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Development of a New Bioprocess for Production of 1,3-propanediol I.: Modeling of Glycerol Bioconversion to 1,3-propanediol with Klebsiella pneumoniae Enzymes

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Abstract

Glycerol is a renewable resource for it is formed as a byproduct during biodiesel production. Because of its large volume production, it seems to be a good idea to develop a technology that converts this waste into products of high value, for example, to 1,3-propanediol (1,3-PD). We suggested an enzymatic bioconversion in a membrane reactor in which the NAD coenzyme can be regenerated, and three key enzymes are retained by a 10-kDa ultrafilter membrane. Unfortunately, some byproducts also formed during successful glycerol to 1,3-PD bioconversion runs, as we used crude enzyme solution of Klebsiella pneumoniae. To study the possibilities to avoid this byproduct formation, we built a mathematical description of this system. The model was also used for simulation bioconversions of high glycerol concentration with and without elimination of byproduct formation and of continuous operation.

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Abbreviations

1,3-PD:

1,3-propanediol

DHA:

1,3-dihydroxyacetone

GDH:

glycerol dehydrogenase enzyme

GDHt:

glycerol dehydratase enzyme

PDOR:

1,3-propanediol oxydoreductase

DHAK:

dihydroxyacetone kinase

TPI:

triose-phosphate isomerase

GAPD:

glyceraldehyde-3-phosphate dehydrogenase

PGK:

phosphoglycerate kinase

PGM:

phosphoglycerate mutase

PPH:

phosphopyruvate hydratase

PK:

pyruvate kinase

PS:

pyruvate synthase

PAT:

phosphate acetyltransferase

PTA:

phospholipid-translocating ATPase

LDH:

lactate-dehydrogenase

LMO:

lactate 2-monooxygenase

BB:

“black-box”

Clha:

chloro-3-hydroxyacetone

References

  1. Dunn-Coleman, N. S., Gatenby, A. A., Valle, F. (1998). Methods for the production of 1,3-propanediol by recombinant organisms. World Patent WO9821339.

  2. Németh, Á., Kupcsulik, B., & Sevella, B. (2003). 1,3-Propanediol oxidoreductase production with Klebsiella pneumoniae DSM2026. World Journal of Microbiology and Biotechnology, 19(7), 659–663.

    Article  Google Scholar 

  3. Johnson, E. A., & Lin, C. C. (1987). Klebsiella pneumoniae 1,3-Propanediol:NAD+ Oxidoreductase. Journal of Bacteriology, 169(5), 2050–2054.

    CAS  Google Scholar 

  4. Toraya, T., Ushio, K., Fukui, S., & Hogenkamp, P. C. (1977). Studies on the mechanism of the adenosylcobalamin-dependent diol dehydrase reaction by the use of analogs of coenzyme. Journal of Biological Chemistry, 252(3), 963–970.

    CAS  Google Scholar 

  5. Biebl, H., Menzel, K., Zeng, A. P., & Deckwer, W. D. (1999). Microbial production of 1,3-propanediol. Applied Microbiology and Biotechnology, 52(3), 289–297.

    Article  CAS  Google Scholar 

  6. Mori, K., Tobimatsu, T., Hara, T., & Toraya, T. (1997). Characterization, sequencing, and expression of the genes encoding a reactivating factor for glycerol-inactivated adenosylcobalamin-dependent diol dehydratase. Journal of Biological Chemistry 272(51), 32034–32041.

    Article  CAS  Google Scholar 

  7. McGregor, W. J., Phillips, J., Suelter, C. H. (1974). Purification and kinetic characterization of a monovalent cation-activated glycerol dehydrogenase from Aerobacter aerogenes. Journal of Biological Chemistry, 249(10), 3132–3139.

    CAS  Google Scholar 

  8. Garcia-Alles, L. F., Siebold, C., Nyffeler, T. L., Flukiger-Bruhwiler, K., Schneider, P., Burgi, H. B., et al. (2004). Phosphoenolpyruvate and ATP-dependent dihydroxyacetone kinases: Covalent substrate-binding and kinetic mechanism. Biochemistry, 43, 13037–13045.

    Article  CAS  Google Scholar 

  9. Yamanishi, M., Yunoki, M., Tobimatsu, T., Sato, H., Matsui, J., Dokiya, A., et al. (2002). The crystal structure of coenzyme B12-dependent glycerol dehydratase in complex with cobalamin and propane-1,2-diol. European Journal of Biochemistry, 269(18), 4484–4494.

    Article  CAS  Google Scholar 

  10. Johnson, E. A., Burke, S. K., Forage, R. G., & Lin, E. C. (1984). Purification and properties of dihydroxyacetone kinase from Klebsiella pneumoniae. Journal of Bacteriology, 160(1), 55–60.

    CAS  Google Scholar 

  11. Cornish Bowden, A. (2004). Fundamentals of Enzyme Kinetics, 3rd edn. London, UK: Portland.

    Google Scholar 

  12. Berglund, O., & Eckstein, F. (1972). ATP and dATP-substituted agaroses and the purification of ribonucleotide reductase. Journal of Biological Chemistry, 224(7276), 253–261.

    Google Scholar 

  13. Bückmann, A. F. (1981). An efficient synthesis of High-Molecular-Weight NAD(H) derivatives suitable for continuous operation with coenzyme-dependent enzyme systems. Journal of Applied Biochemistry, 3, 301–315.

    Google Scholar 

  14. Obon, J. M., Manjon, A., & Iborra, J. L. (1998). Retention and regeneration of native NAD(H) in noncharged ultrafiltration membrane reactors: application to l-lactate and gluconate production. Biotechnology and Bioengineering, 57(5), 510–517.

    Article  CAS  Google Scholar 

  15. Reynaud, C., Sarçabal, P., Meynial-Salles, I., Croux, C., & Soucaille, P. (2003). Molecular characterization of the 1,3-propanediol (1,3-PD) operon of Clostridium butyricum. Applied Biological Sciences, 100(9), 5010–5015.

    Google Scholar 

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Acknowledgment

We are thankful to OTKA T032015 and NKFP-3/A/0035/2002 for the financial support of our work.

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Correspondence to Béla Sevella.

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Németh, Á., Sevella, B. Development of a New Bioprocess for Production of 1,3-propanediol I.: Modeling of Glycerol Bioconversion to 1,3-propanediol with Klebsiella pneumoniae Enzymes. Appl Biochem Biotechnol 144, 47–58 (2008). https://doi.org/10.1007/s12010-007-0040-5

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