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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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$119.00
500 MG
$434.00

About This Item

CAS Number:
EC Number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

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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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1 of 4

This Item
623168061262305
specific activity

≥30 U/mg

specific activity

≥2 U/mg

specific activity

≥30 U/mg

specific activity

~10 U/mg

technique(s)

cell based assay: suitable

technique(s)

analytical sample preparation: suitable

technique(s)

-

technique(s)

-

biological source

bacterial (Pseudomonas cepacia)

biological source

fungus (Candida rugosa)

biological source

fungus (Rhizopus oryzae)

biological source

-

form

powder

form

powder

form

powder

form

powder (fine)

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

storage temp.

2-8°C

solubility

H2O: 2 mg/mL, hazy, faintly yellow

solubility

water: slightly soluble

solubility

-

solubility

-

General description

Research area: cell-signaling

Lipase is a hydrolytic enzyme, found ubiquitously in nature. It belongs to the α/β-hydrolases fold family.[1] Lipase structure contains amphipathic helical lid domain in the active site that helps in interfacial activation of protein.[2]

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[3][4]
  • catalyze the hydrolysis of Morita-Baylis-Hillman acetates during enzymatic kinetic resolution of racemic Morita-Baylis-Hillman adducts[5]
  • 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.[6]

Biochem/physiol Actions

Lipases catalyze the hydrolysis of carboxylic ester bonds in triacylglycerols to yield glycerol and free fatty acids.[7][8] 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.[9] Lipolytic products and intermediates formed during lipolysis are involved in various cell-signaling processes.[10] Lipases have broad substrate specificity and high enantioselectivity.[11] This property of lipase makes it a good catalyst in organic synthesis.[1] Lipases play a vital role in fat digestion and metabolism.[7]

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

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

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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