Evidence map›Paper›PMID 18344327›Full record

ArticleApplied and environmental microbiology2008

Efficient production of L-ribose with a recombinant Escherichia coli biocatalyst.

Ryan D Woodyer, Nathan J Wymer, F Michael Racine, Shama N Khan, Badal C Saha

Abstract read
In one paragraph

Article in Applied and environmental microbiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

9 citing papers in PubMed, 41 citations in OpenAlex.

  1. Microbial and enzymatic strategies for the production of L-ribose.Applied microbiology and biotechnology · 2020
    Review
  2. Article
  3. Review
  4. Enzymes for the biocatalytic production of rare sugars.Journal of industrial microbiology & biotechnology · 2012
    Review
  5. Article
  6. Engineering microbial factories for synthesis of value-added products.Journal of industrial microbiology & biotechnology · 2011
    Review
  7. Article
  8. Article
  9. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Ryan D WoodyerzuChem, Inc., 2225 W. Harrison, Suite F, Chicago, Illinois 60612, USA. rwoodyer@zuchem.com
Nathan J Wymer
F Michael Racine
Shama N Khan
Badal C Saha
zuChem (United States) · USAgricultural Research Service · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A new synthetic platform with potential for the production of several rare sugars, with l-ribose as 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 and their l-sugar counterparts, including the conversion of ribitol to l-ribose. Expression of recombinant MDH in the active form was successfully achieved, 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 the system was improved using shaken flask experiments. It was determined that addition of 50 to 500 microM ZnCl(2) and addition of 5 g/liter glycerol both improved production. The final levels of conversion achieved were >70% at a concentration of 40 g/liter and >50% at a concentration of 100 g/liter. The best conditions determined were then scaled up to a 1-liter fermentation that resulted in 55% conversion of 100 g/liter ribitol in 72 h, for a volumetric productivity of 17.4 g liter(-1) day(-1). This system represents a significantly improved method for the large-scale production of l-ribose.

Indexed as

ApiumChloridesCloning, MolecularCoenzymesEscherichia coliGene ExpressionGlycerolPolymersRecombinant ProteinsRibitolRiboseSugar Alcohol DehydrogenasesZinc CompoundsChloridesCoenzymesGlycerolmannitol-mannose 1-oxidoreductasePolymerspolyolRecombinant ProteinsRibitolRiboseSugar Alcohol Dehydrogenaseszinc chlorideZinc Compounds

Identifiers

PMID18344327
PMCPMC2394927
OpenAlexW2143616964

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.