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Lipase-A Recombinant ( Lipase A )
DescriptionRecombinant Immobilized Serratia marcescens Lipase-A is expressed in E.Coli having a Mw of 65 kDa is purified by standard chromatography techniques.SourceEscherichia Coli.Physical AppearanceSterile Filtered lyophilized
Data sheet
| 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. |
| Purity | Greater than 90% as determined by SDS-PAGE. |
| Description | Recombinant Immobilized Serratia marcescens Lipase-A is expressed in E.Coli having a Mw of 65 kDa is purified by standard chromatography techniques. |
| Protein Background | 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. |
| Expression host | Escherichia Coli. |
| Reagent Appearance | Sterile Filtered lyophilized powder. |
| 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. |
| 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 mol of p-nitrophenol per minute. |
| Biological Activity | 580 units/mg powder. |