L9518
Lipase from Pseudomonas sp.
Type XIII, lyophilized powder, ≥15 units/mg solid
Synonyme(s) :
Extracellular lipase, Triacylglycerol ester hydrolase, lip, Triacylglycerol acylhydrolase, Triacylglycerol lipase
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About This Item
Produits recommandés
Type
Type XIII
Niveau de qualité
Forme
lyophilized powder
Activité spécifique
≥15 units/mg solid
Poids mol.
~134 kDa
Composition
Protein, 40-65% biuret
Température de stockage
2-8°C
Description générale
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.
Actions biochimiques/physiologiques
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).
Propriétés physiques
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)
Définition de l'unité
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.
Forme physique
Lyophilized powder containing Mg+2, sodium cholate, and bovine serum albumin as stabilizers
Remarque sur l'analyse
Protein determined by biuret.
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Équipement de protection individuelle
Eyeshields, Gloves, type N95 (US)
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Les clients ont également consulté
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)
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
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