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], an important intermediate for the synthesis of diltiazem hydrochlorid.
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 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
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℃. 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.
Usage CHI'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.