Why do crown ethers activate enzymes in organic solvents?
β Scribed by Dirk-Jan van Unen; Johan F. J. Engbersen; David N. Reinhoudt
- Publisher
- John Wiley and Sons
- Year
- 2001
- Tongue
- English
- Weight
- 122 KB
- Volume
- 77
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
## Abstract Colyophilization or codrying of subtilisin Carlsberg with the crown ethers 18βcrownβ6, 15βcrownβ5, and 12βcrownβ4 substantially improved enzyme activity in THF, acetonitrile, and 1,4βdioxane in the transesterification reactions of __N__βacetylβLβphenylalanine ethylester and 1βpropanol a
## Abstract Lipase from __Burkholderia cepacia__ (lipase BC) and lipase B from __Candida antarctica__ (CALB) show an increase of the transesterification activity in toluene (up to 2.4β and 1.7βfold, respectively), when lyophilized with 18βcrownβ6. Nevertheless, the increase was observed only for lo
Catalytic activities of β£-chymotrypsin and subtilisin Carlsberg in various hydrous organic solvents were measured as a function of how the enzyme suspension had been prepared. In one method, lyophilized enzyme was directly suspended in the solvent containing 1% water. In another, the enzyme was prec
The dramatic activation of serine proteases in nonaqueous media resulting from lyophilization in the presence of KCl is shown to be unrelated to relaxation of potential substrate diffusional limitations. Specifically, lyophilizing subtilisin Carlsberg in the presence of KCl and phosphate buffer in d