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Merck

E2884

Esterase from porcine liver

ammonium sulfate suspension, ≥150 units/mg protein (biuret)

Synonym(s):

Carboxyl esterase, Carboxylic-ester hydrolase, PLE

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About This Item

CAS Number:
9016-18-6
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
3.1.1.1 (BRENDA, IUBMB)
MDL number:
MFCD00131030
Specific activity:
≥150 units/mg protein (biuret)
Biological source:
Porcine liver

Key Documents

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biological source

Porcine liver

form

ammonium sulfate suspension

specific activity

≥150 units/mg protein (biuret)

mol wt

168 kDa

storage temp.

2-8°C

Quality Level

300

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General description

Esterase, also known as carboxyl ester hydrolase is a member of the hydrolase superfamily of enzymes.

Application

Esterase from porcine liver has been used to unmask the fluorescence in ultraviolet-visible spectroscopy.
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.
The enzyme from Sigma has been used to develop an alternative gel-based protocol for screening for bead-bound catalytic activity in aqueous media. The product has also been used to investigate the properties of the compound L-valine-3-{8-[(E)-2-[3-methoxyphenyl)ethenyl]-7-methyl-1-propargylxanthine-3-yl}propyl ester hydrochloride (MSX-4, an aminoacid ester prodrug of the adenosine A2A receptor antagonist MSX-2).

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.
Esterase enzyme of bacteria and fungi seems to have several industrial applications. It is capable of catalyzing the hydrolysis and synthesis of ester bonds.
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.

Physical form

Suspension in 3.2 M (NH4)2SO4, pH 8

Other Notes

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

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Regulatory Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

7783-20-2

CAS No.

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Certificates of Analysis (COA)

Lot/Batch Number
0000514354
0000514354
0000485712
0000485714
0000485715

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Karl Vollmann et al.
Molecules (Basel, Switzerland), 13(2), 348-359 (2008-02-29)
The compound L-valine-3-{8-[(E)-2-[3-methoxyphenyl)ethenyl]-7-methyl-1-propargylxanthine-3-yl}propyl ester hydrochloride (MSX-4) was synthesized as an amino acid ester prodrug of the adenosine A2A receptor antagonist MSX-2. It was found to be stable in artificial gastric acid, but readily cleaved by pig liver esterase.
Lipolysis and Metabolism of Fatty Acids in Cheese
Cheese, 423-444 (2017)
Fluorogenic affinity label for the facile, rapid imaging of proteins in live cells
Watkins RW, et al.
Organic & Biomolecular Chemistry, 7(19), 3969-3975 (2019)
B Wang et al.
Methods in molecular medicine, 23, 71-85 (1999-01-01)
With the discovery of an increasing number of biologically active peptides and peptide mimetics (1-3), there is a pressing need for the development of strategies to deliver these biologically active compounds to the desired site of action. The preceding two
Robert L Wilensky et al.
Nature medicine, 14(10), 1059-1066 (2008-09-23)
Increased lipoprotein-associated phospholipase A(2) (Lp-PLA(2)) activity is associated with increased risk of cardiac events, but it is not known whether Lp-PLA(2) is a causative agent. Here we show that selective inhibition of Lp-PLA(2) with darapladib reduced development of advanced coronary
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