition
Protein, 40-65% biuret
storage temp.
2-8°C
General description
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.
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.
Application
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.
Biochem/physiol Actions
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.
Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate).
Physical properties
Isoelectric point : 5.95 -/+0.05
Inhibitors : Hg++, Ag+, ionic detergents
Optimum pH : 7.0 - 9.0
Optimum temperature : 45 - 50oC
pH Stability : pH 7.0 - 9.0 (25oC, 20hr)
Thermal stability : below 55oC (pH 7.0, 10min)
Inhibitors : Hg++, Ag+, ionic detergents
Optimum pH : 7.0 - 9.0
Optimum temperature : 45 - 50oC
pH Stability : pH 7.0 - 9.0 (25oC, 20hr)
Thermal stability : below 55oC (pH 7.0, 10min)
Unit Definition
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.
Physical form
Lyophilized powder containing Mg+2, sodium cholate, and bovine serum albumin as stabilizers
Analysis Note
Protein determined by biuret.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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K E Jaeger et al.
Microbial pathogenesis, 10(3), 173-182 (1991-03-01)
Lipase was isolated from P. aeruginosa by ultrafiltration of sterile-filtered culture supernatant. Gel filtration on Sepharose 4B yielded a broad peak corresponding to a molecular mass range of 100 to 1000 kDa. Electron microscopy of a negatively stained lipase preparation
R J Miles et al.
FEMS microbiology letters, 69(3), 283-287 (1992-01-15)
The propionate (Pro), decanoate (Dec) and laurate (Lau) esters of 5-(4-hydroxy-3,5-dimethoxyphenylmethylene)-2-thioxothiazoline++ +-3-acetic acid were assessed as substrates for lipase and esterase. On hydrolysis these substrates yield an intensely red coloured phenol which could be assayed at 505 nm. The Pro
A Gagné et al.
Canadian journal of microbiology, 47(10), 908-915 (2001-11-23)
Eight closely related thermophilic strains were isolated from an aerobic and thermophilic treatment of swine wastes. The pleomorphic cells (short and long rods; cocci) showed peritrichous flagella, terminally swollen sporangium, and liberated spores exhibiting hairy appendages. The Gram reaction was
Ming-Cheng Lin et al.
Chemistry and physics of lipids, 146(2), 85-93 (2007-02-06)
1,2-Ethylene-di-N-n-propylcarbamate (1) is characterized as an essential activator of Pseudomonas species lipase while 1,2-ethylene-di-N-n-butyl-, t-butyl-, n-heptyl-, and n-octyl-carbamates (2-5) are characterized as the pseudo substrate inhibitors of the enzyme in the presence of the detergent taurocholate or triton X-100. The
W Stuer et al.
Journal of bacteriology, 168(3), 1070-1074 (1986-12-01)
Lipase (triacylglycerol acylhydrolase, EC 3.1.1.3) was excreted by Pseudomonas aeruginosa PAC1R during the late logarithmic growth phase. Characterization of cell-free culture supernatants by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of significant amounts of lipopolysaccharide, part of which seemed
Protocols
Assay Procedure for Lipase
Enzymatic assay of lipase type XIII from Pseudomonas sp. using a coupled enzyme system of glycerol kinase and glycerophosphate oxidase (EC 3.1.1.3)
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