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The use of a metal organic framework (MOF) as a support for the in-situ immobilisation of enzymes is described. The MOF support, a Basolite F300-like material, was prepared from FeCl3 and the tridentate linker trimesic acid. Immobilisation 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 one 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 utilised to prepare stable and catalytically active biocatalysts in a rapid and facile manner.
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Lipase AK from Pseudomonas fluorescens and Lipase RM from Rhizomucor miehei were encapsulated into a zeolite imidazolate framework (ZIF‐8) by a “one‐pot” synthesis to obtain AK@ZIF‐8 and RM@ZIF‐8 biocatalysts. The effect of a high (1:40) and low (1:4) Zn/2‐methylimidazole molar ratio on the biocatalysts synthesis was investigated. The different Zn/ligand (L) ratios affected both the surface area, the loading, and the specific activity of the biocatalysts. Samples synthesized by using a high Zn/L ratio had high values of surface area whereas those obtained by using a low Zn/L ratio had higher loadings and specific activities. The decrease of pH (from 11.6 to 9.4) during the synthesis at high Zn/L ratio produced ZIF‐8 samples with features similar to those observed for low Zn/L ratio samples. The low Zn/L (1:4) ratio AK@ZIF‐8 biocatalyst retained 99 % activity after storage for 15 days at 5 °C and 40 % activity after five reaction cycles.
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The use of an in-situ immobilization procedure for the immobilization of hyperhalophilic alcohol dehydrogenase in a metal organic framework material is described. The easy and rapid in situ immobilization process enables retention of activity over a broad range of pH and temperature together with a decrease in the halophilicity of the enzyme. The catalytic activity of the immobilized enzyme was studied in non-aqueous solvent mixtures with the highest retention of activity in aqueous solutions of methanol and ace-tonitrile. The approach demonstrates that this immobilization method can be extended to hyperhalophilic enzymes with enhancements in activity and stability.
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