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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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.
Keywords1,3-Propanediol Klebsiella pneumoniae Enzymatic bioconversion Modelling
glycerol dehydrogenase enzyme
glycerol dehydratase enzyme
We are thankful to OTKA T032015 and NKFP-3/A/0035/2002 for the financial support of our work.
- 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.Google Scholar
- 3.Johnson, E. A., & Lin, C. C. (1987). Klebsiella pneumoniae 1,3-Propanediol:NAD+ Oxidoreductase. Journal of Bacteriology, 169(5), 2050–2054.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.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.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.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
- 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