Sporopollenin as an efficient green support for covalent immobilization of a lipaseElectronic supplementary information (ESI) available. See DOI: 10.1039/c4cy01682c

• Main Authors: de Souza, Stefânia P, Bassut, Jonathan, Marquez, Heiddy V, Junior, Ivaldo I, Miranda, Leandro S. M, Huang, Youkui, Mackenzie, Grahame, Boa, Andrew N, de Souza, Rodrigo O. M. A
• Format: Article
• Language: English
• ISSN: 2044-4753; 2044-4761
• DOI: 10.1039/c4cy01682c

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-BaSO 4 and ammonium formate, led to the acetylated amine with a 94% conversion and >99% ee. Aminoalkyl functionalised sporopollenin exine capsules have been used to immobilize Candida antarctica lipase B using a covalent diimine-based linker.