EC Number   |
Application |
Reference |
|---|
   1.1.3.7 | environmental protection |
the enzyme in white-rot fungi is useful in degradation of aromatic hydrocarbons in a historically contaminated soil |
672700 |
| 1.1.3.7 | more |
a two-enzyme system comprising a dye decolorizing peroxidase (DyP, EC 1.11.1.19) from Mycetinis scorodonius and the Pleurotus sapidus AAO enzyme is successfully employed to bleach the anthraquinone dye Reactive Blue 5. The aryl-alcohol oxidase provides the required H2O2 |
-, 741721 |
| 1.1.3.7 | 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 |
| 1.1.3.7 | 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 |
| 1.1.3.7 | synthesis |
construction of fusion proteins with Saccharomyces cerevisiae unspecific peroxidase, EC 1.11.2.1, using different peptide linkers. The reaction system is optimized to control the aromatic alcohol transformation rate, and therefore the H2O2 supply, to achieve total turnover numbers of 62000 for the biocatalytic synthesis of dextrorphan, a metabolite of the antitussive drug dextromethorphan |
762528 |
| 1.1.3.7 | synthesis |
due to hydride-transfer stereoselectivity and specificity on substituted aldehydes, the enzyme is useful for flavor production and in production of chiral compounds. Flavor synthesis and enzyme stereoselectivity, overview |
724064 |
| 1.1.3.7 | 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 |
| 1.1.3.7 | synthesis |
expression and secretion of AAO with yield of 315 mg/l using Pichia pastoris |
762662 |
| 1.1.3.7 | synthesis |
expression variant carrying 4 mutations in the chimeric signal peptide (prealphaproK), plus mutations H91N/L170M in the mature protein, shows 350fold improved secretion (4.5 mg/l) in Saccharomyces cerevisiae and is stable. Expression in Pichia pastoris and fermentation in a fed-batch bioreactor enhances production to 25 mg/l. Both recombinant AAO from Saccharomyces cerevisiae and Pichia pastoris are subjected to the same N-terminal processing and have a similar pH activity profile, they differ in their kinetic parameters and thermostability |
762839 |
| 1.1.3.7 | synthesis |
high-yield production of AAO in submerged culture using a recombinant Aspergillus nidulans strain grown on corn steep liquor. The optimum medium component concentrations are 61.0 g/l maltose, 26.4 g/L corn steep liquor, and 13.8 g/l NaNO3. The greatest AAO activity achieved is 1021 U/l with a protein concentration of 0.75 g/l |
-, 762812 |
