Immobilization of epoxide hydrolase from Aspergillus niger onto DEAE-cellulose: enzymatic properties and application for the enantioselective resolution of a racemic epoxide
| Autor: | Alain Archelas, Roland Furstoss, Jacques C. Baratti, Salwa Karboune |
|---|---|
| Rok vydání: | 2005 |
| Předmět: |
biology
Immobilized enzyme Chemistry Process Chemistry and Technology Aspergillus niger Batch reactor Enantioselective synthesis Epoxide Bioengineering biology.organism_classification Biochemistry Catalysis Hydrolysis chemistry.chemical_compound Bioreactor Organic chemistry Epoxide hydrolase Nuclear chemistry |
| Zdroj: | Journal of Molecular Catalysis B: Enzymatic. 32:175-183 |
| ISSN: | 1381-1177 |
| Popis: | Recombinant epoxide hydrolase (EH) from Aspergillus niger can be a very promising tool for the resolution of various racemic epoxides by enantioselective hydrolysis. The enzyme was successfully immobilized by ionic adsorption onto DEAE-cellulose (99% yield, 70% of retention activity). The temperature for maximal activity (40 °C) and the activation energy (38.8 kJ/mol) were similar for both the immobilized and free EHs, whereas the optimal pH was about one unit less for the immobilized enzyme. Thermal stability was also affected by immobilization; the immobilized enzyme appeared to be slightly less stable than the free one. However, a gram-scale resolution of racemic para-chlorostyrene oxide (pCSO) was successfully carried out in a repeated batch reactor, operated for seven cycles. Furthermore, using a very high substrate concentration of 2 M (306 g/L), i.e. biphasic conditions, the resolution of 3 g of pCSO was also achieved in a repeated batch reactor using approximately 300 mg of immobilized EH, corresponding to less than 3 mg of the enzymatic powder. |
| Databáze: | OpenAIRE |
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