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26745

Sigma-Aldrich

Cholesterol Esterase from porcine pancreas

lyophilized, powder, white, ~35 U/mg

Synonyme(s) :

bile salt-dependent lipase, bile salt-stimulated lipase, carboxyl ester lipase, nonspecific lipase, pancreatic lysophospholipase, Cholesterol Esterase from hog pancreas, Sterol-ester acylhydrolase

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About This Item

Numéro CAS:
Numéro de classification (Commission des enzymes):
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352204
Nomenclature NACRES :
NA.77

Source biologique

Porcine pancreas

Forme

powder

Qualité

lyophilized

Activité spécifique

~35 U/mg

Poids mol.

Mr ~440000

Couleur

white

Température de stockage

−20°C

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Description générale

Research area: Cell signaling

Pancreatic cholesterol esterase (CEase), also known as bile salt stimulated lipase, is a serine hydrolase belonging to the α/β hydrolase family of enzymes. They are released from the exocrine pancreas. Serine 194, histidine 435 and aspartate 320 represent the catalytic triad of the enzyme.

Application

Cholesterol Esterase from porcine pancreas has been used:
  • in an in vitro simulated digestion model to improve the hydrolysis of carotenoid esters in the intestinal phase
  • to analyze the bioavailability of phytosterol and cholesterol in the aqueous micellar phase of an in vitro simulated digestion model
  • as a standard in enzyme activity assay

Actions biochimiques/physiologiques

Cholesterol esterase (CEase), an enzyme having broad substrate specificity plays a key role in regulating the bile salt mediated hydrolysis of dietary cholesteryl esters. It also participates in the hydrolysis of triglycerides and phospholipids which are essential for normal cholesterol absorption. Cholesterol esterase hydrolysis helps in the determination of total cholesterol levels in the serum and plasma. Additionally, cholesterol esterase (CEase) along with phospholipase A2 is involved in the hydrolysis of lecithin to lysolecithin, forming intestinal micelles that deliver free cholesterol to enterocytes. Loss of enzyme function results in reduced intestinal absorption of dietary cholesteryl esters and prevents the formation of intestinal micelles, thereby failing to deliver cholesterol efficiently. Circulating cholesterol esterases, accumulated in atherosclerotic lesions are involved in triggering the proliferation of smooth muscle cells. Lastly, they are also selectively involved in the hydrolysis/condensation of carboxylic ester bonds.

Définition de l'unité

1 U corresponds to the amount of enzyme which liberates 1 μmol cholesterol per minute at pH 7.0 and 37°C (cholesterol acetate as substrate)

Autres remarques

Sales restrictions may apply

Pictogrammes

Health hazard

Mention d'avertissement

Danger

Mentions de danger

Conseils de prudence

Classification des risques

Resp. Sens. 1

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)


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Consulter la Bibliothèque de documents

R.J. Kazlauskas
Journal of the American Chemical Society, 111, 4953-4953 (1989)
Baojian Li et al.
European journal of medicinal chemistry, 45(5), 1955-1963 (2010-02-13)
Due to the importance of pancreatic cholesterol esterase (CEase) as a potential target in atherosclerosis and for the development of hypocholesterolemic agents, there are increasing interests in designing and synthesizing CEase inhibitors. In the present study, we prepared forty-five isocoumarin
Isocoumarin-based inhibitors of pancreatic cholesterol esterase
Heynekamp JJ, et al.
Journal of Separation Science, 16(9), 5285-5294 (2008)
Ömer Şahin et al.
Journal of biomolecular structure & dynamics, 1-15 (2021-01-23)
In this work, Combining coumarin and thiazole with 3-tertiary butyl salicylaldehyde into in a single molecule, new Schiff base (CTS), and its metal complexes with palladium and platinum were synthesized and characterized by using well-known spectroscopic techniques such as 1H-NMR
J. Siedel et al.
Methods of Enzymatic Analysis, 8, 139-139 (1985)

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