| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 69895 | Journal of Molecular Catalysis B: Enzymatic | 2012 | 6 Pages |
In situ coupling of aldehyde generation, by a mild alcohol oxidation, with an enzymatic aldol addition reaction, mediated by d-fructose-6-phosphate aldolase (FSA) has been investigated as an approach to improve the performance of the process. Four sustainable oxidation methods compatible with the activity and stability of the enzymatic aldol addition have been assayed. Among them, the laccase/O2/2,2,6,6-tetramethylpiperidine-N-oxyl (TEMPO) and alcohol oxidase gave the best results for the N-Cbz-aminoethanol to N-Cbz-glycinal (53%) and furfuryl alcohol to furfural (89%), respectively, followed by the aldol addition with hydroxyacetone catalyzed by FSA A129S mutant.
Graphical abstractFigure optionsDownload full-size imageDownload as PowerPoint slideHighlights► Enzymatic cascade of alcohol to aldehyde oxidation and asymmetric aldol addition. ► Biocatalytic synthesis of high added value polyhydroxylated iminocyclitols. ► Oxidation of furfuryl alcohol to furfural and aldol addition of HA catalyzed by FSA. ► N-Cbz-aminoethanol to N-Cbz-glycinal and aldol addition of HA catalyzed by FSA.
