CHOLESTEROL ESTERASE

Base Information

• Chemical Name: CHOLESTEROL ESTERASE
• CAS No.: 9026-00-0
• Molecular Formula: NULL
• Molecular Weight: 0
• Hs Code.: 35079090
• Mol file: 9026-00-0.mol

Synonyms:Bilesalt-stimulated lipase;Biocatalytics E3;Bucelipase alfa;COE 311;Cholesterase;Cholesterin esterase;Cholesterol ester hydrolase;Cholesterolesterase;Cholesteryl ester hydrolase;Cholesteryl esterase;E.C. 3.1.1.13;Lysosomal acid lipase;Neutral cholesteryl ester hydrolase;Sterol esterhydrolase;

Chemical Property of CHOLESTEROL ESTERASE

Chemical Property:

• Appearance/Colour: White Powder
• Vapor Pressure: 0.004Pa at 25℃
• PSA: 0.00000
• LogP: 0.00000
• Storage Temp.: −20°C
• Solubility.: Dissolve 1mg/ml in 0.1M phosphate buffer, pH 6.0 to 7.0

Purity/Quality:

99.9% ^*data from raw suppliers

Cholesterol Esterase ^*data from reagent suppliers

Safty Information:

• Safety Statements: 22-24/25

MSDS Files:

Total 1 MSDS from other Authors

Useful:

• Uses: Cholesterol Esterase is used for enzymatic determination of total cholesterol when coupled with cholesterol oxidize in clinical analysis. Cholesterol esterase (CE) is a reversible enzyme that can hydrolyze or synthesize fatty acid esters of cholesterol and other sterols. 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 phaseto analyze the bioavailability of phytosterol and cholesterol in the aqueous micellar phase of an in vitro simulated digestion modelas a standard in enzyme activity assay Cholesterol Esterase from bovine pancreas has been used:in γ-oryzanol-hydrolyzing activityin cholesterol esterase enzyme activity for quantification of cholesterol and cholesterol esters associated in tear film and lenses samplesto test in vitro degradation of poly(fumaroyl bioxirane) maleate (PFM) polymer designed for bone tissue engineering

Refernces

Synthesis and enzymatic hydrolysis of esters, constituting simple models of soft drugs

10.1248/cpb.46.591

The research focuses on the synthesis and enzymatic hydrolysis of esters that serve as simple models of soft drugs, with the aim of minimizing systemic side effects of drugs by designing molecules that are rapidly inactivated after acting on their pharmacological targets. The study explores the tissue selectivity of hydrolytic metabolism and the molecular structural factors affecting the rate of enzymatic ester cleavage. The chemicals used in the process include a variety of esters, aromatic rings, and enzymes such as pig liver carboxyl esterase and cholesterol esterase. The conclusions drawn from the study indicate that while low tissue specificity was achieved with the substrates tested, both pig liver esterase and cholesterol esterase were found to be relevant test systems for predicting the rates of hydrolysis in tissue-derived fractions. The 2,4-diaminoquinazolines, however, were identified as poor substrates in the systems tested, suggesting that esters comprising a 2,4-diaminoquinazoline ring are not suitable as soft drugs.