EC Number   |
Application |
Reference |
|---|
   1.14.14.11 | synthesis |
construcution of fusion proteins that join the C-terminus of the epoxidase StyA to the N-terminus of FAD reductase StyB through a linker peptide and application in the synthesis of of a broad range of substituted indoles to indigoid chromophores. The fusion proteins are self-regulated and couple efficiently NADH oxidation to styrene epoxidation |
744072 |
| 1.14.14.11 | synthesis |
development of a highly diastereo- and enantio-selective enzymatic synthesis of glycidol derivatives with contiguous stereogenic centers |
714725 |
| 1.14.14.11 | synthesis |
engineering of a stable whole-cell biocatalyst capable of (S)-2-phenyloxirane formation for continuous two-liquid-phase applications |
-, 713817 |
| 1.14.14.11 | synthesis |
in an organic solvent-water biphasic reaction system, recombinant enzyme enantioselectively converts linear terminal alkenes to their corresponding (S)-epoxyalkanes using glucose and molecular oxygen. When 1-heptene and 6-chloro-1-hexene are used as substrates (400 mM) under optimized conditions, 88.3mM (S)-1,2-epoxyheptane and 246.5mM (S)-1,2-epoxy-6-chlorohexane, respectively, accumulate in the organic phase with good enantiomeric excess (84.2% and 95.5%, respectively) |
744099 |
| 1.14.14.11 | synthesis |
overexpression of StyA and StyB significantly enhances the indigo production, reaching 52.13 mg/L after 24 h. Overexpression of oxide isomerase gene styC does not increase indigo yield |
744756 |
| 1.14.14.11 | synthesis |
production of enantiopure styrene oxide by recombinant Escherichia coli. Two-liquid phase fed-batch process is established for the production of (S)-styrene oxide with hexadecane as an apolar carrier solvent and a nutrient feed consisting of glucose, magnesium sulfate, and yeast extract. Production of 11 g of enantiopure (S)-styrene oxide per liter liquid volume in 10 h |
-, 714556 |
| 1.14.14.11 | synthesis |
production of optically pure (S)-styrene oxide, an important building block in organic synthesis. Recombinant Escherichia coli producing styrene monooxygenase catalyzes the formation of (S)-2-phenyloxirane from inexpensive styrene with an excellent enantiomeric excess of more than 99% at rates up to 180 U/g (dry weight) of cells |
-, 713814 |
| 1.14.14.11 | synthesis |
synthesis of (S)-styrene oxide. Investigation of factors influencing biocatalytic efficiency of oxygenase-based whole-cell biocatalysts under process conditions |
-, 714558 |
| 1.14.14.11 | synthesis |
synthesis of various chiral aryloxides, pilot-scale production of (S)-2-phenyloxirane |
-, 714557 |
| 1.14.14.11 | synthesis |
the enzyme converts aryl ethenyl compounds to the corresponding epoxides in optically pure forms and with good yields |
-, 713815 |
