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26745

Sigma-Aldrich

Cholesterol Esterase from porcine pancreas

lyophilized, powder, white, ~35 U/mg

Synonym(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

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.77

biological source

Porcine pancreas

form

powder

quality

lyophilized

specific activity

~35 U/mg

mol wt

Mr ~440000

color

white

storage temp.

−20°C

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General description

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

Biochem/physiol Actions

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.

Unit Definition

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)

Other Notes

Sales restrictions may apply

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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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
Isocoumarin-based inhibitors of pancreatic cholesterol esterase
Heynekamp JJ, et al.
Journal of Separation Science, 16(9), 5285-5294 (2008)
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
J. Siedel et al.
Methods of Enzymatic Analysis, 8, 139-139 (1985)

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