Immobilization of epoxide hydrolase from Aspergillus niger onto DEAE-cellulose: enzymatic properties and application for the enantioselective resolution of a racemic epoxide |
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Authors: | S Karboune A Archelas R Furstoss J Baratti |
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Institution: | Université de la Méditerranée, Groupe Biocatalyse et Chimie Fine, UMR CNRS 6111, Faculté des Sciences de Luminy, Case 901, 163 avenue de Luminy, 13288 Marseille Cedex 9, France |
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Abstract: | 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. |
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Keywords: | Epoxide hydrolase Aspergillus niger Immobilization Enzymatic resolution Reactor |
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