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L9518

Sigma-Aldrich

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

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
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

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.

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)

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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

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