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Issue 6, 2015
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Sporopollenin as an efficient green support for covalent immobilization of a lipase

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Abstract

Sporopollenin exine capsules (SECs), derived from the spores of Lycopodium clavatum, have been functionalised with 1,n-diamines and the resulting aminoalkyl microcapsules used to immobilize Candida antarctica lipase B (Cal B) via a glutaradehyde-based diimine covalent linker. The supported enzyme efficiently catalyzes the esterification of oleic acid with ethanol. Initial rates using the SEC-CalBs were comparable to the commercial enzyme Novozym 435, but displayed up to 20-fold higher specific activity. The supported enzymes could also be recycled and after four cycles displayed only a modest decrease in conversions. In a kinetic resolution the SEC-CalBs efficiently acetylated rac-1-phenylethanol, with conversions up to 37% after 5 hours and product enantiomeric excesses of >99%. Related to this, the dynamic resolution of rac-1-phenylethylamine, in the presence of Pd–BaSO4 and ammonium formate, led to the acetylated amine with a 94% conversion and >99% ee.

Graphical abstract: Sporopollenin as an efficient green support for covalent immobilization of a lipase

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Publication details

The article was received on 16 Dec 2014, accepted on 17 Jan 2015 and first published on 26 Jan 2015


Article type: Paper
DOI: 10.1039/C4CY01682C
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Citation: Catal. Sci. Technol., 2015,5, 3130-3136
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    Sporopollenin as an efficient green support for covalent immobilization of a lipase

    S. P. de Souza, J. Bassut, H. V. Marquez, I. I. Junior, L. S. M. Miranda, Y. Huang, G. Mackenzie, A. N. Boa and R. O. M. A. de Souza, Catal. Sci. Technol., 2015, 5, 3130
    DOI: 10.1039/C4CY01682C

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