L9518
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-669-1
MDL number:
Product Name
Lipase from Pseudomonas sp., Type XIII, lyophilized powder, ≥15 units/mg solid
type
Type XIII
form
lyophilized powder
specific activity
≥15 units/mg solid
mol wt
~134 kDa
composition
Protein, 40-65% biuret
storage temp.
2-8°C
Quality Level
Analysis Note
Protein determined by biuret.
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).
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.
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.
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)
Other Notes
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
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
含少量动物源组分生物产品
常规特殊物品
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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
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
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
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
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
Protocols
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)
Assay Procedure for Lipase
脂肪酶催化脂质的水解。该实验方案使用与酶活性成比例的比色测定法。用分光光度法在545 nm处测量醌亚胺染料的外观。
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