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One‐Pot Enzyme Cascade for Controlled Synthesis of Furancarboxylic Acids from 5‐Hydroxymethylfurfural by H2O2 Internal Recycling
Furancarboxylic acids are promising biobased building blocks in pharmaceutical and polymer industries. In this work, dual‐enzyme cascade systems composed of galactose oxidase (GOase) and alcohol dehydrogenases (ADHs) are constructed for controlled synthesis of 5‐formyl‐2‐furancarboxylic acid (FFCA)...
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Published in: | ChemSusChem 2019-11, Vol.12 (21), p.4764-4768 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | Furancarboxylic acids are promising biobased building blocks in pharmaceutical and polymer industries. In this work, dual‐enzyme cascade systems composed of galactose oxidase (GOase) and alcohol dehydrogenases (ADHs) are constructed for controlled synthesis of 5‐formyl‐2‐furancarboxylic acid (FFCA) and 2,5‐furandicarboxylic acid (FDCA) from 5‐hydroxymethylfurfural (HMF), based on the catalytic promiscuity of ADHs. The byproduct H2O2, which is produced in GOase‐catalyzed oxidation of HMF to 2,5‐diformylfuran (DFF), is used for horseradish peroxidase (HRP)‐mediated regeneration of the oxidized nicotinamide cofactors for subsequent oxidation of DFF promoted by an ADH, thus implementing H2O2 internal recycling. The desired products FFCA and FDCA are obtained with yields of more than 95 %.
Internal affairs: A dual‐enzyme cascade system, composed of galactose oxidase and alcohol dehydrogenases (ADHs), is developed for controlled synthesis of furancarboxylic acids from 5‐hydroxymethylfurfural, based on the catalytic promiscuity of ADHs. The byproduct H2O2 is used for horseradish peroxidase‐mediated regeneration of the oxidized nicotinamide cofactors, thus implementing H2O2 internal recycling. |
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ISSN: | 1864-5631 1864-564X |
DOI: | 10.1002/cssc.201902199 |