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.

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

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.

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)

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