Production of d-ribose by fermentation

  title={Production of d-ribose by fermentation},
  author={Peter De Wulf and Erick J Vandamme},
  journal={Applied Microbiology and Biotechnology},
The production of d-ribose by fermentation has received much attention lately, possibly because of the use of this pentose to synthesize antiviral and anticancer drugs. This review briefly outlines the methods that have been used to synthesize d-ribose since it was identified in yeast RNA, and focuses in particular on the latest developments in d-ribose fermentation, which have led to d-ribose yields that exceed 90 g/l. Furthermore, the various transketolase-deficient d-ribose-producing mutants… 

Engineering Escherichia coli for D-Ribose Production from Glucose-Xylose Mixtures

This study represents the first example of engineered E. coli for production of D-ribose from glucose and xylose, and demonstrates reengineering of a glucose-xylose co-utilizing mutant co- utilizing mutant LMSE2.

Production of natural and rare pentoses using microorganisms and their enzymes

L-ribose and L-arabinose were prepared biochemically from ribitol by oxidation using Acetobacter aceti IFO 3281 and isomerization using L-RI and L -arabinoses isomerase (L-AI), respectively.

Improvement of D-Ribose Production from Corn Starch Hydrolysate by a Transketolase-Deficient Strain Bacillus subtilis UJS0717

Findings indicated the D-ribose production performance was significantly improved compared to that under original conditions.

Fed-batch production of d-ribose from sugar mixtures by transketolase-deficient Bacillus subtilis SPK1

Optimized fed-batch fermentation of B. subtilis SPK1, feeding a mixture of 200 g l−1 xylose and 50 g-l-1 glucose after the late-exponential phase reduced the residual xylOSE and glucose concentrations to less than 7.0 g–1d-ribose and gave the best results, which were 2.0- and 1.2-fold higher than the corresponding values in a simple batch fermentation.

Optimization of medium components for D-ribose production by transketolase-deficient Bacillus subtilis NJT-1507

Statistical experimental designs were used to optimize the composition of culture media for the production of D-ribose by Bacillus subtilis. A fractional factorial design 2(5-2) was used to determine

Enhanced d-ribose biosynthesis in batch culture of a transketolase-deficient Bacillus subtilis strain by citrate

Investigation of batch culture of a transketolase-deficient strain of Bacillus subtilis EC2 indicated that citrate addition resulted in increased fluxes in the pentose phosphate pathway and TCA cycle, and decreased fluxe in the glycolysis and acetate pathways.

Combined effects of carbon, nitrogen and phosphorus substrates on D‐ribose production via transketolase deficient strain of Bacillus pumilus

The relative rates of PPP and in turn the D-ribose yield were dependent on not only the carbon substrate concentration but also the nitrogen and phosphorus substrates.



d-Ribose Formation by Pseudomonas reptilivora

It was found that ribose was formed not only from glucose but also from d-fructose, d-arabitol, gluconic acid, etc., and that d- fructose and a glucoside were also accumulated at the same time in the culture broth of Pseudomonas reptilivora S-1104.

Carbohydrate Metabolism-Mutants of a Bacillus Species: Part II. d-Ribose Accumulation by Pentose Phosphate Pathway Mutants

During the course of studies on the effects of mutation in carbohydrate metabolism on the synthesis of purine derivatives, it was found that three mutants of a Bacillus species, which lacked


In the fermentation broth of an unidentified bacterium using a medium containing glucose, yeast extract, urea and minerals, a significant accumulation of R-5-P or ribose was observed.

Production of d-ribose

PURPOSE: To remarkably stably produce a large quantity of D-ribose by modifying a D-ribose-producing bacterium so as to enable high-manifestation of the DNA sequence contributing to manifestation of

d-Sedoheptulose-7-phosphate: d-Glyceraldehyde-3-phosphate Glycolaldehydetransferase and d-Ribulose-5-phosphate 3-Epimerase Mutants of a Bacillus Species

Determination of enzyme activities on the non-oxidative section of the pentose phosphate pathway in d-ribose-forming mutants of a Bacillus species revealed that two strains, which were isolated as

Reactivation of Inactivated d-Glucose Dehydrogenase of a Bacillus Species by Pyridine and Adenine Nucleotides

d-Glucose dehydrogenase was synthesized derepressively in a mutant of a Bacillus species which was isolated as an improved strain for d-ribose production and it seems that the enzyme activity is regulated by monomer-dimer interconversion of the enzyme molecule.

Change in the regulation of enzyme synthesis under catabolite repression in Bacillus subtilis pleiotropic mutant lacking transketolase.

Changes in the regulation of enzyme synthesis in Bacillus subtilis pleiotropic mutant lacking transketolase seem to be related to some defect in the cell surface structure of the tkt mutant by which other pleiotropy properties are also generated.


Abstract A new stereoselective synthesis of D -ribose ( 14 ) starting from L -glutamic acid ( 1 ) is described, by making use of the chiral center of 1 as that at C-4 of 14 . Oxidation of methyl

Ribose intervention in the cardiac pentose phosphate pathway is not species-specific.

The activity of glucose-6-phosphate dehydrogenase, the first and rate-limiting enzyme of the oxidative pentose phosphate shunt, was very low in the human heart and was of the same order of magnitude in the myocardium of various animal species.

Control of development: role of regulatory nucleotides synthesized by membranes of Bacillus subtilis in initiation of sporulation.

  • H. RhaeseR. Groscurth
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1976
It is concluded that the plasma membrane synthesizes unusual nucleotides in response to nutrient deficiencies by several as yet unknown steps, which then cuase changes in the metabolism of the organism leading to the formation of spores.