Optimized oxidoreductases for medium and large scale industrial biotransformations
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126
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[ 2019 ]
Linde D, Ayuso-Fernández I, Ruiz-Dueñas FJ, Martínez AT Different fungal peroxidases oxidize nitrophenols at a surface catalytic tryptophan
Arch. Biochem. Biophys., 668: 23-28
[ 2019 ]
Serrano A, Sancho F, Viña-Gonzalez J, Carro J, Alcalde M, Guallar V, Martínez AT Switching the substrate preference of fungal aryl-alcohol oxidase: towards stereoselective oxidation of secondary benzyl alcohols
Catal. Sci. Technol., doi: 10.1039/C8CY02447B
[ 2019 ]
Viña-Gonzalez J, Jimenez-Lalana D, Sancho F, Serrano A, Martínez AT, Guallar V, Alcalde M Structure‐Guided Evolution of Aryl Alcohol Oxidase from Pleurotus eryngii for the Selective Oxidation of Secondary Benzyl Alcohols
Adv. Synth. Catal., 361: 2514-2525
[ 2018 ]
Carro J, Fernandez-Fueyo E, Fernández-Alonso C, Cañada J, Ullrich R, Hofrichter M, Alcalde M, Ferreira P, Martínez AT Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural
Biotechnol. Biofuels, 11: 86-96
[ 2018 ]
Carro J, Ferreira P, Martínez AT, Gadda G Stepwise Hydrogen Atom and Proton Transfers in Dioxygen Reduction by Aryl-Alcohol Oxidase
Biochemistry, doi: 10.1021/acs.biochem.8b00106
[ 2018 ]
Ewing TA, Kühn J, Segarra S, Tortajada M, Zuhse R, van Berkel WJ Multigram Scale Enzymatic Synthesis of (R)‐1‐(4′‐Hydroxyphenyl)ethanol Using Vanillyl Alcohol Oxidase
Adv. Synth. Catal., 360: 2370-2376
year2018
Self-sustained enzymatic cascade for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural
Carro J, Fernandez-Fueyo E, Fernández-Alonso C, Cañada J, Ullrich R, Hofrichter M, Alcalde M, Ferreira P, Martínez AT
Biotechnol. Biofuels, 11: 86-96
Background
2,5-Furandicarboxylic acid is a renewable building block for the production of polyfurandicarboxylates, which are biodegradable polyesters expected to substitute their classical counterparts derived from fossil resources. It may be produced from bio-based 5-hydroxymethylfurfural or 5-methoxymethylfurfural, both obtained by the acidic dehydration of biomass-derived fructose. 5-Methoxymethylfurfural, which is produced in the presence of methanol, generates less by-products and exhibits better storage stability than 5-hydroxymethylfurfural being, therefore, the industrial substrate of choice.
Results
In this work, an enzymatic cascade involving three fungal oxidoreductases has been developed for the production of 2,5-furandicarboxylic acid from 5-methoxymethylfurfural. Aryl-alcohol oxidase and unspecific peroxygenase act on 5-methoxymethylfurfural and its partially oxidized derivatives yielding 2,5-furandicarboxylic acid, as well as methanol as a by-product. Methanol oxidase takes advantage of the methanol released for in situ producing H2O2 that, along with that produced by aryl-alcohol oxidase, fuels the peroxygenase reactions. In this way, the enzymatic cascade proceeds independently, with the only input of atmospheric O2, to attain a 70% conversion of initial 5-methoxymethylfurfural. The addition of some exogenous methanol to the reaction further improves the yield to attain an almost complete conversion of 5-methoxymethylfurfural into 2,5-furandicarboxylic acid.
Conclusions
The synergistic action of aryl-alcohol oxidase and unspecific peroxygenase in the presence of 5-methoxymethylfurfural and O2 is sufficient for the production of 2,5-furandicarboxylic acid. The addition of methanol oxidase to the enzymatic cascade increases the 2,5-furandicarboxylic acid yields by oxidizing a reaction by-product to fuel the peroxygenase reactions.
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[ industrialoxidoreductases ]. Optimized oxidoreductases for medium and large scale industrial biotransformations. This project has received funding from the European Union’s Seventh Framework Programme for research, technological development and demonstration under Grant Agreement nº: FP7-KBBE-2013-7-613549. © indox 2013. Developed by
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