EC Number   |
Application |
Reference |
|---|
    1.14.14.9 | synthesis |
enzyme completely transforms 4-substituted halophenols to 4-halocatechols at 2 mM within a 1-2 h period. An increase in 4-halophenol concentration to 4.8 mM results in a 2.5-20fold decrease in biotransformation efficiency depending on the substrate tested. Organic solvent extraction of the 4-halocatechol products followed by column chromatography results in the production of purified products with a final yield of between 33% and 38% |
713895 |
| 1.14.14.9 | synthesis |
enzyme shows relatively broad substrate specificity, which allows the conversion of a number of non-natural phenolic compounds, into the corresponding catechols. The reaction can be performed based on formate as the electron donor and the organometallic complex [Rh(bpy)-Cp*(H2O)]2+ (Cp*: 1,2,3,4,5-pentamethylcyclopentadiene, bpy: 2,2'-bipyridyl) as the catalyst for FAD reduction |
764477 |
| 1.14.14.9 | synthesis |
in vivo production of ortho-hydroxylated flavonoids by recombinant Escherichia coli. When HpaC is linked with an S-Tag on the C terminus, the enzyme activity is significantly affected. The optimal culture conditions are a substrate concentration of 80 mg/l, an induction temperature of 28°C, an M9 medium, and a substrate delay time of 6 h after IPTG induction. The efficiency of eriodictyol conversion from recombinant strains fed naringin is up to 57.67. Highest conversion efficiencies for production of catechin and caffeate are 35.2 % and 32.93%, respectively |
-, 765429 |
| 1.14.14.9 | synthesis |
investigation of a flask-scale production of caffeic acid from p-coumaric acid as the model reaction for HpaBC-catalyzed synthesis of hydroxycinnamic acids. Since the initial concentrations of the substrate p-coumaric acid higher than 40 mM markedly inhibits its 4-hydroxyphenylacetate 3-hydroxylases-catalyzed oxidation, the reaction is carried out by repeatedly adding 20 mM of this substrate to the reaction mixture. Furthermore, by using the whole-cell catalyst in the presence of glycerol, the experimental setup achieves the high-yield production of caffeic acid, i.e., 56.6 mM (10.2 g/l) within 24 h. These catalytic activities of 4-hydroxyphenylacetate 3-hydroxylases will provide an easy and environment-friendly synthetic approach to hydroxycinnamic acids |
744140 |
| 1.14.14.9 | synthesis |
overexpression of the HpaB and HpaC genes in Saccharomyces cerevisiae achieves hydroxytyrosol titers of 1.15 mg/l and 4.6 mg/l in a minimal medium in which either 1 mM tyrosine or 1 mM tyrosol are respectively added |
-, 764691 |
