Evaluation of deep eutectic solvents as new media for Candida antarctica B lipase catalyzed reactions

► Specific activity and stability of iCALB in deep eutectic solvents were studied. ► Some DESs can react and compete with the substrates in alcoholysis reactions. ► Reactivity for alcoholysis in deep eutectic mixtures may depend on the polarity of the nucleophilic substrate. This study aimed at anal...

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Veröffentlicht in:Process biochemistry (1991) 2012-12, Vol.47 (12), p.2081-2089
Hauptverfasser: Durand, E., Lecomte, J., Baréa, B., Piombo, G., Dubreucq, E., Villeneuve, P.
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Sprache:eng
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Zusammenfassung:► Specific activity and stability of iCALB in deep eutectic solvents were studied. ► Some DESs can react and compete with the substrates in alcoholysis reactions. ► Reactivity for alcoholysis in deep eutectic mixtures may depend on the polarity of the nucleophilic substrate. This study aimed at analyzing the advantages and limitations of several deep eutectic solvents (DESs) as ‘green solvents’ for biotransformation using immobilized Candida antarctica lipase B as catalyst. The transesterification of vinyl laurate was chosen as model reaction and the influence of substrate polarity was assessed using alcohols of various chain lengths. Results showed that grinding of immobilized lipase was essential parameters for good lipase activity. Moreover, in our model reaction some hydrogen-bond donor component from the DES can compete with the alcoholysis reaction. Indeed, side reactions were observed with DES based on dicarboxylic acid or ethylene glycol, leading to some limitations of their use. However, the results showed that other DESs such as choline chloride:urea and choline chloride:glycerol could exhibit high activity and selectivity making them promising solvents for lipase-catalyzed reactions. Finally, the best DES's specific activity – and stability up to five days incubation time – were analyzed and compared with conventional organic solvents. Experiments revealed that iCALB is less influenced by the chain length of alcohol in DES than organic solvents and it is preserves its activity with minimally destructive to protein structure.
ISSN:1359-5113
1873-3298
DOI:10.1016/j.procbio.2012.07.027