| Autor: |
Geerlof A; Department of Microbiology and Enzymology, Delft University of Technology, The Netherlands., Jongejan JA, van Dooren TJ, Racemakers-Franken PC, van den Tweel WJ, Duine JA |
| Jazyk: |
angličtina |
| Zdroj: |
Enzyme and microbial technology [Enzyme Microb Technol] 1994 Dec; Vol. 16 (12), pp. 1059-63. |
| DOI: |
10.1016/0141-0229(94)90143-0 |
| Abstrakt: |
Acetobacter pasteurianus oxidizes glycidol with high activity, comparable to the oxidation of ethanol. The organism has a preference for the S-enantiomer, and the kinetic resolution process obeys a simple relationship, indicating an enantiomeric ratio (E) of 19. The compound is converted into glycidic acid, although a transient accumulation of glycidaldehyde occurs initially. Determination of other parameters revealed a temperature optimum of 50 degrees C, long-term stability (cells in the resting state), and a pH optimum compatible with the chemical stability of glycidol. However, it was also noted that respiration rates decrease at concentrations of glycidol above 1 M. This is most likely caused by substrate inhibition of the glycidol-oxidizing enzyme, the quinohemoprotein ethanol dehydrogenase. Comparison with existing methods for enantiomerically pure glycidol production indicated a number of attractive points for the method described here, although definitive evaluation must await further studies on the long-term stability under process conditions, reusability of the cells, and the mechanism of glycidol inhibition. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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