4.2 Article

Allitol bioproduction by recombinant Escherichia coli with NADH regeneration system co-expressing ribitol dehydrogenase (RDH) and formate dehydrogenase (FDH) in individual or in fusion

Journal

ELECTRONIC JOURNAL OF BIOTECHNOLOGY
Volume 55, Issue -, Pages 91-98

Publisher

UNIV CATOLICA DE VALPARAISO
DOI: 10.1016/j.ejbt.2021.11.007

Keywords

Allitol; Bioproduction; Co-expression; Cofactor recycle; D -Allulose; Formate dehydrogenase; Fusion expression; NADH regeneration system; Recombinant Escherichia coli; Ribitol dehydrogenase; Sugar alcohol

Funding

  1. National Key Research and Development Program of China [2017YFC1701502, 2017YFC1701504, 2017YFC1702701]
  2. Taishan Scholar Project [ts201511107]
  3. Major increase and decrease projects of Central Government [2060302]
  4. Jinan Agricultural Application Technology Innovation Plan [CX202112]
  5. Ecological Planting and Quality Assurance Project of Genuine Medicinal Materials
  6. China Postdoctoral Science Foundation [2021M701994]

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In this study, two recombinant Escherichia coli strains were constructed to produce allitol through individual expression strain, and achieved a high yield of allitol, which was the highest reported productivity.
Background: As a kind of rare sugar alcohol, allitol has important application values in food and medication. In addition, it can be used as a key substrate to produce other D/L-rare sugars. Allitol can be effectively produced by the resting-cell biotransformation method. Results: Two recombinant Escherichia coli strains, one simultaneously expressing ribitol dehydrogenase (RDH) and formate dehydrogenase (FDH) in fusion (fusion expression strain for short) and the other expressing the above two enzymes individually (individual expression strain for short), were respectively constructed and used for allitol bioproduction. The produced allitol was confirmed by HPLC, mass spectrometry, and polarimetry. The individual expression strain had higher activity, which produced 58.5 g/L allitol from 90 g/L D-allulose (also named D-psicose) in 1 h with an allitol productivity of 58.5 g/L/h under optimized conditions. Conclusions: The constructed individual expression strain had the highest allitol productivity among the reports. The production process developed in this study was simple, highly efficient, and had the potential for mass production of allitol. How to cite: Wen X, Lin H, Ren Y, et al. Allitol bioproduction by recombinant Escherichia coli with NADH regeneration system co-expressing Ribitol Dehydrogenase (RDH) and Formate Dehydrogenase (FDH) in individual or in fusion. Electron J Biotechnol 2022;55. https://doi.org/10.1016/j.ejbt.2021.11.007 (c) 2021 Pontificia Universidad Catolica de Valparaiso. Production and hosting by Elsevier B.V. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/).

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