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62309

Sigma-Aldrich

Lipase from Pseudomonas cepacia

powder, light beige, ≥30 U/mg

Synonym(s):

PCL, PS Lipase, 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

biological source

bacterial (Pseudomonas cepacia)

Quality Level

form

powder

specific activity

≥30 U/mg

storage condition

(Tightly closed. Dry)

technique(s)

cell based assay: suitable

color

light beige

solubility

H2O: 2 mg/mL, hazy, faintly yellow

UniProt accession no.

storage temp.

2-8°C

InChI

1S/C11H9N3O2.Na/c15-8-4-5-9(10(16)7-8)13-14-11-3-1-2-6-12-11;/h1-7,16H,(H,12,14);/q;+1/b13-9-;

InChI key

QWZUIMCIEOCSJF-CHHCPSLASA-N

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General description

Research area: cell-signaling

Lipase is a hydrolytic enzyme, found ubiquitously in nature. It belongs to the α/β-hydrolases fold family. Lipase structure contains amphipathic helical lid domain in the active site that helps in interfacial activation of protein.

Application

Lipases are used industrially for the resolution of chiral compounds and the transesterification production of biodiesel.

Lipase from Pseudomonas cepacian has been used to:
  • catalyze the degradation of polycaprolactone scaffold
  • catalyze the hydrolysis of Morita-Baylis-Hillman acetates during enzymatic kinetic resolution of racemic Morita-Baylis-Hillman adducts
  • as a standard for the generation of a calibration curve to determine the activity of lipase produced by microorganisms isolated from sludge derived from an urban wastewater treatment plant for ethanol production.

Biochem/physiol Actions

Lipases catalyze the hydrolysis of carboxylic ester bonds in triacylglycerols to yield glycerol and free fatty acids. Tri-, di-, and monoglycerides are hydrolyzed (in decreasing order of rate). Triacylglycerol lipases specifically hydrolyze the outer links of triacylglycerols and operate exclusively on the water-lipid interface. Lipolytic products and intermediates formed during lipolysis are involved in various cell-signaling processes. Lipases have broad substrate specificity and high enantioselectivity. This property of lipase makes it a good catalyst in organic synthesis. Lipases play a vital role in fat digestion and metabolism.

Unit Definition

1 U corresponds to the amount of enzyme which liberates 1 μmol oleic acid per minute at pH 8.0 and 40 °C (triolein, Cat. No. 62314 as substrate)

Other Notes

Note: When triacetin is used as substrate, the pH is 7.4. Incubation time: 60 minutes.
Chemoenzymatic synthesis of (-)-carbocyclic 7-deazaoxetanocin G

Pictograms

Health hazard

Signal Word

Danger

Hazard Statements

Precautionary Statements

Hazard Classifications

Resp. Sens. 1

Storage Class Code

11 - Combustible Solids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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Patricia Godoy et al.
Frontiers in microbiology, 9, 2634-2634 (2018-11-18)
A collection of lipase-producing microorganisms was isolated from sludge derived from an urban wastewater treatment plant. The microorganisms with the highest levels of lipase activity were selected in order to use triglycerides present in the sludge effectively and were then
3D-printed poly-$\varepsilon$-caprolactone-CaCO 3-biocompositescaffolds for hard tissue regeneration
Neumann R, et al.
Express Polymer Letters, 13(1) (2019)
4.5 - Biochemistry of Digestion
W.R. Terra, C. Ferreira
A Comprehensive Guide to the Hazardous Properties of Chemical Substances, 4 (2005)
Cammy K-M Chen et al.
Journal of molecular biology, 390(4), 672-685 (2009-05-19)
Several crystal structures of AFL, a novel lipase from the archaeon Archaeoglobus fulgidus, complexed with various ligands, have been determined at about 1.8 A resolution. This enzyme has optimal activity in the temperature range of 70-90 degrees C and pH
Shi-Lin Cao et al.
Scientific reports, 6, 20420-20420 (2016-02-05)
Magnetic cellulose nanocrystals (MCNCs) were prepared and used as an enzyme support for immobilization of Pseudomonas cepacialipase (PCL). PCL was successfully immobilized onto MCNCs (PCL@MCNC) by a precipitation-cross-linking method. The resulting PCL@MCNC with a nanoscale size had high enzyme loading

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