2 research outputs found

    Biosynthesis of L‑Erythrose by Assembly of Two Key Enzymes in <i>Gluconobacter oxydans</i>

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    L-erythrose, a rare aldotetrose, possesses various pharmacological activities. However, efficient L-erythrose production is challenging. Currently, L-erythrose is produced by a two-step fermentation process from erythritol. Here, we describe a novel strategy for the production of L-erythrose in <i>Gluconobacter oxydans</i> (<i>G. oxydans</i>) by localizing the assembly of L-ribose isomerase (L-RI) to membrane-bound sorbitol dehydrogenase (SDH) via the protein–peptide interactions of the PDZ domain and PDZ ligand. To demonstrate this self-assembly, green fluorescent protein (GFP) replaced L-RI and its movement to membrane-bound SDH was observed by fluorescence microscopy. The final L-erythrose production was improved to 23.5 g/L with the stepwise metabolic engineering of <i>G. oxydans</i>, which was 1.4-fold higher than that obtained using coexpression of SDH and L-RI in <i>G. oxydans</i>. This self-assembly strategy shows remarkable potential for further improvement of L-erythrose production
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