Two-component flavoprotein monooxygenases consist of a reductase and an oxygenase enzyme. The proof of functionality of the latter without its counterpart as well as the mechanism of flavin transfer remains...
Pickering emulsions (PEs) are particle-stabilized multiphase systems with promising features for synthetic applications.D escribed here is an ovel, simplified set-up employing catalytically active whole cells for simultaneous emulsion stabilization and synthetic reaction. In the stereoselective carboligation of benzaldehyde to (R)-benzoin catalyzed by abenzaldehyde lyase in E. coli, the set-up yielded maximum substrate conversion within very short time,while economizing material demand and waste.F ormation and activity of freshly produced PEs were enhanced when the catalytic whole cells were covered with hydrophobic silicone prior to PE formation. Benchmarked against other easy-to-handle whole-cell biocatalysts in pure organic solvent, neat substrate,a na queous emulsion in substrate,and amicro-aquatic system, respectively, the cell-stabilized PE outperformed all other systems by far.
With the aim of applying redox‐neutral cascade reactions in organic media, fusions of a type II flavin‐containing monooxygenase (FMO‐E) and horse liver alcohol dehydrogenase (HLADH) were designed. The enzyme orientation and expression vector were found to influence the overall fusion enzyme activity. The resulting bifunctional enzyme retained the catalytic properties of both individual enzymes. The lyophilized cell‐free extract containing the bifunctional enzyme was applied for the convergent cascade reaction consisting of cyclobutanone and butane‐1,4‐diol in different microaqueous media with only 5 % (v/v) aqueous buffer without any addition of external cofactor. Methyl tert‐butyl ether and cyclopentyl methyl ether were found to be the best organic media for the synthesis of γ‐butyrolactone, resulting in about 27 % analytical yield.
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