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Rapid In Situ Immobilization of Enzymes in Metal–Organic Framework Supports under Mild Conditions
Author(s) -
Gascón Victoria,
Carucci Cristina,
Jiménez Mayra B.,
Blanco Rosa M.,
SánchezSánchez Manuel,
Magner Edmond
Publication year - 2017
Publication title -
chemcatchem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.497
H-Index - 106
eISSN - 1867-3899
pISSN - 1867-3880
DOI - 10.1002/cctc.201601342
Subject(s) - lipase , immobilized enzyme , chemistry , trimesic acid , metal organic framework , glucose oxidase , in situ , catalysis , alcohol dehydrogenase , aqueous solution , organic chemistry , combinatorial chemistry , biocatalysis , enzyme , reaction mechanism , molecule , adsorption
The use of a metal–organic framework (MOF) as a support for the in situ immobilization of enzymes was explored. The MOF support, a Basolite F300‐like material, was prepared from FeCl 3 and the tridentate linker trimesic acid. Immobilization of alcohol dehydrogenase, lipase, and glucose oxidase was performed in situ under mild conditions (aqueous solution, neutral pH, and at room temperature) in a rapid and facile manner with retention of activity for at least 1 week. 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.