L9518
Lipase from Pseudomonas sp.
Type XIII, lyophilized powder, ≥15 units/mg solid
Synonym(s):
Triacylglycerol acylhydrolase, Triacylglycerol lipase
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About This Item
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type
Type XIII
Quality Level
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
Lipases are hydrolytic enzymes which break down triacylglycerides into free fatty acids and glycerols.
Application
This enzyme is useful 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). Usually, the reaction can be completed in 5 minutes at 37oC by using 2.5 oC~3.0 units of the enzyme per test (3.0ml) at pH around 7.0. Lipase from Pseudomonas sp. has been used in a study to assess enzymatic synthesis of biodiesel from palm oil assisted by microwave irradiation.
Biochem/physiol Actions
Lipase from Pseudomonas was shown to inhibit monocytes chemotaxis in human peripheral blood.
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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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
Patrícia C M Da Rós et al.
Bioprocess and biosystems engineering, 36(4), 443-451 (2012-08-21)
Optimal conditions for enzymatic synthesis of biodiesel from palm oil and ethanol were determined with lipase from Pseudomonas fluorescens immobilized on epoxy polysiloxane-polyvinyl alcohol hybrid composite under a microwave heating system. The main goal was to reduce the reaction time
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
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
T Miida et al.
Arteriosclerosis, thrombosis, and vascular biology, 20(11), 2428-2433 (2000-11-14)
Prebeta1-high density lipoprotein (prebeta1-HDL), the initial acceptor of cell-derived cholesterol, can be generated from HDL(2) by hepatic lipase. Because bezafibrate elevates lipase activity, it may increase prebeta1-HDL at the expense of HDL(2). To answer this question, we determined the apolipoprotein
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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