46058
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
Productos recomendados
biological source
Porcine liver
Quality Level
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
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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signalword
Danger
hcodes
pcodes
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)
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)
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