Activity and enantioselectivity of wildtype and lid mutated Candida rugosa lipase isoform 1 in organic solvents
β Scribed by Francesco Secundo; Giacomo Carrea; Chiara Tarabiono; Stefania Brocca; Marina Lotti
- Publisher
- John Wiley and Sons
- Year
- 2004
- Tongue
- English
- Weight
- 103 KB
- Volume
- 86
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
π SIMILAR VOLUMES
The activity of different formulations of Candida antarctica lipase B (CALB), such as crude CALB, purified CALB, purified CALB lyophilized with PEG (CALB + PEG) or oleic acid (CALB + OA), and the commercial formulation Novozym 435, was determined in toluene, carbon tetrachloride, and 1,4-dioxane at
Lipase from Candida rugosa immobilized on a nylon support has been used to synthesize lovastatin, a drug which lowers serum cholesterol levels, by the regioselective acylation of a diol lactone precursor with 2methylbutyric acid in mixtures of organic solvents. Analogs of lovastatin having a differe
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 Β΅ g of protein was used in a reaction volume of 1 ml. Th
## 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