Abstract
Lipase from Candida cylindracea catalyses two reactions between racemic hydroxyacid esters and octanoic acid in heptane: esterification of the hydroxy group, leading to acyloxyacid esters, and transesterification via acidolysis, liberating the free hydroxy acids. The reaction rate and stereochemical course of these pathways are dependent on the structure of the ester substrate. Enantioselective transesterification is the major reaction of ethyl 2-hydroxyhexanoate and leads to products of considerable optical purity. Shifting the position of the hydroxy group in the substrate causes increased esterification and a reversal of the enantioselectivities of the competing pathways. Analogous reactions in aqueous medium confirmed these phenomena.
| Original language | English |
|---|---|
| Pages (from-to) | 655-660 |
| Number of pages | 6 |
| Journal | Enzyme and Microbial Technology |
| Volume | 13 |
| Issue number | 8 |
| DOIs | |
| State | Published - Aug 1991 |
| Externally published | Yes |
Keywords
- Lipase
- enantioselectivity
- esterification
- hydroxyacid esters
- transesterification