Lipase from Pseudomonas cepacia
SIGMA/62309 - powder, light beige, ≥30 U/mg
Synonym: PCL; PS Lipase; Triacylglycerol acylhydrolase; Triacylglycerol lipase
CAS Number: 9001-62-1
EC Number: 232-619-9
MDL Number: MFCD00131509
Product Type: Chemical
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| biological source | bacterial (Pseudomonas cepacia) |
| color | light beige |
| form | powder |
| InChI | 1S/C11H9N3O2.Na/c15-8-4-5 |
| InChI key | QWZUIMCIEOCSJF-CHHCPSLASA |
| Quality Level | 100  |
| solubility | H2O: 2 mg/mL, hazy, faintly yellow |
| specific activity | ≥30 U/mg |
| storage condition | (Tightly closed. Dry) |
| storage temp. | 2-8°C |
| technique(s) | cell based assay: suitable |
| UniProt accession no. | A0A0J5WKE3  |
| 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. |
| 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. |
| Other Notes: | 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. |
| Other Notes: | Note: When triacetin is used as substrate, the pH is 7.4. Incubation time: 60 minutes. |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 1 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥30 U/mg |
| Storage Temp. | 2-8°C |
| Enzyme Commission (EC) Number | 3.1.1.3 ( BRENDA | IUBMB ) |
| UNSPSC | 12352204 |