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Volumn 11, Issue 4, 2011, Pages 338-349

Influence of fructose and oxygen gradients on fed-batch recombinant protein production using Bacillus megaterium

Author keywords

DO based feeding; Flow cytometry; Scale down; Single cell analysis; Substrate gradients

Indexed keywords

BACILLUS MEGATERIUM; CONSTANT GRADIENTS; CONTROL PARAMETERS; CONTROLLER OUTPUTS; DO CONCENTRATION; DO-BASED FEEDING; EXPERIMENTAL APPROACHES; FED BATCHES; FEED CONTROL; GREEN FLUORESCENT PROTEIN; HIGH FREQUENCY OSCILLATIONS; LOW-AMPLITUDE; OPTIMAL FEEDING; PRODUCT FORMATION; PUMPING CAPACITY; RECOMBINANT PROTEIN PRODUCTIONS; SCALE DOWN; SINGLECELL ANALYSIS; STIRRED TANK REACTORS; SUBSTRATE CONCENTRATIONS;

EID: 84860389633     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.201000161     Document Type: Article
Times cited : (7)

References (36)
  • 1
    • 34548668469 scopus 로고    scopus 로고
    • Bacillus megaterium -- from simple soil bacterium to industrial protein production host
    • Vary, P. S., Biedendieck, R., Fürch, T., Meinhardt, et al., Bacillus megaterium -- from simple soil bacterium to industrial protein production host. Appl. Microbiol. Biotechnol. 2007, 76, 957-967.
    • (2007) Appl. Microbiol. Biotechnol. , vol.76 , pp. 957-967
    • Vary, P.S.1    Biedendieck, R.2    Fürch, T.3    Meinhardt4
  • 2
    • 33947331692 scopus 로고    scopus 로고
    • Export, purification, and activities of affinity tagged Lactobacillus reuteri levansucrase produced by Bacillus megaterium
    • Biedendieck, R., Beine, R., Gamer, M., Jordan, E., et al., Export, purification, and activities of affinity tagged Lactobacillus reuteri levansucrase produced by Bacillus megaterium. Appl. Microbiol. Biotechnol. 2007, 74, 1062-1073.
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 1062-1073
    • Biedendieck, R.1    Beine, R.2    Gamer, M.3    Jordan, E.4
  • 3
    • 0028959277 scopus 로고
    • Cloning and sequencing of the pac gene encoding the penicillin G acylase of Bacillus megaterium ATCC 14945
    • Martin, L., Prieto, M. A., Cortes, E., Garcia, J. L., Cloning and sequencing of the pac gene encoding the penicillin G acylase of Bacillus megaterium ATCC 14945. FEMS Microbiol. Lett. 1995, 125, 287-292.
    • (1995) FEMS Microbiol. Lett. , vol.125 , pp. 287-292
    • Martin, L.1    Prieto, M.A.2    Cortes, E.3    Garcia, J.L.4
  • 4
    • 0040280205 scopus 로고
    • Novel maltose-producing amylase from Bacillus megaterium G-2
    • Takasaki, Y., Novel maltose-producing amylase from Bacillus megaterium G-2. Agri. Biol. Chem. 1989, 53, 341-347.
    • (1989) Agri. Biol. Chem. , vol.53 , pp. 341-347
    • Takasaki, Y.1
  • 5
    • 0032189235 scopus 로고    scopus 로고
    • Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon
    • Raux, E., Lanois, A., Warren, M. J., Rambach, A., Thermes, C., Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon. Biochem. J. 1998, 335, 159-166.
    • (1998) Biochem. J. , vol.335 , pp. 159-166
    • Raux, E.1    Lanois, A.2    Warren, M.J.3    Rambach, A.4    Thermes, C.5
  • 6
    • 0025821274 scopus 로고
    • A barbiturate-regulated protein binding to a common sequence in the cytochrome P450 genes of rodents and bacteria
    • He, J. S., Fulco, A. J., A barbiturate-regulated protein binding to a common sequence in the cytochrome P450 genes of rodents and bacteria. J. Biol. Chem. 1991, 266, 7864-7869.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7864-7869
    • He, J.S.1    Fulco, A.J.2
  • 7
    • 26844493677 scopus 로고    scopus 로고
    • Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glucosyltransferase
    • Wang, W., Hollmann, R., Furch, T., Nimtz, M., et al., Proteome analysis of a recombinant Bacillus megaterium strain during heterologous production of a glucosyltransferase. Proteome Sci. 2005, 3, 4.
    • (2005) Proteome Sci. , vol.3 , pp. 4
    • Wang, W.1    Hollmann, R.2    Furch, T.3    Nimtz, M.4
  • 8
    • 35748946941 scopus 로고    scopus 로고
    • Effect of different carbon sources on central metabolic fluxes and the recombinant production of a hydrolase from Thermobifida fusca in Bacillus megaterium
    • Furch, T., Wittmann, C., Wang, W., Franco-Lara, E., et al., Effect of different carbon sources on central metabolic fluxes and the recombinant production of a hydrolase from Thermobifida fusca in Bacillus megaterium. J. Biotechnol. 2007, 132, 385-394.
    • (2007) J. Biotechnol. , vol.132 , pp. 385-394
    • Furch, T.1    Wittmann, C.2    Wang, W.3    Franco-Lara, E.4
  • 9
    • 0022052161 scopus 로고
    • A microbial culture with oxygen-sensitive product distribution as a potential tool for characterizing bioreactor oxygen transport
    • Moes, J., Griot, M., Keller, J., Heinzle, E., et al., A microbial culture with oxygen-sensitive product distribution as a potential tool for characterizing bioreactor oxygen transport. Biotechnol. Bioeng. 1985, 27, 482-489.
    • (1985) Biotechnol. Bioeng. , vol.27 , pp. 482-489
    • Moes, J.1    Griot, M.2    Keller, J.3    Heinzle, E.4
  • 10
    • 2942545896 scopus 로고    scopus 로고
    • Pyruvate formation and suppression in recombinant Bacillus megaterium cultivation
    • Hollmann, R., Deckwer, W. D., Pyruvate formation and suppression in recombinant Bacillus megaterium cultivation. J. Biotechnol. 2004, 111, 89-96.
    • (2004) J. Biotechnol. , vol.111 , pp. 89-96
    • Hollmann, R.1    Deckwer, W.D.2
  • 11
    • 33846913266 scopus 로고    scopus 로고
    • Plasmid system for the intracellular production and purification of affinity-tagged proteins in Bacillus megaterium
    • Biedendieck, R., Yang, Y., Deckwer, W. D., Malten, M., Jahn, D., Plasmid system for the intracellular production and purification of affinity-tagged proteins in Bacillus megaterium. Biotechnol. Bioeng. 2007, 96, 525-537.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 525-537
    • Biedendieck, R.1    Yang, Y.2    Deckwer, W.D.3    Malten, M.4    Jahn, D.5
  • 12
    • 0000658485 scopus 로고
    • High cell density culture of E. coli in a fed-batch system with dissolved oxygen as substrate feed indicator
    • Cutayar, J. M., Poillon, D., High cell density culture of E. coli in a fed-batch system with dissolved oxygen as substrate feed indicator. Biotechnol. Lett. 1989, 11, 155-160.
    • (1989) Biotechnol. Lett. , vol.11 , pp. 155-160
    • Cutayar, J.M.1    Poillon, D.2
  • 13
    • 77953641137 scopus 로고    scopus 로고
    • High-yield intra- and extracellular protein production using Bacillus megaterium
    • Stammen, S., Müller, B. K., Korneli, C., Biedendieck, R., et al., High-yield intra- and extracellular protein production using Bacillus megaterium. Appl. Environ. Microbiol. 2010, 76, 4037-4046.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 4037-4046
    • Stammen, S.1    Müller, B.K.2    Korneli, C.3    Biedendieck, R.4
  • 14
    • 0035852880 scopus 로고    scopus 로고
    • Physiological responses to mixing in large scale bioreactors
    • Enfors, S. O., Jahic, M., Rozkov, A., Xu, B., et al., Physiological responses to mixing in large scale bioreactors. J. Biotechnol. 2001, 85, 175-185.
    • (2001) J. Biotechnol. , vol.85 , pp. 175-185
    • Enfors, S.O.1    Jahic, M.2    Rozkov, A.3    Xu, B.4
  • 15
    • 0031891446 scopus 로고    scopus 로고
    • Substrate gradient formation in the large-scale bioreactor lowers cell yield and increases by-product formation
    • Bylund, F., Collet, E., Enfors, S. O., Larsson, G., Substrate gradient formation in the large-scale bioreactor lowers cell yield and increases by-product formation. Bioproc. Biosyst. Eng. 1998, 18, 171-180.
    • (1998) Bioproc. Biosyst. Eng. , vol.18 , pp. 171-180
    • Bylund, F.1    Collet, E.2    Enfors, S.O.3    Larsson, G.4
  • 16
    • 85047680567 scopus 로고    scopus 로고
    • Comparison of the Baker's yeast process performance in laboratory and production scale
    • George, S., Larsson, G., Olsson, K., Enfors, S. O., Comparison of the Baker's yeast process performance in laboratory and production scale. Bioprocess. Eng. 1998, 18, 135-142.
    • (1998) Bioprocess. Eng. , vol.18 , pp. 135-142
    • George, S.1    Larsson, G.2    Olsson, K.3    Enfors, S.O.4
  • 17
    • 62149119307 scopus 로고    scopus 로고
    • Bioreactor mixing efficiency modulates the activity of a prpoS::GFP reporter gene in E. coli
    • Delvigne, F., Boxus, M., Ingels, S., Thonart, P., Bioreactor mixing efficiency modulates the activity of a prpoS::GFP reporter gene in E. coli. Microb. Cell Fact. 2009, 8, 15.
    • (2009) Microb. Cell Fact. , vol.8 , pp. 15
    • Delvigne, F.1    Boxus, M.2    Ingels, S.3    Thonart, P.4
  • 18
    • 33846906037 scopus 로고    scopus 로고
    • A comparison of high cell density fed-batch fermentations involving both induced and non-induced recombinant Escherichia coli under well-mixed small-scale and simulated poorly mixed large-scale conditions
    • Hewitt, C. J., Onyeaka, H., Lewis, G., Taylor, I. W., Nienow, A. W., A comparison of high cell density fed-batch fermentations involving both induced and non-induced recombinant Escherichia coli under well-mixed small-scale and simulated poorly mixed large-scale conditions. Biotechnol. Bioeng. 2007, 96, 495-505.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 495-505
    • Hewitt, C.J.1    Onyeaka, H.2    Lewis, G.3    Taylor, I.W.4    Nienow, A.W.5
  • 19
    • 33846885651 scopus 로고    scopus 로고
    • Living with heterogeneities in bioreactors: understanding the effects of environmental gradients on cells
    • Lara, A. R., Galindo, E., Ramirez, O. T., Palomares, L. A., Living with heterogeneities in bioreactors: understanding the effects of environmental gradients on cells. Mol. Biotechnol. 2006, 34, 355-381.
    • (2006) Mol. Biotechnol. , vol.34 , pp. 355-381
    • Lara, A.R.1    Galindo, E.2    Ramirez, O.T.3    Palomares, L.A.4
  • 20
    • 0035811224 scopus 로고    scopus 로고
    • Scale-down model to simulate spatial pH variations in large-scale bioreactors
    • Amanullah, A., McFarlane, C. M., Emery, A. N., Nienow, A. W., Scale-down model to simulate spatial pH variations in large-scale bioreactors. Biotechnol. Bioeng. 2001, 73, 390-399.
    • (2001) Biotechnol. Bioeng. , vol.73 , pp. 390-399
    • Amanullah, A.1    McFarlane, C.M.2    Emery, A.N.3    Nienow, A.W.4
  • 21
    • 33846913266 scopus 로고    scopus 로고
    • Plasmid System for the Intracellular Production and Purification of Affinity-Tagged Proteins in Bacillus megaterium
    • Biedendieck, R., Yang, Y., Deckwer, W.-D., Malten, M., Jahn, D., Plasmid System for the Intracellular Production and Purification of Affinity-Tagged Proteins in Bacillus megaterium. Biotechnol. Bioeng. 2007, 96, 525-537.
    • (2007) Biotechnol. Bioeng. , vol.96 , pp. 525-537
    • Biedendieck, R.1    Yang, Y.2    Deckwer, W.-D.3    Malten, M.4    Jahn, D.5
  • 22
    • 33845645093 scopus 로고    scopus 로고
    • High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium
    • Yang, Y., Biedendieck, R., Wang, W., Gamer, M., et al., High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium. Microb. Cell Fact. 2006, 5, 36.
    • (2006) Microb. Cell Fact. , vol.5 , pp. 36
    • Yang, Y.1    Biedendieck, R.2    Wang, W.3    Gamer, M.4
  • 23
    • 0028919496 scopus 로고
    • Inactivation of the major extracellular protease from Bacillus megaterium DSM319 by gene replacement
    • Wittchen, K. D., Meinhardt, F., Inactivation of the major extracellular protease from Bacillus megaterium DSM319 by gene replacement. Appl. Microbiol. Biotechnol. 1995, 42, 871-877.
    • (1995) Appl. Microbiol. Biotechnol. , vol.42 , pp. 871-877
    • Wittchen, K.D.1    Meinhardt, F.2
  • 24
    • 0025892985 scopus 로고
    • Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon
    • Rygus, T., Hillen, W., Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon. Appl. Microbiol. Biotechnol. 1991, 35, 594-599.
    • (1991) Appl. Microbiol. Biotechnol. , vol.35 , pp. 594-599
    • Rygus, T.1    Hillen, W.2
  • 25
    • 0027663345 scopus 로고
    • The use of Bacillus subtilis as an oxygen sensitive culture to simulate dissolved oxygen cycling in large scale fermenters
    • Amanullah, A., Nienow, A. W., Emery, A. N., McFarlane, C. M., The use of Bacillus subtilis as an oxygen sensitive culture to simulate dissolved oxygen cycling in large scale fermenters. Food Bioprod. Process.: Trans. Inst. Chem. Eng., Part C 1993, 71, 206-208.
    • (1993) Food Bioprod. Process.: Trans. Inst. Chem. Eng., Part C , vol.71 , pp. 206-208
    • Amanullah, A.1    Nienow, A.W.2    Emery, A.N.3    McFarlane, C.M.4
  • 26
    • 79959265502 scopus 로고    scopus 로고
    • Influence of the hydromechanical stress and temperature on growth and antibody fragment production with Bacillus megaterium
    • doi: 10.1007/s00253-011-3193-7.
    • Lüders, S., David, F., Steinwand, M., Jordan, E., et al., Influence of the hydromechanical stress and temperature on growth and antibody fragment production with Bacillus megaterium. Appl. Microbiol. Biotechnol. 2011, doi: 10.1007/s00253-011-3193-7.
    • (2011) Appl. Microbiol. Biotechnol.
    • Lüders, S.1    David, F.2    Steinwand, M.3    Jordan, E.4
  • 27
    • 0027960505 scopus 로고
    • Identification of inhibitory metabolites in high density culture of recombinant Bacillus megaterium pCK108
    • Yoon, S. M., Kim, S. C., Kim, J. H., Identification of inhibitory metabolites in high density culture of recombinant Bacillus megaterium pCK108. Biotechnol. Lett. 1994, 16, 1011-1014.
    • (1994) Biotechnol. Lett. , vol.16 , pp. 1011-1014
    • Yoon, S.M.1    Kim, S.C.2    Kim, J.H.3
  • 28
    • 33645580745 scopus 로고    scopus 로고
    • Transcriptional and metabolic response of recombinant Escherichia coli to spatial dissolved oxygen tension gradients simulated in a scale-down system
    • Lara, A. R., Leal, L., Flores, N., Gosset, G., et al., Transcriptional and metabolic response of recombinant Escherichia coli to spatial dissolved oxygen tension gradients simulated in a scale-down system. Biotechnol. Bioeng. 2006, 93, 372-385.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 372-385
    • Lara, A.R.1    Leal, L.2    Flores, N.3    Gosset, G.4
  • 29
    • 0043032584 scopus 로고    scopus 로고
    • Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR
    • Salmon, K., Hung, S. P., Mekjian, K., Baldi, P., et al., Global gene expression profiling in Escherichia coli K12. The effects of oxygen availability and FNR. J. Biol. Chem. 2003, 278, 29837-29855.
    • (2003) J. Biol. Chem. , vol.278 , pp. 29837-29855
    • Salmon, K.1    Hung, S.P.2    Mekjian, K.3    Baldi, P.4
  • 31
    • 0007874893 scopus 로고    scopus 로고
    • Monitoring of genes that respond to process-related stress in large-scale bioprocesses
    • Schweder, T., Kruger, E., Xu, B., Jurgen, B., et al., Monitoring of genes that respond to process-related stress in large-scale bioprocesses. Biotechnol. Bioeng. 1999, 65, 151-159.
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 151-159
    • Schweder, T.1    Kruger, E.2    Xu, B.3    Jurgen, B.4
  • 32
    • 70449393144 scopus 로고    scopus 로고
    • Proteome analysis of the Escherichia coli heat shock response under steady-state conditions
    • Lüders, S., Fallet, C., Franco-Lara, E., Proteome analysis of the Escherichia coli heat shock response under steady-state conditions. Proteome Sci. 2009, 7, 36.
    • (2009) Proteome Sci. , vol.7 , pp. 36
    • Lüders, S.1    Fallet, C.2    Franco-Lara, E.3
  • 33
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. G., Phillips, G. N., Jr., The molecular structure of green fluorescent protein. Nat. Biotechnol. 1996, 14, 1246-1251.
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 34
    • 33646870346 scopus 로고    scopus 로고
    • Genetic oxygen sensor: GFP as an indicator of intracellular oxygenation
    • Takahashi, E., Takano, T., Numata, A., Hayashi, N., et al., Genetic oxygen sensor: GFP as an indicator of intracellular oxygenation. Adv. Exp. Med. Biol. 2005, 566, 39-44.
    • (2005) Adv. Exp. Med. Biol. , vol.566 , pp. 39-44
    • Takahashi, E.1    Takano, T.2    Numata, A.3    Hayashi, N.4
  • 35
    • 0029973636 scopus 로고    scopus 로고
    • FACS-optimized mutants of the green fluorescent protein (GFP)
    • Cormack, B. P., Valdivia, R. H., Falkow, S., FACS-optimized mutants of the green fluorescent protein (GFP). Gene 1996, 173, 33-38.
    • (1996) Gene , vol.173 , pp. 33-38
    • Cormack, B.P.1    Valdivia, R.H.2    Falkow, S.3
  • 36
    • 37249066180 scopus 로고    scopus 로고
    • Control of cultivation processes for recombinant protein production: a review
    • Gnoth, S., Jenzsch, M., Simutis, R., Lubbert, A., Control of cultivation processes for recombinant protein production: a review. Bioprocess Biosyst. Eng. 2008, 31, 21-39.
    • (2008) Bioprocess Biosyst. Eng. , vol.31 , pp. 21-39
    • Gnoth, S.1    Jenzsch, M.2    Simutis, R.3    Lubbert, A.4


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