Characterization of a New Glyoxal Oxidase from the Thermophilic Fungus Myceliophthora thermophila M77: Hydrogen Peroxide Production Retained in 5-Hydroxymethylfurfural Oxidation

Kadowaki, Marco Antonio Seiki; Godoy, Mariana Ortiz de; Kumagai, Patricia S.; Costa-Filho, Antonio J.; Mort, Andrew J.; Prade, Rolf A.; Polikarpov, Igor

doi:10.3390/catal8100476

Cited by 27 publications

(30 citation statements)

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“…Significant differences in the kinetic parameters and products’ yields for the oxidation of HMF were observed between the three enzymes, with the highest catalytic efficiency on HMF obtained with Pci GLOX3 ( K cat/ K m = 118.35 s −1 M −1 ). The oxidation of HMF using a phylogenetically different GLOX from Myceliophthora thermophila M77 ( Mt GLOX) has been recently published [32]. Similarly to Pci GLOX described in this paper, low conversion levels were observed with HMF.…”

Section: Resultsmentioning

confidence: 53%

“…This is the second example of alcohol oxidation by these enzymes, which have been previously found to be active on glycerol [25, 29]. HMF oxidation to DFF as the only product was recently observed with Mt GLOX; however this enzyme was unable to further oxidize DFF in the reaction [32]. Enzymes known to convert HMF to DFF include also AAO, alcohol oxidase, GAO, and HMFO [16, 18, 19, 33, 34] and these enzymes showed higher yields of DFF compared to Pci GLOX.…”

Section: Resultsmentioning

confidence: 84%

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Pycnoporus cinnabarinus glyoxal oxidases display differential catalytic efficiencies on 5-hydroxymethylfurfural and its oxidized derivatives

Daou

Yassine

Wikee

et al. 2019

Fungal Biol Biotechnol

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Background 5-Hydroxymethylfurfural (HMF), a major residual component of a lignocellulosic bio-refinery process, can be transformed into fundamental building blocks for green chemistry via oxidation. While chemical methods are well established, interest is also being directed into the enzymatic oxidation of HMF into the bio-plastic precursor 2,5-furandicarboxylic acid (FDCA). Results We demonstrate that three glyoxal oxidases ( Pci GLOX) isoenzymes from the Basidiomycete fungus Pycnoporus cinnabarinus were able to oxidize HMF, with Pci GLOX2 and Pci GLOX3 being the most efficient. The major reaction product obtained with the three isoenzymes was 5-hydroxymethyl-2-furancarboxylic (HMFCA), a precursor in polyesters and pharmaceuticals production, and very little subsequent conversion of this compound was observed. However, small concentrations of FDCA, a substitute for terephthalic acid in the production of polyesters, were also obtained. The oxidation of HMF was significantly boosted in the presence of catalase for Pci GLOX2, leading to 70% HMFCA yield. The highest conversion percentages were observed on 2,5-furandicarboxaldehyde (DFF), a minor product from the reaction of Pci GLOX on HMF. To bypass HMFCA accumulation and exploit the efficiency of Pci GLOX in oxidizing DFF and 5-formyl-2-furan carboxylic acid (FFCA) towards FDCA production, HMF was oxidized in a cascade reaction with an aryl alcohol oxidase ( Uma AAO). After 2 h of reaction, Uma AAO completely oxidized HMF to DFF and further to FFCA, with FDCA only being detected when Pci GLOX3 was added to the reaction. The maximum yield of 16% FDCA was obtained 24 h after the addition of Pci GLOX3 in the presence of catalase. Conclusions At least two conversion pathways for HMF oxidation can be considered for Pci GLOX; however, the highest selectivity was seen towards the production of the valuable polyester precursor HMFCA. The three isoenzymes showed differences in their catalytic efficiencies and substrate specificities when reacted with HMF derivatives. Electronic supplementary material The online version of this article (10.1186/s40694-019-0067-8) contains supplementary material, which is available to authorized users.

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Section: Resultsmentioning

confidence: 53%

Section: Resultsmentioning

confidence: 84%

Pycnoporus cinnabarinus glyoxal oxidases display differential catalytic efficiencies on 5-hydroxymethylfurfural and its oxidized derivatives

Daou

Yassine

Wikee

et al. 2019

Fungal Biol Biotechnol

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“…Select oxidases are capable of sequential oxidation of HMF to the various intermediates shown in Fig. 4 [ 14 , 70 – 74 ]. Hence, we analyzed the reaction kinetics and products of Fgr AAO and Fox AAO in each of these steps.…”

Section: Resultsmentioning

confidence: 99%

“…Fgr AAO and Fox AAO display similar specificity constants on HMF to the eponymous bacterial HMF oxidase (a GMC superfamily oxidoreductase) [ 73 ], and exhibit higher specificity constants than other enzymes with HMF oxidase activity, including some glyoxal oxidases from AA5_1 (Additional file 1 : Table S5) [ 70 , 71 , 74 ]. However, the recently reported Cgr AAO [ 19 ] has tenfold higher activity on HMF than both Fgr AAO and Fox AAO (Additional file 1 : Table S5).…”

Section: Resultsmentioning

confidence: 99%

Two Fusarium copper radical oxidases with high activity on aryl alcohols

Cleveland

Lafond

Xia

et al. 2021

Biotechnol Biofuels

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Background Biomass valorization has been suggested as a sustainable alternative to petroleum-based energy and commodities. In this context, the copper radical oxidases (CROs) from Auxiliary Activity Family 5/Subfamily 2 (AA5_2) are attractive biocatalysts for the selective oxidation of primary alcohols to aldehydes. Originally defined by the archetypal galactose 6-oxidase from Fusarium graminearum, fungal AA5_2 members have recently been shown to comprise a wide range of specificities for aromatic, aliphatic and furan-based alcohols. This suggests a broader substrate scope of native CROs for applications. However, only 10% of the annotated AA5_2 members have been characterized to date. Results Here, we define two homologues from the filamentous fungi Fusarium graminearum and F. oxysporum as predominant aryl alcohol oxidases (AAOs) through recombinant production in Pichia pastoris, detailed kinetic characterization, and enzyme product analysis. Despite possessing generally similar active-site architectures to the archetypal FgrGalOx, FgrAAO and FoxAAO have weak activity on carbohydrates, but instead efficiently oxidize specific aryl alcohols. Notably, both FgrAAO and FoxAAO oxidize hydroxymethyl furfural (HMF) directly to 5-formyl-2-furoic acid (FFCA), and desymmetrize the bioproduct glycerol to the uncommon L-isomer of glyceraldehyde. Conclusions This work expands understanding of the catalytic diversity of CRO from AA5_2 to include unique representatives from Fusarium species that depart from the well-known galactose 6-oxidase activity of this family. Detailed enzymological analysis highlights the potential biotechnological applications of these orthologs in the production of renewable plastic polymer precursors and other chemicals.

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“…Senger et al successfully analyzed the infrared characterization of [NiFe]-hydrogenase from Escherichia coli HYD-2 by in situ attenuated total reflection Fourier-transform infrared spectroscopy which proved as an efficient and powerful technique for the analysis of biological macromolecules and enzymatic small molecule catalysis [4]. Glyoxal oxidase, an extracellular oxidoreductase that oxidizes aldehydes and α-hydroxy carbonyl substrates coupled to the reduction of O 2 to H 2 O 2 , from Myceliophthora thermophyla, has been characterized by Kadowaki et al [5]. In addition, hydroxylation mechanism of soluble methane monooxygenase from Methylosinus sporium strain 5, a type II methanotrophs, was reported by Park et al, which revealed that two molar equivalents of methane monooxygenase regulatory protein B (MMOB) are necessary to achieve catalytic activities toward a broad range of substrates including alkanes, alkenes, halogens, and aromatics [6].…”

mentioning

confidence: 99%