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Volumn 143, Issue 3, 2009, Pages 213-223

Effect of CO2 on succinate production in dual-phase Escherichia coli fermentations

Author keywords

13C labeling; Metabolic flux analysis; PEP carboxylase; Succinic acid

Indexed keywords

13C-LABELING; AEROBIC CELLS; CARBON FLUXES; COFACTORS; CONCENTRATION OF; EFFECT OF CO; ELEVATED CO; EXPLICIT MODELS; GASPHASE; GROWTH PHASE; LACTATE DEHYDROGENASE; METABOLIC FLUX ANALYSIS; PENTOSE PHOSPHATE PATHWAY; PEP CARBOXYLASE; PHOSPHOENOLPYRUVATES; PHOSPHOTRANSFERASE SYSTEM; PYRUVATE FORMATE LYASE; SPECIFIC PRODUCTIVITY; SUCCINATE PRODUCTION; SUCCINIC ACID;

EID: 69049084383     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2009.07.012     Document Type: Article
Times cited : (60)

References (36)
  • 1
    • 0036968064 scopus 로고    scopus 로고
    • Microbial enzymes involved in carbon dioxide fixation
    • Atom H. Microbial enzymes involved in carbon dioxide fixation. J. Biosci. Bioeng. 94 (2002) 497-505
    • (2002) J. Biosci. Bioeng. , vol.94 , pp. 497-505
    • Atom, H.1
  • 2
    • 0004232671 scopus 로고
    • Diffusion: macroscopic theory
    • Princeton University Press, Princeton, New Jersey
    • Berg H.C. Diffusion: macroscopic theory. Random Walks in Biology (1983), Princeton University Press, Princeton, New Jersey
    • (1983) Random Walks in Biology
    • Berg, H.C.1
  • 3
    • 0011666083 scopus 로고    scopus 로고
    • Uptake of carbon dioxide from flue gas by microalgae
    • Brown L. Uptake of carbon dioxide from flue gas by microalgae. Energy Convers. Manage. 37 (1996) 1363-1367
    • (1996) Energy Convers. Manage. , vol.37 , pp. 1363-1367
    • Brown, L.1
  • 4
    • 84907682314 scopus 로고
    • The solubility of carbon dioxide in water at low pressure
    • Carroll J., Slupsky J., and Mather A. The solubility of carbon dioxide in water at low pressure. J. Phys. Chem. Ref. Data 20 (1991) 1201-1209
    • (1991) J. Phys. Chem. Ref. Data , vol.20 , pp. 1201-1209
    • Carroll, J.1    Slupsky, J.2    Mather, A.3
  • 5
    • 0035158424 scopus 로고    scopus 로고
    • Mutation of the ptsG gene results in increased production of succinate in fermentation of glucose by Escherichia coli
    • Chatterjee R., Millard C.S., Champion K., Clark D.P., and Donnelly M.I. Mutation of the ptsG gene results in increased production of succinate in fermentation of glucose by Escherichia coli. Appl. Environ. Microbiol. 67 (2001) 148-154
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 148-154
    • Chatterjee, R.1    Millard, C.S.2    Champion, K.3    Clark, D.P.4    Donnelly, M.I.5
  • 6
    • 0024723183 scopus 로고
    • The fermentation pathways of Escherichia coli
    • Clark D.P. The fermentation pathways of Escherichia coli. FEMS Microbiol. Rev. 63 (1989) 223-234
    • (1989) FEMS Microbiol. Rev. , vol.63 , pp. 223-234
    • Clark, D.P.1
  • 7
    • 0031856455 scopus 로고    scopus 로고
    • A novel fermentation pathway in an Escherichia coli mutant producing succinic acid, acetic acid, and ethanol
    • Donnelly M.I., Millard C.S., Clark D.P., Chen M.J., and Rathke J.W. A novel fermentation pathway in an Escherichia coli mutant producing succinic acid, acetic acid, and ethanol. Appl. Biochem. Biotechnol. 70-72 (1998) 187-198
    • (1998) Appl. Biochem. Biotechnol. , vol.70-72 , pp. 187-198
    • Donnelly, M.I.1    Millard, C.S.2    Clark, D.P.3    Chen, M.J.4    Rathke, J.W.5
  • 8
    • 0031562034 scopus 로고    scopus 로고
    • Optimization of the ion-exchange analysis of organic acids from fermentation
    • Eiteman M.A., and Chastain M.J. Optimization of the ion-exchange analysis of organic acids from fermentation. Anal. Chim. Acta 338 (1997) 69-75
    • (1997) Anal. Chim. Acta , vol.338 , pp. 69-75
    • Eiteman, M.A.1    Chastain, M.J.2
  • 9
    • 0032997695 scopus 로고    scopus 로고
    • Seaweed proteins: biochemical, nutritional aspects and potential uses
    • Fleurence J. Seaweed proteins: biochemical, nutritional aspects and potential uses. Trends Food. Sci. Technol. 10 (1999) 25-28
    • (1999) Trends Food. Sci. Technol. , vol.10 , pp. 25-28
    • Fleurence, J.1
  • 10
    • 64049099490 scopus 로고    scopus 로고
    • Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism
    • Fuhrer T., and Sauer U. Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism. J. Biotechnol. 191 (2009) 2112-2121
    • (2009) J. Biotechnol. , vol.191 , pp. 2112-2121
    • Fuhrer, T.1    Sauer, U.2
  • 11
    • 0016263084 scopus 로고
    • Escherichia coli phosphoenolpyruvate carboxylase: effect of allosteric inhibitors on the kinetic parameters and sedimentation behavior
    • Gold E.W., and Smith T.E. Escherichia coli phosphoenolpyruvate carboxylase: effect of allosteric inhibitors on the kinetic parameters and sedimentation behavior. Arch. Biochem. Biophys. 164 (1974) 447-455
    • (1974) Arch. Biochem. Biophys. , vol.164 , pp. 447-455
    • Gold, E.W.1    Smith, T.E.2
  • 12
    • 0017750205 scopus 로고
    • Diffusion of carbon dioxide through lipid bilayer membranes: effects of carbonic anhydrase, bicarbonate, and unstirred layers
    • Gutknecht J., Bisson M., and Tosteson F. Diffusion of carbon dioxide through lipid bilayer membranes: effects of carbonic anhydrase, bicarbonate, and unstirred layers. J. Gen. Physiol. 69 (1977) 779-794
    • (1977) J. Gen. Physiol. , vol.69 , pp. 779-794
    • Gutknecht, J.1    Bisson, M.2    Tosteson, F.3
  • 15
    • 0014690485 scopus 로고
    • Phosphoenolpyruvate carboxylase of Salmonella. Some chemical and allosteric properties
    • Maeba P., and Sanwal B. Phosphoenolpyruvate carboxylase of Salmonella. Some chemical and allosteric properties. J. Biol. Chem. 244 (1969) 2549-2557
    • (1969) J. Biol. Chem. , vol.244 , pp. 2549-2557
    • Maeba, P.1    Sanwal, B.2
  • 16
    • 0036899531 scopus 로고    scopus 로고
    • Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases
    • Matsumura H., Xie Y., Shirakata S., Inoue T., Yoshinaga T., Ueno Y., Izui K., and Kai Y. Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases. Structure (Camb) 10 (2002) 1721-1730
    • (2002) Structure (Camb) , vol.10 , pp. 1721-1730
    • Matsumura, H.1    Xie, Y.2    Shirakata, S.3    Inoue, T.4    Yoshinaga, T.5    Ueno, Y.6    Izui, K.7    Kai, Y.8
  • 17
    • 0030887028 scopus 로고    scopus 로고
    • Structure and mechanism of phosphoenolpyruvate carboxykinase
    • Matte A., Tari L.W., Goldie H., and Delbaere L.T.J. Structure and mechanism of phosphoenolpyruvate carboxykinase. J. Biol. Chem. 272 (1997) 8105-8108
    • (1997) J. Biol. Chem. , vol.272 , pp. 8105-8108
    • Matte, A.1    Tari, L.W.2    Goldie, H.3    Delbaere, L.T.J.4
  • 18
    • 33847326777 scopus 로고    scopus 로고
    • Determining Actinobacillus succinogenes metabolic pathways and fluxes by NMR and GC-MS analyses of 13C-labeled metabolic products isotopomers
    • McKinlay J.B., Shachar-Hill Y., Zeikus J.G., and Vieille C. Determining Actinobacillus succinogenes metabolic pathways and fluxes by NMR and GC-MS analyses of 13C-labeled metabolic products isotopomers. Metab. Eng. 9 (2007) 177-192
    • (2007) Metab. Eng. , vol.9 , pp. 177-192
    • McKinlay, J.B.1    Shachar-Hill, Y.2    Zeikus, J.G.3    Vieille, C.4
  • 19
    • 0028786959 scopus 로고
    • Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: rapid and efficient purification using dye-ligand affinity chromatography
    • Modak H.V., and Kelly D.J. Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: rapid and efficient purification using dye-ligand affinity chromatography. Microbiology 141 (1995) 2619-2628
    • (1995) Microbiology , vol.141 , pp. 2619-2628
    • Modak, H.V.1    Kelly, D.J.2
  • 20
    • 0003796783 scopus 로고    scopus 로고
    • Neidhardt F.C., Curtiss III R., Ingraham J.L., Lin E.C.C., Low Jr. K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., and Umbarger H.E. (Eds), ASM Press, Washington, D.C.
    • In: Neidhardt F.C., Curtiss III R., Ingraham J.L., Lin E.C.C., Low Jr. K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., and Umbarger H.E. (Eds). Escherichia coli and Salmonella typhimurium: cellular and molecular biology. 2nd ed. (1996), ASM Press, Washington, D.C.
    • (1996) Escherichia coli and Salmonella typhimurium: cellular and molecular biology. 2nd ed.
  • 21
    • 0036330537 scopus 로고    scopus 로고
    • Noninvasive measurement of bacterial intracellular pH on a single-cell level with green fluorescent protein and fluorescence ratio imaging microscopy
    • Olsen K., Budde B., Siegumfeldt H., Rechinger K., Jakobsen M., and Ingmer H. Noninvasive measurement of bacterial intracellular pH on a single-cell level with green fluorescent protein and fluorescence ratio imaging microscopy. Appl. Environ. Microbiol. 68 (2002) 4145-4147
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 4145-4147
    • Olsen, K.1    Budde, B.2    Siegumfeldt, H.3    Rechinger, K.4    Jakobsen, M.5    Ingmer, H.6
  • 22
    • 0035964581 scopus 로고    scopus 로고
    • 2 fixation and utilization system
    • 2 fixation and utilization system. Sci. Total Environ. 277 (2001) 21-25
    • (2001) Sci. Total Environ. , vol.277 , pp. 21-25
    • Otsuki, T.1
  • 24
    • 0026254425 scopus 로고
    • Estimation of dissolved carbon dioxide concentrations in aerobic fermentations
    • Royce P.N.C., and Thornhill N.F. Estimation of dissolved carbon dioxide concentrations in aerobic fermentations. AIChE J. 37 (1991) 1680-1686
    • (1991) AIChE J. , vol.37 , pp. 1680-1686
    • Royce, P.N.C.1    Thornhill, N.F.2
  • 25
    • 84994800753 scopus 로고    scopus 로고
    • Isotopic compositions of the elements
    • Rosman K.J.R., and Taylor P.D.P. Isotopic compositions of the elements. Pure Appl. Chem. 70 (1998) 217-230
    • (1998) Pure Appl. Chem. , vol.70 , pp. 217-230
    • Rosman, K.J.R.1    Taylor, P.D.P.2
  • 26
    • 1342325419 scopus 로고    scopus 로고
    • The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli
    • Sauer U., Canonaco F., Heri S., Perrenoud A., and Fischer E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 279 (2004) 6613-6619
    • (2004) J. Biol. Chem. , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 27
    • 0026516223 scopus 로고
    • Network analysis of intermediary metabolism using linear optimisation. I. Development of mathematical formalism
    • Savinell J.M., and Palsson B.O. Network analysis of intermediary metabolism using linear optimisation. I. Development of mathematical formalism. J. Theor. Biol. 154 (1992) 421-454
    • (1992) J. Theor. Biol. , vol.154 , pp. 421-454
    • Savinell, J.M.1    Palsson, B.O.2
  • 28
    • 0031752797 scopus 로고    scopus 로고
    • Something from almost nothing: carbon dioxide fixation in chemoautotrophs
    • Shively J.M., van Keulen G., and Meijer W.G. Something from almost nothing: carbon dioxide fixation in chemoautotrophs. Annu. Rev. Microbiol. 52 (1998) 191-230
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 191-230
    • Shively, J.M.1    van Keulen, G.2    Meijer, W.G.3
  • 29
    • 0343471424 scopus 로고    scopus 로고
    • Modeling isotopomer distributions in biochemical networks using isotopomer mapping matrices
    • Schmidt K., Carlsen M., Nielsen J., and Villadsen J. Modeling isotopomer distributions in biochemical networks using isotopomer mapping matrices. Biotechnol. Bioeng. 55 (1997) 831-840
    • (1997) Biotechnol. Bioeng. , vol.55 , pp. 831-840
    • Schmidt, K.1    Carlsen, M.2    Nielsen, J.3    Villadsen, J.4
  • 33
    • 0036210809 scopus 로고    scopus 로고
    • Effects of growth mode and pyruvate carboxylase on succinic acid production by metabolically engineered strains of Escherichia coli
    • Vemuri G.N., Eiteman M.A., and Altman E. Effects of growth mode and pyruvate carboxylase on succinic acid production by metabolically engineered strains of Escherichia coli. Appl. Environ. Microbiol. 68 (2002) 1715-1727
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 1715-1727
    • Vemuri, G.N.1    Eiteman, M.A.2    Altman, E.3
  • 34
    • 0036309458 scopus 로고    scopus 로고
    • Succinate production in dual-phase Escherichia coli fermentations depends on the time of transition from aerobic to anaerobic conditions
    • Vemuri G.N., Eiteman M.A., and Altman E. Succinate production in dual-phase Escherichia coli fermentations depends on the time of transition from aerobic to anaerobic conditions. J. Ind. Microbiol. Biotechnol. 28 (2002) 325-332
    • (2002) J. Ind. Microbiol. Biotechnol. , vol.28 , pp. 325-332
    • Vemuri, G.N.1    Eiteman, M.A.2    Altman, E.3
  • 35
    • 0001173929 scopus 로고    scopus 로고
    • 2 conversion technologies using a photobioreactor incorporating microalgae-energy and material balance
    • 2 conversion technologies using a photobioreactor incorporating microalgae-energy and material balance. Energy Convers. Manage. 37 (1996) 1321-1326
    • (1996) Energy Convers. Manage. , vol.37 , pp. 1321-1326
    • Watanabe, Y.1    Hall, D.O.2
  • 36
    • 0036276675 scopus 로고    scopus 로고
    • Optimized aeration by carbon dioxide gas for microalgal production and mass transfer characterization in a vertical flat-plate photobioreactor
    • Zhang K., Kurano N., and Miyachi S. Optimized aeration by carbon dioxide gas for microalgal production and mass transfer characterization in a vertical flat-plate photobioreactor. Bioprocess Biosyst. Eng. 25 (2002) 97-101
    • (2002) Bioprocess Biosyst. Eng. , vol.25 , pp. 97-101
    • Zhang, K.1    Kurano, N.2    Miyachi, S.3


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