Journal
CHEMCATCHEM
Volume 9, Issue 7, Pages 1182-1186Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cctc.201601342
Keywords
biocatalysis; enzymes; immobilization; metal-organic frameworks; supported catalysts
Categories
Funding
- Science Foundation Ireland [12/RC/2275]
- Programme for Third Level Institutions
- Irish Research Council [GOIPD/2015/287]
- Spanish Government [MAT-2012-31127]
- Spanish State Research Agency (Agencia Espanola de Investigacion, AEI)
- European Regional Development Fund (Fondo Europeo de Desarrollo Regional, FEDER) [MAT2016-77496-R]
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The use of a metal-organic framework (MOF) as a support for the insitu immobilization of enzymes was explored. The MOF support, a Basolite F300-like material, was prepared from FeCl3 and the tridentate linker trimesic acid. Immobilization of alcohol dehydrogenase, lipase, and glucose oxidase was performed insitu under mild conditions (aqueous solution, neutral pH, and at room temperature) in a rapid and facile manner with retention of activity for at least 1week. The catalytic activities of lipase and glucose oxidase were similar to the activities of the free enzymes; with alcohol dehydrogenase, there was a substantial decrease in activity on immobilization that may arise from diffusion limitations. The approach demonstrates that a MOF material, prepared from cheap and commercially available materials, can be successively utilized to prepare stable and catalytically active biocatalysts in a rapid and facile manner.
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