Enzymatic catalysis in supercritical carbon dioxide: Comparison of different lipases and a novel esterase
β Scribed by H. Michor; R. Marr; T. Gamse; T. Schilling; E. Klingsbichel; H. Schwab
- Book ID
- 104637187
- Publisher
- Springer Netherlands
- Year
- 1996
- Tongue
- English
- Weight
- 429 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0141-5492
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β¦ Synopsis
The resolution of racemic citronellol and menthol by enzymatically catalyzed transesterification in supercritical carbon dioxide (SC-C02) was investigated. Different lipases and an esterase in connection with various acylating reagents were employed. While the transesterification of (+)-menthol was reasonably fast and gave high enantiomeric excess, resolution of (?)-citronellol was not feasible.
π SIMILAR VOLUMES
## Abstract The stability and activity of lipases from __Pseudomonas fluorescens, Rhizopus javanicus, Rhizopus niveus__, porcine pancreas and __Candida rugosa__ in a nonβsolvent system at atmospheric pressure, in supercritical carbon dioxide (SCβCO~2~), and nearβcritical propane at 100 bar and 40βΒ°