EC Number   |
Application |
Reference |
|---|
   1.1.3.47 | biofuel production |
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 |
-, 742155 |
| 1.1.3.47 | 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 |
762843 |
| 1.1.3.47 | 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 |
762844 |
| 1.1.3.47 | synthesis |
biocatalytic production of furan-2,5-dicarboxylate, a biobased platform chemical for the production of polymers |
728965 |
| 1.1.3.47 | 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 |
763751 |
| 1.1.3.47 | 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 |
762588 |
| 1.1.3.47 | 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 |
763437 |
| 1.1.3.47 | 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% |
762622 |
| 1.1.3.47 | 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 |
763286 |
| 1.1.3.47 | 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) |
762602 |
