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Title: Efficient production of L-ribose with a recombinant Escherichia coli

Author
item WOODYER, RYAN - ZUCHEM
item RACINE, MICHAEL - ZUCHEM
item DEMIRJIAN, DAVID - ZUCHEM
item Saha, Badal

Submitted to: American Chemical Society Abstracts
Publication Type: Abstract Only
Publication Acceptance Date: 8/21/2008
Publication Date: 8/21/2008
Citation: Woodyer, R., Racine, M., Demirjian, D.C., Saha, B.C. 2008. Efficient production of L-ribose with a recombinant Escherichia coli [abstract]. American Chemical Society. Paper No. BIOT 297.

Interpretive Summary:

Technical Abstract: A new synthetic platform with potential for the production of several rare sugars, with L-ribose being the model target, is described. The gene encoding the unique NAD-dependent mannitol-1-dehydrogenase (MDH) from Apium graveolens (garden celery) was synthetically constructed for optimal expression in Escherichia coli. This MDH enzyme catalyzes the interconversion of several polyols with their L-sugar counterparts including ribitol to L-ribose. Recombinant MDH expression was successfully achieved in active form, and one-step purification was demonstrated. Using the created recombinant E. coli strain as a whole cell catalyst, the synthetic utility was demonstrated for production of L-ribose, and this system was improved using shaken flask experiments. The final achieved conversions were >70% at a concentration of 40 g/L and >50% at a concentration of 100 g/L. The best conditions determined were then scaled up to a 1 L fermentation that resulted in a 55% conversion of 100 g/L ribitol in 72 hours for a volumetric productivity of 17.4 gL-1d-1. While this system already represents a significantly improved method for the large scale production of L-ribose, directed evolution has shown promise for further improvement. Production of other L-sugars using this same system has been demonstrated.