Hydrolysis of p-nitrophenyl laurate in supercritical carbon dioxide: comparison of two different enzymes
β Scribed by Shireesh Srivastava; Giridhar Madras
- Book ID
- 102314475
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 2001
- Tongue
- English
- Weight
- 74 KB
- Volume
- 76
- Category
- Article
- ISSN
- 0268-2575
- DOI
- 10.1002/jctb.442
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β¦ Synopsis
Abstract
The enzymatic hydrolysis of pβnitrophenyl laurate (PNPL) to pβnitrophenol (PNP) was studied in supercritical carbon dioxide using crude Hog Pancreas Lipase (HPL) and P roqueforti Lipase (PRL). The two enzymes were compared for their optimal activity temperatures and reaction kinetics. HPL had a higher optimal temperature (65βΒ°C) and better yield (22.5%) compared with PRL whose optimal temperature was 50βΒ°C with a 15.3% yield. This is considerably higher than the optimum temperature of 37βΒ°C and yields of less than 1% observed in the aqueous medium.
Β© 2001 Society of Chemical Industry
π SIMILAR VOLUMES
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