Enantioselective hydrolysis of methoxyphenyl glycidic acid methyl ester [(±)-MPGM] by a thermostable and alkalostable lipase from Pseudomonas aeruginosa
| Autor: | Sawraj Singh, Uttam Chand Banerjee |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
chemistry.chemical_classification
biology Chemistry Process Chemistry and Technology Triacylglycerol lipase Bioengineering Biochemistry Medicinal chemistry Catalysis Glycidic acid Hydrolysis chemistry.chemical_compound Enzyme biology.protein Organic chemistry Lipase Enantiomeric excess Magnesium ion Thermostability |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic. 36:30-35 |
| ISSN: | 1381-1177 |
| DOI: | 10.1016/j.molcatb.2005.07.005 |
| Popis: | A potent bacterial strain, Pseudomonas aeruginosa, has been isolated from the soil which produces extracellular lipase that can carry out the excellent stereospecific hydrolysis of trans-3-(4-methoxyphenyl)glycidic acid methyl ester [(±)-MPGM)] to give [(−)-MPGM], an intermediate required in the synthesis of cardiovascular drug, diltiazem. As a preliminary experiment for enzymatic resolution, we characterized the fractionated enzyme. The enzyme had a pH and temperature optima of 8.0 and 60 °C, respectively. The enzyme showed high degree of thermostability. Also, the enzyme was found to be stable in alkaline condition and in organic solvents. The activity of the enzyme increased by the addition of magnesium ions. The small-scale hydrolysis of (±)-MPGM (250 mg) with partially purified enzyme (21,000 U) gave (−)-MPGM with good isolated yield (44%) and excellent enantiomeric excess (99.9%) in a very short time (12 h). |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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