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L9518

Sigma-Aldrich

Lipase from Pseudomonas sp.

Type XIII, lyophilized powder, ≥15 units/mg solid

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Synonym(s):
Triacylglycerol acylhydrolase, Triacylglycerol lipase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

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)

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

Regulatory Information

含少量动物源组分生物产品
常规特殊物品

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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
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
Kinetics and Protein-Inhibitor Docking Studies of Enantiomers of exo-2-Norbornyl-N-n-butylcarbamates as Pseudomonas Lipase Inhibitors to Probe the Enantioselectivity of the Enzyme
Shen, Y-F. and Lin, G.
J. Chin. Chem. Soc., 59(1), 60-65 (2012)
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
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

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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