Complete oxidation of hydroxymethylfurfural to furandicarboxylic acid by aryl-alcohol oxidase

Serrano, Ana; Calviño, Eva; Carro, Juan; Sánchez-Ruiz, María Isabel; Cañada, F. Javier; Martínez, Ángel T.

doi:10.1186/s13068-019-1555-z

Cited by 56 publications

(80 citation statements)

References 31 publications

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“…The new enzymes from Pseudomonas strains were able to directly produce FDCA from HMF, with slight differences in their optimal reaction conditions, such as the higher activity and stability of Pseni HMFO under slightly alkaline conditions. Although the new HMFOs do not show more activity on HMF and DFF than Metsp HMFO, it is important to mention that they show higher efficiencies for FFCA oxidation, the rate-limiting step in FDCA production by HMFO ( 14 ) and other oxidases ( 16 ).…”

Section: Discussionmentioning

confidence: 90%

“…peroxygenase (15,20), GLOX/AAO (21) or AAO/catalase (16) couples, already reported. Therefore, MetspHMFO is the only enzyme described to date able to perform by itself (i.e.…”

Section: Downloaded Frommentioning

confidence: 86%

“…Steady-state kinetic parameters for HMF and DFF oxidation by HMFOs were calculated by monitoring the production of H 2 O 2 during oxidation of the different substrates, using an HRP-coupled assay with AmplexRed as the final substrate in 50 mM Tris-HCl, pH 7.0, as previously described ( 16 ).…”

Section: Methodsmentioning

confidence: 99%

“…Other oxidases, such as galactose oxidase (GAO) from Dactylium dendroides and glyoxal oxidase (GLOX) from Pycnoporus cinnabarinus , have also been reported to act on furfural derivatives, but their activity is restricted to the alcohol or the aldehyde groups, respectively ( 15 ). A recent study has demonstrated the ability of aryl-alcohol oxidase (AAO) from Pleurotus eryngii to catalyze the separate oxidation of HMF, DFF, and FFCA, although the complete oxidation of HMF by AAO stops at the FFCA level, due to inhibition of the last oxidation step by the peroxide generated in the first two reactions ( 16 ). More recently, a new copper radical oxidase from Colletotrichum graminicola has been described as an AAO-type enzyme and reported to oxidize HMF into DFF and 5-hydroxymethylfurancarboxylic acid (HMFCA) into FFCA without detected activity on the aldehyde groups of these compounds ( 17 ).…”

Section: Introductionmentioning

confidence: 99%

“…More recently, a new copper radical oxidase from Colletotrichum graminicola has been described as an AAO-type enzyme and reported to oxidize HMF into DFF and 5-hydroxymethylfurancarboxylic acid (HMFCA) into FFCA without detected activity on the aldehyde groups of these compounds ( 17 ). Due to the above-named characteristics, efficient production of FDCA by the latter oxidases requires the combination of several enzymes, such as the AAO/chloroperoxidase ( 18 ), AAO/peroxygenase ( 15 , 19 ), GAO/peroxygenase ( 15 , 20 ), GLOX/AAO ( 21 ), or AAO/catalase ( 16 ) couples already reported. Therefore, Metsp HMFO is the only enzyme described to date able to perform by itself (i.e., without the concourse of a second enzyme) the three oxidation steps for FDCA production from HMF.…”

Section: Introductionmentioning

confidence: 99%

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Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Viñambres

Espada

Martínez

et al. 2020

Appl Environ Microbiol

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The enzymatic production of 2,5-furandicarboxylic acid (FDCA) from 5-hydroxy-methylfurfural (HMF) has gained interest in recent years, as the renewable precursor of poly(ethylene-2,5-furandicarboxylate) (PEF). 5-Hydroxymethylfurfural oxidases (HMFOs) form a flavoenzyme family with genes annotated in a dozen bacterial species, but only one enzyme purified and characterized to date (after heterologous expression of a Methylovorus sp hmfo gene). This oxidase acts on both furfuryl alcohols and aldehydes being, therefore, able to catalyze the conversion of HMF into FDCA through 2,5-diformylfuran (DFF) and 2,5-formylfurancarboxylic acid (FFCA), with the only need of oxygen as cosubstrate. To enlarge the repertoire of HMFO enzymes available, genetic databases were screened for putative hmfo genes, followed by heterologous expression in Escherichia coli. After unsuccessful trials with other bacterial hmfo genes, HMFOs from two Pseudomonas species were produced as active soluble enzymes, purified and characterized. The Methylovorus sp enzyme was also produced and purified in parallel for comparison. Enzyme stability against temperature, pH and hydrogen peroxide, three key aspects for application, were evaluated (together with optimal conditions for activity) revealing differences between the three HMFOs. Also the kinetic parameters for HMF, DFF and FFCA oxidation were determined, having the new HMFOs higher efficiencies for the oxidation of FFCA, which constitutes the bottleneck in the enzymatic route for FDCA production. These results were used to set up the best conditions for FDCA production by each enzyme, attaining a compromise between optimal activity and half-life under different operation conditions. IMPORTANCE: HMFO is the only enzyme described to date catalyzing by itself the three consecutive oxidation steps to produce FDCA from HMF. Unfortunately, only one HMFO enzyme is currently available for biotechnological application. This availability is enlarged here by the identification, heterologous production, purification and characterization of two new HMFOs from Pseudomonas nitroreducens and an unidentified Pseudomonas species. Compared to the previously known Methylovorus HMFO, the new enzyme from P. nitroreducens exhibits better performance for FDCA production in wider pH and temperature ranges, with higher tolerance to the hydrogen peroxide formed, longer half-life during oxidation, and higher yield and total turnover number in long-term conversions under optimized conditions. All these features are relevant properties for the industrial production of FDCA. In summary, gene screening and heterologous expression can facilitate the selection and improvement of HMFO enzymes as biocatalysts for the enzymatic synthesis of renewable building blocks in the production of bioplastics.

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Section: Discussionmentioning

confidence: 90%

“…peroxygenase (15,20), GLOX/AAO (21) or AAO/catalase (16) couples, already reported. Therefore, MetspHMFO is the only enzyme described to date able to perform by itself (i.e.…”

Section: Downloaded Frommentioning

confidence: 86%

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Viñambres

Espada

Martínez

et al. 2020

Appl Environ Microbiol

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Aryl‐Alcohol‐Oxidase‐Mediated Synthesis of Piperonal and Other Valuable Aldehydes

2022

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The use of fungal aryl‐alcohol oxidases in biocatalysis is still modest, despite their advantageous capability to produce valuable aldehydes via oxidation of the respective alcohols without the need for costly external cofactors. For biocatalytic application, enzyme stability in the presence of organic solvents used for substrate solubilization has to be investigated, and process limitations due to low oxygen supply and the accumulation of the by‐product H2O2 must be addressed. In this study, we showed that the aryl‐alcohol oxidase PeAAO2 from Pleurotus eryngii P34 remained active and stable in the presence of up to 30% (v/v) various organic solvents and up to 500 mM H2O2. The potential of this biocatalyst was explored based on conversion of piperonyl alcohol to the fragrance compound piperonal. After reaction optimization, product titers of up to 245 mM were achieved within 3 h. Addition of catalase was imperative to re‐introduce O2 as co‐substrate into the reaction, thereby diminishing oxygen limitation. On a preparative scale, space‐time‐yield of 9.5 g/l/h was achieved and 244.6 mg piperonal (85% yield) with >99% purity were isolated via simple crystallization from n‐hexane extract. Under optimized reaction conditions four other substrates, cumic alcohol, 2‐thiophenemethanol, trans,trans‐2,4‐heptadienol and trans‐2‐cis‐6‐nonadienol, at concentrations of up to 300 mM were converted to the corresponding aldehydes within 20 h. Our results demonstrate that PeAAO2 is a versatile and promising biocatalyst for the production of valuable aldehydes.

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Efficient Oxidation of 5‐Hydroxymethylfurfural Using a Flavoprotein Oxidase from the Honeybee Apis mellifera

Tjallinks,

Boverio,

Jager

et al. 2023

ChemBioChem

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The chemical 5‐hydroxymethylfurfural (HMF) can be derived from lignocellulose and is an interesting bio‐based platform chemical as it has the potential to be transformed into numerous valuable building blocks such as the polymer‐precursor 2,5‐diformylfuran (DFF). To date, only few oxidases acting on HMF are known and by sampling atypical species, we discovered a novel flavin‐dependent oxidoreductase from the honeybee Apis mellifera (beeHMFO). The enzyme can perform the chemoselective oxidation of HMF to DFF but can also readily accept other aromatic alcohols as substrates. The function of the enzyme may well be the antimicrobial generation of hydrogen peroxide using HMF, which is very abundant in honey. The discovery of this insect‐derived flavoprotein oxidase holds promising potential in the synthesis of renewable products and demonstrates that insects can be an interesting source for novel biocatalysts.

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Complete oxidation of hydroxymethylfurfural to furandicarboxylic acid by aryl-alcohol oxidase

Cited by 56 publications

References 31 publications

Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Aryl‐Alcohol‐Oxidase‐Mediated Synthesis of Piperonal and Other Valuable Aldehydes

Efficient Oxidation of 5‐Hydroxymethylfurfural Using a Flavoprotein Oxidase from the Honeybee Apis mellifera

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