z-logo
Premium
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 , metal organic framework , trimesic acid , glucose oxidase , in situ , alcohol dehydrogenase , catalysis , aqueous solution , combinatorial chemistry , biocatalysis , organic chemistry , alcohol , 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.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom