Two-step oxidation of glycerol to glyceric acid catalyzed by the Phanerochaete chrysosporium glyoxal oxidase

Roncal, Tomás; Muñoz, C.; Lorenzo, Leire; Maestro, Belén; Guereñu, María del Mar Díaz de

doi:10.1016/j.enzmictec.2011.11.007

Cited by 18 publications

(20 citation statements)

References 19 publications

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“…In the case of MtGLOx, the hypothesis of H 2 O 2 oxidative damage was not supported by our experimental results, since catalase addition was unable to promote an increased MtGLOx activity ( Figure S2B). The same phenomenon was observed for GLOx from P. chrysosporium [25]. A selective oxidation mechanism of primary alcohols to aldehydes has been previously described for a flavoenzyme, aryl-alcohol oxidase [49].…”

Section: Catalytic Properties Of Mtgloxsupporting

confidence: 75%

“…A possible autooxidation of 5-HMF in solution was discarded, as can be seen in the reaction control ( Figure S2A). The low yields have been attributed to oxidative damage that is caused by H 2 O 2 , acidification, in the case of carboxylic acid products, or end-product inhibition [25]. In the case of MtGLOx, the hypothesis of H 2 O 2 oxidative damage was not supported by our experimental results, since catalase addition was unable to promote an increased MtGLOx activity ( Figure S2B).…”

Section: Catalytic Properties Of Mtgloxmentioning

confidence: 67%

“…The time course reaction shows that MtGLOx oxidized 56% of the HMF in 24 h ( Figure 2C) but it was unable to further oxidize DFF. Low conversion levels were also observed for other characterized GLOxes [25,27] and for a new AA5_2 from Colletotrichum graminicola able to oxidize 1-butanol to butanal [33]. A possible autooxidation of 5-HMF in solution was discarded, as can be seen in the reaction control ( Figure S2A).…”

Section: Catalytic Properties Of Mtgloxmentioning

confidence: 72%

“…Family AA5 also includes a second subfamily, AA5_2, containing galactose and alcohol oxidases. GLOx couples the two-electron oxidation of aldehydes to carboxylic acids to the reduction of O 2 to H 2 O 2 [21,24,25], α-Hydroxy carbonyl and α-diol substrates can also be oxidized in two steps to carboxylic acids. Previous reports on the enzymatic activity of GLOxes from Phanerochaete chrysosporium [26] and Pycnoporus cinnabarinus [27] indicate that glyoxal and methylglyoxal are the best substrates for the enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…Both aldehydes are recognized as products of glucose degradation through a combination of retroaldol condensation and auto-oxidation , and are found in ligninolytic cultures [28,29]. Another reported substrate that is oxidized by GLOx is glycerol, formed in bulk during biodiesel production [25]. Experimental evidence suggests that GLOxes need to be activated by other enzymes such as lignin peroxidases and can enhance lignolytic activity of white-rot fungi in biomass degradation [26,29,30].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2018

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Myceliophthora thermophyla is a thermophilic industrially relevant fungus that secretes an assortment of hydrolytic and oxidative enzymes for lignocellulose degradation. Among them is glyoxal oxidase (MtGLOx), an extracellular oxidoreductase that oxidizes several aldehydes and α-hydroxy carbonyl substrates coupled to the reduction of O2 to H2O2. This copper metalloprotein belongs to a class of enzymes called radical copper oxidases (CRO) and to the “auxiliary activities” subfamily AA5_1 that is based on the Carbohydrate-Active enZYmes (CAZy) database. Only a few members of this family have been characterized to date. Here, we report the recombinant production, characterization, and structure-function analysis of MtGLOx. Electron Paramagnetic Resonance (EPR) spectroscopy confirmed MtGLOx to be a radical-coupled copper complex and small angle X-ray scattering (SAXS) revealed an extended spatial arrangement of the catalytic and four N-terminal WSC domains. Furthermore, we demonstrate that methylglyoxal and 5-hydroxymethylfurfural (HMF), a fermentation inhibitor, are substrates for the enzyme.

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Section: Catalytic Properties Of Mtgloxsupporting

confidence: 75%

Section: Catalytic Properties Of Mtgloxmentioning

confidence: 67%

Section: Catalytic Properties Of Mtgloxmentioning

confidence: 72%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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

et al. 2018

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Unveiling Cutting Edge Innovations in the Catalytic Valorization of Biodiesel Byproduct Glycerol into Value Added Products

et al. 2023

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The increasing production of biodiesel has led to a glut in the production of glycerol, which is a byproduct. This has resulted in the quest for alternative applications using glycerol as a cheap and readily available starting material. One promising approach is the catalytic valorization of glycerol, which converts glycerol into valuable chemicals such as 1,2‐propanediol, lactic acid, and acrolein. The glycerol formed affects the efficiency of the biodiesel, and hence it must be removed. Different processes can convert glycerol to various useful products like glycerol carbonate, glycidol, solketal, lactic acid, and glyceric acid. These different products, the processes used for synthesis, and the various catalysts used have been discussed. The most effective methods for the syntheses, the numerous catalyst systems, mechanisms of the reactions, and applications of these products in different fields are discussed in this review. The paper also discusses the challenges and opportunities of glycerol valorization, including the need for improved catalyst selectivity and activity and the potential for integrating glycerol valorization with other biorefinery processes. Overall, the catalytic valorization of glycerol offers a promising pathway for utilizing this abundantly available resource, and this review provides valuable insights for researchers and practitioners working in this area.

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Glyoxal oxidases: their nature and properties

Daou

Faulds

2017

World J Microbiol Biotechnol

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HO has been found to be required for the activity of the main microbial enzymes responsible for lignin oxidative cleavage, peroxidases. Along with other small radicals, it is implicated in the early attack of plant biomass by fungi. Among the few extracellular HO-generating enzymes known are the glyoxal oxidases (GLOX). GLOX is a copper-containing enzyme, sharing high similarity at the level of active site structure and chemistry with galactose oxidase. Genes encoding GLOX enzymes are widely distributed among wood-degrading fungi especially white-rot degraders, plant pathogenic and symbiotic fungi. GLOX has also been identified in plants. Although widely distributed, only few examples of characterized GLOX exist. The first characterized fungal GLOX was isolated from Phanerochaete chrysosporium. The GLOX from Utilago maydis has a role in filamentous growth and pathogenicity. More recently, two other glyoxal oxidases from the fungus Pycnoporus cinnabarinus were also characterized. In plants, GLOX from Vitis pseudoreticulata was found to be implicated in grapevine defence mechanisms. Fungal GLOX were found to be activated by peroxidases in vitro suggesting a synergistic and regulatory relationship between these enzymes. The substrates oxidized by GLOX are mainly aldehydes generated during lignin and carbohydrates degradation. The reactions catalysed by this enzyme such as the oxidation of toxic molecules and the production of valuable compounds (organic acids) makes GLOX a promising target for biotechnological applications. This aspect on GLOX remains new and needs to be investigated.

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Two-step oxidation of glycerol to glyceric acid catalyzed by the Phanerochaete chrysosporium glyoxal oxidase

Cited by 18 publications

References 19 publications

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

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

Unveiling Cutting Edge Innovations in the Catalytic Valorization of Biodiesel Byproduct Glycerol into Value Added Products

Glyoxal oxidases: their nature and properties

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