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Volumn 155, Issue 2, 2011, Pages 178-184

Quantification of metabolic limitations during recombinant protein production in Escherichia coli

Author keywords

13C flux analysis; Flux probe; Metabolic network analysis; MFA; Recombinant protein production

Indexed keywords

ATP GENERATION; BATCH CULTIVATION; BIOMASS YIELD; CELLULAR ENERGY; E. COLI; ELECTRON TRANSPORT CHAIN; ENERGY DEMANDS; EXPRESSION VECTORS; FLUX ANALYSIS; FLUX DISTRIBUTIONS; GENERATION RATE; METABOLIC FLUX ANALYSIS; METABOLIC NETWORK ANALYSIS; MFA; MOLECULAR GENETICS; RECOMBINANT PROTEIN; RECOMBINANT PROTEIN PRODUCTIONS; REFERENCE STRAINS; SOLUBLE TRANSHYDROGENASE; TCA CYCLE;

EID: 80051474345     PISSN: 01681656     EISSN: 18734863     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2011.06.016     Document Type: Article
Times cited : (57)

References (48)
  • 1
    • 0028968239 scopus 로고
    • Critical limitations in ciological production of chemicals: process or genetic solutions?
    • Bailey J.E. Critical limitations in ciological production of chemicals: process or genetic solutions?. FEMS Microbiol. Rev. 1995, 16:271-276.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 271-276
    • Bailey, J.E.1
  • 2
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • Baneyx F. Recombinant protein expression in Escherichia coli. Curr. Opin. Biotechnol. 1999, 10:411-421.
    • (1999) Curr. Opin. Biotechnol. , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 3
    • 0025405549 scopus 로고
    • Plasmid-encoded protein: the principal factor in the "metabolic burden" associated with recombinant bacteria
    • Bentley W.E., Mirjalili N., Andersen D.C., Davis R.H., Kompala D.S. Plasmid-encoded protein: the principal factor in the "metabolic burden" associated with recombinant bacteria. Biotechnol. Bioeng. 1990, 35:668-681.
    • (1990) Biotechnol. Bioeng. , vol.35 , pp. 668-681
    • Bentley, W.E.1    Mirjalili, N.2    Andersen, D.C.3    Davis, R.H.4    Kompala, D.S.5
  • 4
    • 25444467580 scopus 로고    scopus 로고
    • 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast
    • 13C-flux analysis reveals mechanistic principles of metabolic network robustness to null mutations in yeast. Genome Biol. 2005, 6:R49.
    • (2005) Genome Biol. , vol.6
    • Blank, L.M.1    Kuepfer, L.2    Sauer, U.3
  • 5
    • 0032945184 scopus 로고    scopus 로고
    • The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase
    • Boonstra B., French C.E., Wainwright I., Bruce N.C. The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase. J. Bacteriol. 1999, 181:1030-1034.
    • (1999) J. Bacteriol. , vol.181 , pp. 1030-1034
    • Boonstra, B.1    French, C.E.2    Wainwright, I.3    Bruce, N.C.4
  • 6
    • 40549093298 scopus 로고    scopus 로고
    • NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain
    • Buehler B., Park J.B., Blank L.M., Schmid A. NADH availability limits asymmetric biocatalytic epoxidation in a growing recombinant Escherichia coli strain. Appl. Environ. Microbiol. 2008, 74:1436-1446.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1436-1446
    • Buehler, B.1    Park, J.B.2    Blank, L.M.3    Schmid, A.4
  • 7
    • 74849113944 scopus 로고    scopus 로고
    • Metabolic flux analysis for recombinant protein production by Pichia pastoris using dual carbon sources: effects of methanol feeding rate
    • Celik E., Calik P., Oliver S.G. Metabolic flux analysis for recombinant protein production by Pichia pastoris using dual carbon sources: effects of methanol feeding rate. Biotechnol. Bioeng. 2010, 105:317-329.
    • (2010) Biotechnol. Bioeng. , vol.105 , pp. 317-329
    • Celik, E.1    Calik, P.2    Oliver, S.G.3
  • 8
    • 34548012600 scopus 로고    scopus 로고
    • Engineering cell physiology to enhance recombinant protein production in Escherichia coli
    • Chou C.P. Engineering cell physiology to enhance recombinant protein production in Escherichia coli. Appl. Microbiol. Biotechnol. 2007, 76:521-532.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 521-532
    • Chou, C.P.1
  • 9
    • 0022711472 scopus 로고
    • Theoretical growth yield estimates for recombinant cells
    • Da Silva N.A., Bailey J.E. Theoretical growth yield estimates for recombinant cells. Biotechnol. Bioeng. 1985, 28:741-746.
    • (1985) Biotechnol. Bioeng. , vol.28 , pp. 741-746
    • Da Silva, N.A.1    Bailey, J.E.2
  • 12
    • 64049099490 scopus 로고    scopus 로고
    • Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism
    • Fuhrer T., Sauer U. Different biochemical mechanisms ensure network-wide balancing of reducing equivalents in microbial metabolism. J. Bacteriol. 2009, 191:2112-2121.
    • (2009) J. Bacteriol. , vol.191 , pp. 2112-2121
    • Fuhrer, T.1    Sauer, U.2
  • 14
    • 24344438618 scopus 로고    scopus 로고
    • A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic β-tri- and β-dipeptides
    • Geueke B., Namoto K., Seebach D., Kohler H.P. A novel β-peptidyl aminopeptidase (BapA) from strain 3-2W4 cleaves peptide bonds of synthetic β-tri- and β-dipeptides. J. Bacteriol. 2005, 187:5910-5917.
    • (2005) J. Bacteriol. , vol.187 , pp. 5910-5917
    • Geueke, B.1    Namoto, K.2    Seebach, D.3    Kohler, H.P.4
  • 15
    • 33751117982 scopus 로고    scopus 로고
    • Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β, α-oligopeptides
    • Geueke B., Heck T., Limbach M., Nesatyy V., Seebach D., Kohler H.P. Bacterial β-peptidyl aminopeptidases with unique substrate specificities for β-oligopeptides and mixed β, α-oligopeptides. FEBS J. 2006, 273:5261-5272.
    • (2006) FEBS J. , vol.273 , pp. 5261-5272
    • Geueke, B.1    Heck, T.2    Limbach, M.3    Nesatyy, V.4    Seebach, D.5    Kohler, H.P.6
  • 16
    • 35348887734 scopus 로고    scopus 로고
    • Metabolic flux analysis for optimizing the specific growth rate of recombinant Aspergillus niger
    • Gheshlaghi R., Scharer J.M., Moo-Young M., Douglas P.L. Metabolic flux analysis for optimizing the specific growth rate of recombinant Aspergillus niger. Bioproc. Biosyst. Eng. 2007, 30:397-418.
    • (2007) Bioproc. Biosyst. Eng. , vol.30 , pp. 397-418
    • Gheshlaghi, R.1    Scharer, J.M.2    Moo-Young, M.3    Douglas, P.L.4
  • 17
    • 0033672578 scopus 로고    scopus 로고
    • A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli
    • Gill R.T., Valdes J.J., Bentley W.E. A comparative study of global stress gene regulation in response to overexpression of recombinant proteins in Escherichia coli. Metab. Eng. 2000, 2:178-189.
    • (2000) Metab. Eng. , vol.2 , pp. 178-189
    • Gill, R.T.1    Valdes, J.J.2    Bentley, W.E.3
  • 18
    • 0028801765 scopus 로고
    • Metabolic load and heterologous gene expression
    • Glick B.R. Metabolic load and heterologous gene expression. Biotechnol. Adv. 1995, 13:247-261.
    • (1995) Biotechnol. Adv. , vol.13 , pp. 247-261
    • Glick, B.R.1
  • 19
    • 0035140099 scopus 로고    scopus 로고
    • Network identification and flux quantification in the central metabolism of Saccharomyces cerevisiae under different conditions of glucose repression
    • Gombert A.K., Moreira dos Santos M., Christensen B., Nielsen J. Network identification and flux quantification in the central metabolism of Saccharomyces cerevisiae under different conditions of glucose repression. J. Bacteriol. 2001, 183:1441-1451.
    • (2001) J. Bacteriol. , vol.183 , pp. 1441-1451
    • Gombert, A.K.1    Moreira dos Santos, M.2    Christensen, B.3    Nielsen, J.4
  • 21
    • 34948904391 scopus 로고    scopus 로고
    • Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes
    • Heck T., Kohler H.P.E., Limbach M., Flogel O., Seebach D., Geueke B. Enzyme-catalyzed formation of β-peptides: β-peptidyl aminopeptidases BapA and DmpA acting as β-peptide-synthesizing enzymes. Chem. Biodivers. 2007, 4:2016-2030.
    • (2007) Chem. Biodivers. , vol.4 , pp. 2016-2030
    • Heck, T.1    Kohler, H.P.E.2    Limbach, M.3    Flogel, O.4    Seebach, D.5    Geueke, B.6
  • 22
    • 71449083602 scopus 로고    scopus 로고
    • Correlation between TCA cycle flux and glucose uptake rate during respiro-fermentative growth of Saccharomyces cerevisiae
    • Heyland J., Fu J., Blank L.M. Correlation between TCA cycle flux and glucose uptake rate during respiro-fermentative growth of Saccharomyces cerevisiae. Microbiology 2009, 155:3827-3837.
    • (2009) Microbiology , vol.155 , pp. 3827-3837
    • Heyland, J.1    Fu, J.2    Blank, L.M.3
  • 24
    • 78149252300 scopus 로고    scopus 로고
    • Quantitative physiology of Pichia pastoris during glucose-limited high cell-density fed-batch cultivation for recombinant protein production
    • Heyland J., Fu J., Blank L.M., Schmid A. Quantitative physiology of Pichia pastoris during glucose-limited high cell-density fed-batch cultivation for recombinant protein production. Biotechnol. Bioeng. 2010, 107:357-368.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 357-368
    • Heyland, J.1    Fu, J.2    Blank, L.M.3    Schmid, A.4
  • 25
    • 79959227594 scopus 로고    scopus 로고
    • Carbon metabolism limits recombinant protein production in Pichia pastoris
    • Heyland J., Fu J., Blank L.M., Schmid A. Carbon metabolism limits recombinant protein production in Pichia pastoris. Biotechnol. Bioeng. 2011.
    • (2011) Biotechnol. Bioeng.
    • Heyland, J.1    Fu, J.2    Blank, L.M.3    Schmid, A.4
  • 26
    • 0037027382 scopus 로고    scopus 로고
    • Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 1. Readjustment of metabolic enzyme synthesis
    • Hoffmann F., Weber J., Rinas U. Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 1. Readjustment of metabolic enzyme synthesis. Biotechnol. Bioeng. 2002, 80:313-319.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 313-319
    • Hoffmann, F.1    Weber, J.2    Rinas, U.3
  • 27
    • 2942755215 scopus 로고    scopus 로고
    • Stress induced by recombinant protein production in Escherichia coli
    • Springer Verlag, Berlin/Heidelberg
    • Hoffmann F., Rinas U. Stress induced by recombinant protein production in Escherichia coli. Adv Biochem Eng Biotechnol 2004, vol. 89. Springer Verlag, Berlin/Heidelberg, pp. 73-92.
    • (2004) Adv Biochem Eng Biotechnol , vol.89 , pp. 73-92
    • Hoffmann, F.1    Rinas, U.2
  • 28
    • 0031560764 scopus 로고    scopus 로고
    • Metabolic flux distributions in recombinant Saccharomyces cerevisiae during foreign protein production
    • Jin S., Ye K., Shimizu K. Metabolic flux distributions in recombinant Saccharomyces cerevisiae during foreign protein production. J. Biotechnol. 1997, 54:161-174.
    • (1997) J. Biotechnol. , vol.54 , pp. 161-174
    • Jin, S.1    Ye, K.2    Shimizu, K.3
  • 30
    • 43149090780 scopus 로고    scopus 로고
    • Analysis of metabolic flux in Escherichia coli expressing human-like collagen in fed-batch culture
    • Luo Y.E., Fan D.D., Shang L.A., Shi H.J., Ma X.X., Mi Y., Zhao G.F. Analysis of metabolic flux in Escherichia coli expressing human-like collagen in fed-batch culture. Biotechnol. Lett. 2008, 30:637-643.
    • (2008) Biotechnol. Lett. , vol.30 , pp. 637-643
    • Luo, Y.E.1    Fan, D.D.2    Shang, L.A.3    Shi, H.J.4    Ma, X.X.5    Mi, Y.6    Zhao, G.F.7
  • 33
    • 11144250932 scopus 로고    scopus 로고
    • Metabolic flux analysis of recombinant protein overproduction in Escherichia coli
    • Ozkan P., Sariyar B., Utkur F.O., Akman U., Hortacsu A. Metabolic flux analysis of recombinant protein overproduction in Escherichia coli. Biochem. Eng. J. 2005, 22:167-195.
    • (2005) Biochem. Eng. J. , vol.22 , pp. 167-195
    • Ozkan, P.1    Sariyar, B.2    Utkur, F.O.3    Akman, U.4    Hortacsu, A.5
  • 36
    • 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., Fischer E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J. Biol. Chem. 2004, 279:6613-6619.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 37
    • 0035498813 scopus 로고    scopus 로고
    • A method for the quantitative recovery of proteins from polyacrylamide gels
    • Scheer J.M., Ryan C.A. A method for the quantitative recovery of proteins from polyacrylamide gels. Anal. Biochem. 2001, 298:130-132.
    • (2001) Anal. Biochem. , vol.298 , pp. 130-132
    • Scheer, J.M.1    Ryan, C.A.2
  • 38
    • 0033230145 scopus 로고    scopus 로고
    • Secretion dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy generating dissimilatory pathway
    • Schmidt M., Viaplana E., Hoffmann F., Marten S., Villaverde A., Rinas U. Secretion dependent proteolysis of heterologous protein by recombinant Escherichia coli is connected to an increased activity of the energy generating dissimilatory pathway. Biotechnol. Bioeng. 1999, 66:61-67.
    • (1999) Biotechnol. Bioeng. , vol.66 , pp. 61-67
    • Schmidt, M.1    Viaplana, E.2    Hoffmann, F.3    Marten, S.4    Villaverde, A.5    Rinas, U.6
  • 40
    • 38849088087 scopus 로고    scopus 로고
    • Isotopomer distributions in amino acids from a highly expressed protein as a proxy for those from total protein
    • Shaikh A.S., Tang Y.J., Mukhopadhyay A., Keasling J.D. Isotopomer distributions in amino acids from a highly expressed protein as a proxy for those from total protein. Anal. Chem. 2008, 80:886-890.
    • (2008) Anal. Chem. , vol.80 , pp. 886-890
    • Shaikh, A.S.1    Tang, Y.J.2    Mukhopadhyay, A.3    Keasling, J.D.4
  • 42
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sorensen H.P., Mortensen K.K. Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 2005, 115:113-128.
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 43
    • 33748535379 scopus 로고    scopus 로고
    • Metabolic physiology of Pseudomonas putida for heterologous production of myxochromide
    • Stephan S., Heinzle E., Wenzel S.C., Krug D., Müller R., Wittmann C. Metabolic physiology of Pseudomonas putida for heterologous production of myxochromide. Process Biochem. 2006, 41:2146-2152.
    • (2006) Process Biochem. , vol.41 , pp. 2146-2152
    • Stephan, S.1    Heinzle, E.2    Wenzel, S.C.3    Krug, D.4    Müller, R.5    Wittmann, C.6
  • 44
    • 78649511651 scopus 로고    scopus 로고
    • Systems biology approach reveals that overflow metabolism of acetate in Escherichia coli is triggered by carbon catabolite repression of acetyl-CoA synthetase
    • Valgepea K., Adamberg K., Nahku R., Lahtvee P.J., Arike L., Vilu R. Systems biology approach reveals that overflow metabolism of acetate in Escherichia coli is triggered by carbon catabolite repression of acetyl-CoA synthetase. BMC Syst. Biol. 2010, 4:166.
    • (2010) BMC Syst. Biol. , vol.4 , pp. 166
    • Valgepea, K.1    Adamberg, K.2    Nahku, R.3    Lahtvee, P.J.4    Arike, L.5    Vilu, R.6
  • 45
    • 33846827387 scopus 로고    scopus 로고
    • Global gene expression analysis of glucose overflow metabolism in Escherichia coli and reduction of aerobic acetate formation
    • Veit A., Polen T., Wendisch V.F. Global gene expression analysis of glucose overflow metabolism in Escherichia coli and reduction of aerobic acetate formation. Appl. Microbiol. Biotechnol. 2007, 74:406-421.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 406-421
    • Veit, A.1    Polen, T.2    Wendisch, V.F.3
  • 46
    • 0037027392 scopus 로고    scopus 로고
    • Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 2. Redirection of metabolic fluxes
    • Weber J., Hoffmann F., Rinas U. Metabolic adaptation of Escherichia coli during temperature-induced recombinant protein production: 2. Redirection of metabolic fluxes. Biotechnol. Bioeng. 2002, 80:320-330.
    • (2002) Biotechnol. Bioeng. , vol.80 , pp. 320-330
    • Weber, J.1    Hoffmann, F.2    Rinas, U.3
  • 47
    • 33847691476 scopus 로고    scopus 로고
    • Fluxome analysis using GC-MS
    • Wittmann C. Fluxome analysis using GC-MS. Microb. Cell Fact. 2007, 6:6.
    • (2007) Microb. Cell Fact. , vol.6 , pp. 6
    • Wittmann, C.1
  • 48
    • 35748959651 scopus 로고    scopus 로고
    • Response of fluxome and metabolome to temperature-induced recombinant protein synthesis in Escherichia coli
    • Wittmann C., Weber J., Betiku E., Kromer J., Bohm D., Rinas U. Response of fluxome and metabolome to temperature-induced recombinant protein synthesis in Escherichia coli. J. Biotechnol. 2007, 132:375-384.
    • (2007) J. Biotechnol. , vol.132 , pp. 375-384
    • Wittmann, C.1    Weber, J.2    Betiku, E.3    Kromer, J.4    Bohm, D.5    Rinas, U.6


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