46058

Sigma-Aldrich

Esterase from porcine liver

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

Synonym(s):
PLE, Carboxylic-ester hydrolase, Carboxyl esterase
CAS Number:
Enzyme Commission number:
EC Number:
MDL number:
NACRES:
NA.54

Quality Level

form

lyophilized solid
powder

quality

lyophilized

specific activity

≥50 U/mg

mol wt

Mr ~162000

color

slightly beige

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

General description

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

Application

Pig liver esterase is commonly used for kinetic resolutions and assymetric synthesis in organic chemistry.
Esterase from porcine liver has been used as a negative control in fluorescence measurement studies.
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

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.
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.

Components

contains 1,4-dithioerythritol

Unit Definition

1 U corresponds to the amount of enzyme which hydrolyzes 1 μmol ethyl valerate (CAt. No. 30784) per minute at pH 8.0 and 25°C

Other Notes

Sales restrictions may apply

Personal Protective Equipment

dust mask type N95 (US),Eyeshields,Gloves

RIDADR

NONH for all modes of transport

WGK Germany

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificate of Analysis

Certificate of Origin

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)
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)
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...
Bornscheuer, UT & Kazlauskas, RJ
Hydrolases in Organic Synthesis, 2 (2005)

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.