Esterase from porcine liver

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

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).

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

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.

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.

Suspension in 3.2 M (NH₄)₂SO₄, pH 8

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