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46058

Sigma-Aldrich

Esterase from porcine liver

lyophilized, powder, slightly beige, ≥50 U/mg

Sinónimos:

Carboxyl esterase, Carboxylic-ester hydrolase, PLE

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About This Item

Número de CAS:
9016-18-6
Comisión internacional de enzimas:
3.1.1.1 (BRENDA, IUBMB)
EC Number:
232-773-7
MDL number:
MFCD00131030
UNSPSC Code:
12352204
NACRES:
NA.54

biological source

Porcine liver

Quality Level

100

form

lyophilized solid
powder

quality

lyophilized

specific activity

≥50 U/mg

mol wt

Mr ~162000

color

slightly beige

storage temp.

−20°C

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General description

Porcine liver esterase (PLE) is localized in the endoplasmic reticulum (ER).

Application

Esterase from porcine liver has been used as a negative control in fluorescence measurement studies.
Pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry.
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.
Porcine liver esterase (PLE) displays good stability, broad substrate specificity, and is a low-cost enzyme. It is useful in the hydrolysis of ester- and amide-containing compounds, to free acids and is useful detoxification of xenobiotics.

Components

contiene 1,4-ditioeritritol

Unit Definition

1 U corresponde a la cantidad de enzima que hidroliza 1 μmol de etil valerato (Fluka® No. 30784) por minuto a pH 8.0 y 25°C

Other Notes

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pictograms

Health hazard
GHS08

signalword

Danger

hcodes

H334

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)

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Elke Brüsehaber et al.
Bioorganic & medicinal chemistry, 17(23), 7878-7883 (2009-11-04)
The possible physiological role of PLE (E.C. 3.1.1.1) located in the endoplasmic reticulum (ER) of pig liver cells in the conversion of endogenous compounds was investigated as it was reported, that PLE acts as prenylated methylated protein methyl esterase (PMPMEase)
Scale-up of a recombinant pig liver esterase-catalyzed desymmetrization of Dimethyl Cyclohex-4-ene-cis-1, 2-dicarboxylate
Su?ss P, et al.
Organic Process Research & Development, 18 (2014)
Active-site model for interpreting and predicting the specificity of pig liver esterase
Toone, EJ et al.
Journal of the American Chemical Society, 112, 4946-4952 (1990)
Bornscheuer, UT & Kazlauskas, RJ
Hydrolases in Organic Synthesis, 2 (2005)
Qing Zhu et al.
Macromolecular rapid communications, 31(12), 1060-1064 (2011-05-19)
Herein we describe a novel and simple conjugated polymer-fluorescent probe based platform for trypsin detection from protein mixtures in homogeneous solution. This platform takes advantage of specific interaction between the probe and the active site of trypsin and the electrostatic
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