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E3019

Sigma-Aldrich

Esterase from porcine liver

lyophilized powder, ≥15 units/mg solid

Synonym(s):

Carboxyl esterase, Carboxylic-ester hydrolase, PLE

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About This Item

CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

form

lyophilized powder

specific activity

≥15 units/mg solid

mol wt

168 kDa

application(s)

diagnostic assay manufacturing

storage temp.

−20°C

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Application

Esterase from porcine liver has been used in a study to assess the effect of 5-aminolaevulinic acid peptide prodrugs on photosensitization for photodynamic therapy. Esterase from porcine liver has also been used in a study to investigate how site-specific atherogenic gene expression correlates with subsequent variable lesion development in coronary and peripheral vasculature.
The enzyme from Sigma has been immobilised in hollow fibre ultrafiltration membrane and used for the asymmetric hydrolysis of a meso-diester. Esterase from Sigma has been used to investigate its effect on the release of methacrylic acid (MAA) and 2-hydroxyethyl methacrylate (HEMA) from adhesives formulated under conditions simulating wet bonding. It has been used to examine the ability of carboxylesterase activity to remove permethrin- and bifenthrin-associated toxicity to Ceriodaphnia dubia and Hyalella azteca in a variety of matrices.
Porcine liver esterase is used to catalyze the hydrolysis of pentaacetyl catechin and epicatechin for use in pharmaceutical and industrial applications.

Pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry.

Biochem/physiol Actions

Esterase acts on water-soluble carboxyl esters containing short chain fatty acids. Its functionality is attributed to the catalytic triad of Ser, His and Asp/Glu.
Pig liver esterase catalyzes enantioselective conversion of an ester to a carboxylic acid. The molecular weight is found to be 168 kDa. It is a serine enzyme with two active sites on each molecule, which dissociates into active half-molecules in the presence of dilute acid or concentrated salts.

Unit Definition

One unit will hydrolyze 1.0 μmole of ethyl butyrate to butyric acid and ethanol per min at pH 8.0 at 25 °C.

pictograms

Health hazard

signalword

Danger

hcodes

Hazard Classifications

Resp. Sens. 1

Storage Class

11 - Combustible Solids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


Certificates of Analysis (COA)

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Craig E Wheelock et al.
Environmental toxicology and chemistry, 25(4), 973-984 (2006-04-25)
Increases in the use and application of pyrethroid insecticides have resulted in concern regarding potential effects on aquatic ecosystems. Methods for the detection of pyrethroids in receiving waters are required to monitor environmental levels of these insecticides. One method employed
Kazuhito Watanabe et al.
Biological & pharmaceutical bulletin, 28(9), 1743-1747 (2005-09-06)
The properties of ES46.5K, an esterase from mouse hepatic microsomes, were compared with those of carboxylesterases from rabbit and porcine liver. The inhibitory profile with a serine hydrolase inhibitor (bis-p-nitrophenylphosphate) and detergents (sodium dodecylsulfate, Emulgen 911) was different between ES46.5K
Elisabet L Kostoryz et al.
Journal of biomedical materials research. Part B, Applied biomaterials, 88(2), 394-401 (2008-04-09)
Dentin adhesives may undergo phase separation when bonding to wet demineralized dentin. We hypothesized that adhesives exhibiting phase separation will experience enhanced biodegradation of methacrylate ester groups. The objective of this project was to study the effect of enzyme-exposure on
Enzyme-responsive snap-top covered silica nanocontainers.
Kaushik Patel et al.
Journal of the American Chemical Society, 130(8), 2382-2383 (2008-02-01)
Pig liver esterase. Reactions with alcohols, structure-reactivity correlations, and the acyl-enzyme intermediate.
P Greenzaid et al.
Biochemistry, 10(7), 1210-1222 (1971-03-30)

Protocols

Objective: To standardize a procedure for the enzymatic determination of Esterase activity using Ethyl Butyrate as a substrate.

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