Chloroperoxidase-Catalyzed Oxidation of 5-Hydroxymethylfurfural

Deurzen, M. P. J. van; Rantwijk, Fred van; Sheldon, Roger A.

doi:10.1080/07328309708006531

Cited by 90 publications

(43 citation statements)

References 18 publications

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“…Then the reaction proceeded to FDCA, although the conversion was rather inefficient, as UPO activity towards FFCA is much lower compared to HMF. Although oxidation of HMF and related compounds has not previously been described for a basidiomycete UPO, similar reactions have been reported for another member of the heme-thiolate peroxidase superfamily, chloroperoxidase (CPO, EC 1.11.1.10) from the ascomycete Caldariomyces fumago, albeit in the presence of high enzyme concentrations [29].…”

Section: Hmf and Dff: Two New Aao Substratesmentioning

confidence: 91%

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

Ferreira²,

et al. 2015

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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 H 2 O 2 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 H 2 O 2 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 O 2 is the only co-substrate required, and water is the only byproduct formed.

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Section: Hmf and Dff: Two New Aao Substratesmentioning

confidence: 91%

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

Ferreira²,

et al. 2015

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“…The first instance of enzymatic conversion of HMF into FDCA, to our knowledge, was described by van Deurzen et al (1997), Hanke (2009) using a chloroperoxidase from Caldariomyces fumago. This enzyme was able to oxidize both the alcohol and aldehyde moieties of HMF, producing a mix of FDCA, HMF acid, and in some cases DFF.…”

Section: Enzymatic Catalysts For the Production Of 25-furandicarboxymentioning

confidence: 99%

Whole-Cell Biocatalytic Production of 2,5-Furandicarboxylic Acid

Wierckx

Schuurman²,

Blank

et al. 2014

Microorganisms in Biorefineries

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“…CPO from Caldariomyces fumago is a heme-containing peroxidase producing mainly the single oxidized products diformyl furan (DFF) and 5-hydroxymethyl-2-furoic acid (HMF acid) (74 and 20%, respectively) from HMF. The triple-oxidation product FDCA is not formed (7).…”

mentioning

confidence: 99%

“…However, enzymes active on HMF are scarce. To date, only a few enzymes were shown to be active toward HMF (6,7), of which only one oxidizes HMF, chloroperoxidase (CPO). CPO from Caldariomyces fumago is a heme-containing peroxidase producing mainly the single oxidized products diformyl furan (DFF) and 5-hydroxymethyl-2-furoic acid (HMF acid) (74 and 20%, respectively) from HMF.…”

mentioning

confidence: 99%

Discovery and Characterization of a 5-Hydroxymethylfurfural Oxidase from Methylovorus sp. Strain MP688

Dijkman

Fraaije

2014

Appl Environ Microbiol

129

200

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In the search for useful and renewable chemical building blocks, 5-hydroxymethylfurfural (HMF) has emerged as a very promising candidate, as it can be prepared from sugars. HMF can be oxidized to 2,5-furandicarboxylic acid (FDCA), which is used as a substitute for petroleum-based terephthalate in polymer production. On the basis of a recently identified bacterial degradation pathway for HMF, candidate genes responsible for selective HMF oxidation have been identified. Heterologous expression of a protein from Methylovorus sp. strain MP688 in Escherichia coli and subsequent enzyme characterization showed that the respective gene indeed encodes an efficient HMF oxidase (HMFO). HMFO is a flavin adenine dinucleotide-containing oxidase and belongs to the glucose-methanol-choline-type flavoprotein oxidase family. Intriguingly, the activity of HMFO is not restricted to HMF, as it is active with a wide range of aromatic primary alcohols and aldehydes. The enzyme was shown to be relatively thermostable and active over a broad pH range. This makes HMFO a promising oxidative biocatalyst that can be used for the production of FDCA from HMF, a reaction involving both alcohol and aldehyde oxidations.

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Chloroperoxidase-Catalyzed Oxidation of 5-Hydroxymethylfurfural

Cited by 90 publications

References 18 publications

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

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

Whole-Cell Biocatalytic Production of 2,5-Furandicarboxylic Acid

Discovery and Characterization of a 5-Hydroxymethylfurfural Oxidase from Methylovorus sp. Strain MP688

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