Catalogue number
ENZ-473
Introduction
Lipase (EC 3.1.1.3) is a ubiquitous enzyme that catalyzes the hydrolysis of fats and oil. The Serratia marcescens lipase is recognized for its excellent enantioselectivity in biocatalytic hydrolysis of trans-3-(4-methoxyphynyl) glycidic acid methyl ester [(±)-MPGM] to produce (2R, 3S)-3-(4-methoxyphenyl) glycidic acid methyl ester [(-)-MPGM].
Description
Recombinant Immobilized Serratia marcescens Lipase-A is expressed in E.Coli having a Mw of 65 kDa is purified by standard chromatography techniques.
Source
Escherichia Coli.
Physical Appearance
Sterile Filtered lyophilized powder.
Formulation
The protein was lyophilized without additives.
Solubility
It is recommended to reconstitute the lyophilized Lipase-A in sterile 10%-50% DMSO, isopropyl ether, petroleum ether, ethanol, acetone and isopropanol.
Stability
Recombinant Lipase-A although stable at room temp for 1 week, should be stored desiccated below -18C.
For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please prevent freeze-thaw cycles.
Application Stability
pH5~10
Unstable at higher than 50°C.
Higher activity can be reached in 10%-50% DMSO, isopropyl ether and petroleum ether, 10%-25% ethanol, acetone and isopropanol, 50% activity can be kept in 50% acetone and isopropanol, no activity detected in 50% ethanol.
Purity
Greater than 90% as determined by SDS-PAGE.
Unit Definition
Lipase-A was assayed using p-nitrophenyl acetate ( pNPA) as a substrate.
One unit of lipase activity was defined as the amount of enzyme releasing 1.0 μmol of p-nitrophenol per minute.
Biological Activity
580 units/mg powder.
Safety Data Sheet
Usage
ProSpec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
