62309
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:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-619-9
MDL number:
Specific activity:
≥30 U/mg
Biological source:
bacterial (Pseudomonas cepacia)
InChI key
QWZUIMCIEOCSJF-CHHCPSLASA-N
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-;
biological source
bacterial (Pseudomonas cepacia)
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
Quality Level
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.
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:
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.
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)
Chemoenzymatic synthesis of (-)-carbocyclic 7-deazaoxetanocin G.
Note: When triacetin is used as substrate, the pH is 7.4. Incubation time: 60 minutes.
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
Regulatory Information
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Enzymatic kinetic resolution of Morita-Baylis-Hillman acetates
Juma WP, et al., et al.
Tetrahedron Asymmetry, 28(9), 155-155 (2017)
Emily Cottam et al.
Medical engineering & physics, 31(2), 221-226 (2008-09-02)
This paper investigates the effect of sterilisation by gamma irradiation (dose 2.5Mrad) on the following properties of polycaprolactone (PCL): (1) degradation rate (catalysed by lipase), (2) mechanical properties, (3) the ability of cells to attach and subsequently grow on its
Biochemistry, Lipase
Pirahanchi Y and Sharma S
StatPearls [Internet] (2022)
X. Chen et al.
Tetrahedron Letters, 33, 2249-2249 (1992)
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
Articles
Efficient epimerization catalyst for enzyme mediated dynamic kinetic resolution (DKR).
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