1.1.3.47: 5-(hydroxymethyl)furfural oxidase
This is an abbreviated version!
For detailed information about 5-(hydroxymethyl)furfural oxidase, go to the full flat file.
Word Map on EC 1.1.3.47
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1.1.3.47
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synthesis
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2,5-furandicarboxylic
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biocatalyst
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bio-based
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biocatalytic
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oxidases
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putida
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methylovorus
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basilensis
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fed-batch
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petroleum-based
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terephthalate
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cupriavidus
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flavin
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ornithinolytica
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biomass-derived
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raoultella
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eugenol
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enantioselective
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polyesters
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cosolvents
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one-pot
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fusing
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biotechnology
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biofuel production
- 1.1.3.47
- synthesis
-
2,5-furandicarboxylic
-
biocatalyst
-
bio-based
-
biocatalytic
- oxidases
- putida
- methylovorus
- basilensis
-
fed-batch
-
petroleum-based
- terephthalate
-
cupriavidus
- flavin
- ornithinolytica
-
biomass-derived
-
raoultella
- eugenol
-
enantioselective
-
polyesters
-
cosolvents
-
one-pot
-
fusing
- biotechnology
- biofuel production
Reaction
Synonyms
5-hydroxymethylfurfural oxidase, AAO, AOX1, GaoB, Glox2, Glox3, GLRG_02805, HFMO, HMF oxidase, HMF/furfural oxidoreductase, HmfH, HMFO, MPQ_0130
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Application
Application on EC 1.1.3.47 - 5-(hydroxymethyl)furfural oxidase
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biofuel production
biotechnology
development of a facile gene shuffling approach to rapidly combine stabilizing mutations in a one-pot reaction. This allows the identification of the optimal combination of several beneficial mutations. The approach quickly discriminates stable and active multi-site variants, making it a very useful addition to FRESCO (framework for rapid enzyme stabilization by computational libraries) method
synthesis
current large-scale pretreatment processes for lignocellulosic biomass are generally accompanied by the formation of toxic degradation products, such as 5-hydroxymethylfurfural (HMF), which inhibit cellulolytic enzymes and fermentation by ethanol-producing yeast. Overcoming these toxic effects is a key technical barrier in the biochemical conversion of plant biomass to biofuels. Pleurotus ostreatus, a white-rot fungus, can efficiently degrade lignocellulose, and it can tolerate and metabolize HMF involving HMF oxidase (HMFO) encoded by HmfH
biofuel production
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current large-scale pretreatment processes for lignocellulosic biomass are generally accompanied by the formation of toxic degradation products, such as 5-hydroxymethylfurfural (HMF), which inhibit cellulolytic enzymes and fermentation by ethanol-producing yeast. Overcoming these toxic effects is a key technical barrier in the biochemical conversion of plant biomass to biofuels. Pleurotus ostreatus, a white-rot fungus, can efficiently degrade lignocellulose, and it can tolerate and metabolize HMF involving HMF oxidase (HMFO) encoded by HmfH
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biocatalytic production of furan-2,5-dicarboxylate, a biobased platform chemical for the production of polymers
synthesis
AAO is able to produce 2,5-furandicarboxylic acid from formylfurancarboxylic acid, allowing full oxidation of 5-hydroxymethylfurfural. During 5-hydroxymethylfurfural reactions, an inhibitory effect of the H2O2 produced in the first two oxidation steps is the cause of the lack of AAO activity on formylfurancarboxylic acid. 5-Hydroxymethylfurfural is successfully converted into 2,5-furandicarboxylic acid when the AAO reaction is carried out in the presence of catalase
synthesis
biooxidation of benzylic alcohols in the presence of various organic (co)solvents. The enzyme activity decreases at elevated concentrations of water-miscible polar solvents, while the presence of (halogenated) hydrocarbons is tolerated up to 90% (v/v), which leads to drastically improved conversions of up to >99% in case of hexafluorobenzene. This effect is correlated with the improved solubility of O2 in the employed solvents
synthesis
enantioselective oxidation of sec-allylic alcohols using variants of the berberine bridge enzyme analogue from Arabidopsis thaliana (AtBBE15) and the 5-(hydroxymethyl)furfural oxidase (HMFO) and its variants V465T, V465S, V465T/W466H and V367R/W466F. The enantioselectivity can be tuned by applying either pressure or by the addition of cosolvents
synthesis
expression of HMFO in Pseudomonas putida S12 for the biocatalytic conversion of 5-hydroxymethylfurfural to FDCA. 35.7 mM 2,5-furandicarboxylic acid is produced from 50 mM 5-hydroxymethylfurfural in 24 h without notable inhibition. When the initial 5-ydroxymethylfurfural concentration is elevated to 100 mM, remarkable inhibition on 2,5-furandicarboxylic acid production is observed. Increasing the inoculum density solves the substrate inhibition. Using a fed-batch strategy, 545 mM of 2,5-furandicarboxylic acid can be accumulatively produced after 72 h
synthesis
HMFO is used to convert 5-hydroxymethylfurfural to 2,5-diformylfuran and 5-formylfuroic acid (FFA), which is consecutively transformed to 2,5-furandicarboxylic acid by lipase Novozym 435. To facilitate the purification, a coupled alkali precipitation was developed to recover 2,5-furandicarboxylic acid from organic solvent with an improved purity from 84.4 to 99.0% and recovery of 78.1%
synthesis
one-pot synthetic pathway to yield 2,5-furandicarboxylic acid from furfural. An oxidase and a prenylated flavin mononucleotide-dependent reversible decarboxylase, catalyze furfural oxidation and carboxylation of 2-furoic acid, respectively. The reversible decarboxylase is identified in Paraburkholderia fungorum KK1, whereas hydroxymethylfurfural oxidase from Methylovorus sp. MP688 exhibits furfural oxidation activity
synthesis
oxidative kinetic resolution of racemic sec-thiols by enzyme variants, yielding the corresponding thioketones and nonreacted R-configured thiols with excellent enantioselectivities (E+200)
synthesis
production of 2,5-furandicarboxylic acid by biotransformation of 5-hydroxymethylfurfural. Genes encoding 5-hydroxymethylfurfural oxidase and 5-hydroxymethylfurfural/furfural oxidoreductase from Cupriavidus basilensis HMF14 are introduced into Raoultella ornithinolytica BF60. The 2,5-furandicarboxylic acid production in the engineered whole-cell biocatalyst increases from 51.0 to 93.6 mM, and the molar conversion ratio of 5-hydroxymethylfurfural to 2,5-furandicarboxylic acid increases from 51.0 to 93.6%
synthesis
synthetic pathway to yield 2,5-furandicarboxylic acid from furfural, produced from lignocellulosic biomass. The pathway consists of an oxidase and a prenylated flavin mononucleotide (prFMN)-dependent reversible decarboxylase, catalyzing furfural oxidation and carboxylation of 2-furoic acid, respectively. Upon coexpression in Escherichia coli, as well as a flavin prenyltransferase, 2,5-furandicarboxylic acid can be produced from furfural via 2-furoic acid in one pot
synthesis
the combination of alcohol oxidase and catalase is most effective in converting over 97% 5-hydroxymethylfurfural to 2,5-diformylfuran in 72 h
synthesis
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utilization of whole-cell Paraburkholderia azotifigens F18 for selective reduction of 5-hydroxymethylfurfural to 2,5-bis(hydroxymethyl)furan (BHMF) or oxidation to 5-hydroxymethyl-2-furancarboxylic acid (HMFCA). The whole-cell system can proceed an efficient hydrogenation reaction toward 5-hydroxymethylfurfural with a good selectivity of 97.6% to yield the BHMF at 92.2%. BHMF can be further oxidized to HMFCA and 2,5-furandicarboxylic acid (FDCA). The genes encoding HMF oxidoreductase/oxidase of whole-cell F18 are then deleted to prevent the further conversion of HMFCA to FDCA, which leads to a 10-fold decrease of FDCA. An 5-hydroxymethylfurfural conversion of 100% with an HMFCA yield of 98.3% is finally achieved, with an selectivity of 96.3% and a yield of 85.1% even at a high substrate concentration of up to 200 mM
synthesis
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utilization of whole-cell Paraburkholderia azotifigens F18 for selective reduction of 5-hydroxymethylfurfural to 2,5-bis(hydroxymethyl)furan (BHMF) or oxidation to 5-hydroxymethyl-2-furancarboxylic acid (HMFCA). The whole-cell system can proceed an efficient hydrogenation reaction toward 5-hydroxymethylfurfural with a good selectivity of 97.6% to yield the BHMF at 92.2%. BHMF can be further oxidized to HMFCA and 2,5-furandicarboxylic acid (FDCA). The genes encoding HMF oxidoreductase/oxidase of whole-cell F18 are then deleted to prevent the further conversion of HMFCA to FDCA, which leads to a 10-fold decrease of FDCA. An 5-hydroxymethylfurfural conversion of 100% with an HMFCA yield of 98.3% is finally achieved, with an selectivity of 96.3% and a yield of 85.1% even at a high substrate concentration of up to 200 mM
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synthesis
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the combination of alcohol oxidase and catalase is most effective in converting over 97% 5-hydroxymethylfurfural to 2,5-diformylfuran in 72 h
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