Enhanced enzyme activity and enantioselectivity of lipases in organic solvents by crown ethers and cyclodextrins
โ Scribed by Yurie Mine; Kimitoshi Fukunaga; Kyoko Itoh; Makoto Yoshimoto; Katsumi Nakao; Yoshiaki Sugimura
- Book ID
- 114399447
- Publisher
- Elsevier Science
- Year
- 2003
- Tongue
- English
- Weight
- 1001 KB
- Volume
- 95
- Category
- Article
- ISSN
- 1389-1723
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๐ SIMILAR VOLUMES
5 5.1 a Relative to crude lipase BC taken as 1. b The transesterifi cation between 1 -octanol (0.19 M) and vinyl butyrate (0.79 M) to give 1 -octyl butyrate and acetaldehyde was used as a model reaction. An amount of enzyme form containing 10 ยต g of protein was used in a reaction volume of 1 ml. Th
## Abstract Colyophilization or codrying of subtilisin Carlsberg with the crown ethers 18โcrownโ6, 15โcrownโ5, and 12โcrownโ4 substantially improved enzyme activity in THF, acetonitrile, and 1,4โdioxane in the transesterification reactions of __N__โacetylโLโphenylalanine ethylester and 1โpropanol 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 2.4โ and 1.7โfold, respectively), when lyophilized with 18โcrownโ6. Nevertheless, the increase was observed only for lo