46058
Esterase from porcine liver
lyophilized, powder, slightly beige, ≥50 U/mg
Synonym(s):
Carboxyl esterase, Carboxylic-ester hydrolase, PLE
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biological source
Porcine liver
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.
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
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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Toone, EJ et al.
Journal of the American Chemical Society, 112, 4946-4952 (1990)
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)
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)
Bornscheuer, UT & Kazlauskas, RJ
Hydrolases in Organic Synthesis, 2 (2005)
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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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