5‐hydroxymethylfurfural conversion by fungal aryl‐alcohol oxidase and unspecific peroxygenase

Oxidative conversion of 5‐hydroxymethylfurfural (HMF) is of biotechnological interest for the production of renewable (lignocellulose‐based) platform chemicals, such as 2,5‐furandicarboxylic acid (FDCA). To the best of our knowledge, the ability of fungal aryl‐alcohol oxidase (AAO) to oxidize HMF is...

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Published in:The FEBS journal 2015-08, Vol.282 (16), p.3218-3229
Main Authors: Carro, Juan, Ferreira, Patricia, Rodríguez, Leonor, Prieto, Alicia, Serrano, Ana, Balcells, Beatriz, Ardá, Ana, Jiménez‐Barbero, Jesús, Gutiérrez, Ana, Ullrich, René, Hofrichter, Martin, Martínez, Angel T
Format: Article
Language:English
Subjects:
2,5‐formylfurancarboxylic acid
2,5‐furandicarboxylic acid
5‐hydroxymethylfurfural
active sites
Agrocybe - enzymology
Alcohol
Alcohol Oxidoreductases - metabolism
aryl‐alcohol oxidase
Biotechnology
Catalytic Domain
Enzymes
Fungal Proteins - metabolism
Fungi
Furaldehyde - analogs & derivatives
Furaldehyde - chemistry
Furaldehyde - metabolism
Gas Chromatography-Mass Spectrometry
glycols
heme
hydrogen peroxide
hydroxymethylfurfural
Kinetics
Lignin - metabolism
Magnetic Resonance Spectroscopy
Mixed Function Oxygenases - metabolism
oxidation
Oxidation-Reduction
oxygen
Pleurotus - enzymology
Renewable Energy
unspecific peroxygenase
Water - metabolism
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Summary:Oxidative conversion of 5‐hydroxymethylfurfural (HMF) is of biotechnological interest for the production of renewable (lignocellulose‐based) platform chemicals, such as 2,5‐furandicarboxylic acid (FDCA). To the best of our knowledge, the ability of fungal aryl‐alcohol oxidase (AAO) to oxidize HMF is reported here for the first time, resulting in almost complete conversion into 2,5‐formylfurancarboxylic acid (FFCA) in a few hours. The reaction starts with alcohol oxidation, yielding 2,5‐diformylfuran (DFF), which is rapidly converted into FFCA by carbonyl oxidation, most probably without leaving the enzyme active site. This agrees with the similar catalytic efficiencies of the enzyme with respect to oxidization of HMF and DFF, and its very low activity on 2,5‐hydroxymethylfurancarboxylic acid (which was not detected by GC‐MS). However, AAO was found to be unable to directly oxidize the carbonyl group in FFCA, and only modest amounts of FDCA are formed from HMF (most probably by chemical oxidation of FFCA by the H₂O₂ previously generated by AAO). As aldehyde oxidation by AAO proceeds via the corresponding geminal diols (aldehyde hydrates), the various carbonyl oxidation rates may be related to the low degree of hydration of FFCA compared with DFF. The conversion of HMF was completed by introducing a fungal unspecific heme peroxygenase that uses the H₂O₂ generated by AAO to transform FFCA into FDCA, albeit more slowly than the previous AAO reactions. By adding this peroxygenase when FFCA production by AAO has been completed, transformation of HMF into FDCA may be achieved in a reaction cascade in which O₂ is the only co‐substrate required, and water is the only by‐product formed.
ISSN:1742-464X
1742-4658
DOI:10.1111/febs.13177