A Novel 2,5-Furandicarboxylic Acid Biosynthesis Route from Biomass-Derived 5-Hydroxymethylfurfural Based on the Consecutive Enzyme Reactions

Shu-li, WU; Liu, Qishun; Tan, Haidong; Zhang, Fuyun; Yin, Heng

doi:10.1007/s12010-020-03290-1

Cited by 20 publications

(18 citation statements)

References 40 publications

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“…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. In recent years, several strategies have been followed to increase the performance of Metsp HMFO for FDCA bioproduction, such as its coexpression with the HmfH enzyme, which oxidizes HMF by the HMFCA route ( 3 ), in whole-cell systems ( 22 ), directed mutagenesis of Metsp HMFO ( 23 ), or its combination with lipase in an enzymatic cascade ( 24 ).…”

Section: Introductionmentioning

confidence: 99%

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: Introductionmentioning

confidence: 99%

Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Viñambres

Espada

Martínez

et al. 2020

Appl Environ Microbiol

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“…MP688 (46% aa identity) and termed HmfO [53] . Due to its biocatalytic potential, the properties of HmfO have been comprehensively studied [52] , [54] , [55] , [56] , [57] . It should be noted that most probably HMFCA or FFCA are not physiological substrates for this enzyme since no hmfABCDE genes could be identified by us in the genome of Methylovorus sp .…”

Section: Resultsmentioning

confidence: 99%

Widespread distribution of hmf genes in Proteobacteria reveals key enzymes for 5-hydroxymethylfurfural conversion

Donoso

González-Toro

Pérez‐Pantoja

2021

Computational and Structural Biotechnology Journal

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“…An enzymatic cascade reaction leading to a product yield of 94% was introduced by the combining 5-hydroxymethylfurfural oxidase (HMFO) of Methylovorus sp. MP688 and Novozym 435 [ 252 ].…”

Section: Biocatalytic Production Of Monomersmentioning

confidence: 99%

Prospects of Using Biocatalysis for the Synthesis and Modification of Polymers

Nikulin

Švedas

2021

Molecules

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Trends in the dynamically developing application of biocatalysis for the synthesis and modification of polymers over the past 5 years are considered, with an emphasis on the production of biodegradable, biocompatible and functional polymeric materials oriented to medical applications. The possibilities of using enzymes not only as catalysts for polymerization but also for the preparation of monomers for polymerization or oligomers for block copolymerization are considered. Special attention is paid to the prospects and existing limitations of biocatalytic production of new synthetic biopolymers based on natural compounds and monomers from biomass, which can lead to a huge variety of functional biomaterials. The existing experience and perspectives for the integration of bio- and chemocatalysis in this area are discussed.

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A Novel 2,5-Furandicarboxylic Acid Biosynthesis Route from Biomass-Derived 5-Hydroxymethylfurfural Based on the Consecutive Enzyme Reactions

Cited by 20 publications

References 40 publications

Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Screening and Evaluation of New Hydroxymethylfurfural Oxidases for Furandicarboxylic Acid Production

Widespread distribution of hmf genes in Proteobacteria reveals key enzymes for 5-hydroxymethylfurfural conversion

Prospects of Using Biocatalysis for the Synthesis and Modification of Polymers

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