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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 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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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
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
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
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
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)

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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