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Volumn 8, Issue 2, 2008, Pages 132-138

Applications of PAT-process analytical technology in recombinant protein processes with Escherichia coli

Author keywords

Bioprocess monitoring; Biotechnology; Radio frequency impedance measurement

Indexed keywords

CELLS; ESCHERICHIA COLI; PROCESS MONITORING; PROTEINS; QUALITY CONTROL;

EID: 42649126394     PISSN: 16180240     EISSN: 16182863     Source Type: Journal    
DOI: 10.1002/elsc.200720232     Document Type: Article
Times cited : (29)

References (20)
  • 1
    • 0035829831 scopus 로고    scopus 로고
    • On-line estimation of the metabolic burden resulting from the synthesis of plasmid-encoded and heat-shock proteins by monitoring respiratory energy generation
    • F. Hoffmann, U. Rinas, On-line estimation of the metabolic burden resulting from the synthesis of plasmid-encoded and heat-shock proteins by monitoring respiratory energy generation, Biotechnol. Bioeng. 2001, 76 (4), 333-340.
    • (2001) Biotechnol. Bioeng , vol.76 , Issue.4 , pp. 333-340
    • Hoffmann, F.1    Rinas, U.2
  • 2
    • 0029874193 scopus 로고    scopus 로고
    • High cell-density culture of Escherichia coli
    • S. Y. Lee, High cell-density culture of Escherichia coli, Trends Biotechnol. 1996, 14, 98-105.
    • (1996) Trends Biotechnol , vol.14 , pp. 98-105
    • Lee, S.Y.1
  • 3
    • 0029636928 scopus 로고
    • Fed-batch feeding and induction policies that improve foreign synthesis and stability by avoiding stress responses
    • D. M. Ramirez, W. E. Bentley, Fed-batch feeding and induction policies that improve foreign synthesis and stability by avoiding stress responses, Biotechnol. Bioeng. 1995, 47, 596-608.
    • (1995) Biotechnol. Bioeng , vol.47 , pp. 596-608
    • Ramirez, D.M.1    Bentley, W.E.2
  • 4
    • 0031943426 scopus 로고    scopus 로고
    • Growth associated synthesis of recombinant human glucon and human growth hormone in high-cell-density cultures of Escherichia coli
    • C. S. Shin, M. S. Hong, D. Y. Kim, H. C. Shin, J. Lee, Growth associated synthesis of recombinant human glucon and human growth hormone in high-cell-density cultures of Escherichia coli, Appl. Microbiol. Biotechnol. 1998, 49, 364-370.
    • (1998) Appl. Microbiol. Biotechnol , vol.49 , pp. 364-370
    • Shin, C.S.1    Hong, M.S.2    Kim, D.Y.3    Shin, H.C.4    Lee, J.5
  • 5
    • 12244259063 scopus 로고    scopus 로고
    • Limiting factors in Escherichia coli fed-batch production of recombinant proteins
    • A. M. Sandén, J. Prytz, I. Tubulekas, C. Förberg, H. Le, A. Hektor et al., Limiting factors in Escherichia coli fed-batch production of recombinant proteins, Biotechnol. Bioeng. 2002, 81, 158-166.
    • (2002) Biotechnol. Bioeng , vol.81 , pp. 158-166
    • Sandén, A.M.1    Prytz, J.2    Tubulekas, I.3    Förberg, C.4    Le, H.5    Hektor, A.6
  • 6
    • 0025314282 scopus 로고
    • The production of recombinant β-galactosidase in Escherichia coli in yeast extract enriched medium
    • X. Li, J. W. Robbins, K. B. Taylor, The production of recombinant β-galactosidase in Escherichia coli in yeast extract enriched medium, J. Ind. Microbiol. 1990, 5, 85-94.
    • (1990) J. Ind. Microbiol , vol.5 , pp. 85-94
    • Li, X.1    Robbins, J.W.2    Taylor, K.B.3
  • 7
    • 0026245821 scopus 로고
    • Metabolic roles of peptone and yeast extract for the culture of a recombinant strain of Escherichia coli
    • N. Nancib, H. Branlant, C. Boudrant, Metabolic roles of peptone and yeast extract for the culture of a recombinant strain of Escherichia coli, J. Ind, Microbiol. 1991, 8, 165-170.
    • (1991) J. Ind, Microbiol , vol.8 , pp. 165-170
    • Nancib, N.1    Branlant, H.2    Boudrant, C.3
  • 8
    • 0027909089 scopus 로고
    • Enhancement of recombinant protein synthesis and stability via coordinated amino acid addition
    • D. M. Ramirez, W. E. Bentley, Enhancement of recombinant protein synthesis and stability via coordinated amino acid addition, Biotechnol. Bioeng. 1993, 41, 557-565.
    • (1993) Biotechnol. Bioeng , vol.41 , pp. 557-565
    • Ramirez, D.M.1    Bentley, W.E.2
  • 9
    • 0025969480 scopus 로고
    • Temperature and induction effects in the degradation rate of an abnormal β-galactosidase in Escherichia coli
    • M. J. Kosinski, J. E. Bailey, Temperature and induction effects in the degradation rate of an abnormal β-galactosidase in Escherichia coli, J. Biotechnol. 1991, 18, 55-68.
    • (1991) J. Biotechnol , vol.18 , pp. 55-68
    • Kosinski, M.J.1    Bailey, J.E.2
  • 10
    • 0026417070 scopus 로고
    • Effect of chemically-induced cloned-gene expression on protein synthesis in E. coli
    • T. K. Wood, S. W. Peretti, Effect of chemically-induced cloned-gene expression on protein synthesis in E. coli, Biotechnol. Bioeng. 1991, 38, 397-412.
    • (1991) Biotechnol. Bioeng , vol.38 , pp. 397-412
    • Wood, T.K.1    Peretti, S.W.2
  • 11
    • 0033527396 scopus 로고    scopus 로고
    • Monitoring GF Poperon fusion protein expression during high cell density cultivation of Escherichia coli using an on-line optical sensor
    • M. P. DeLisa, J. Li, G. Rao, W. A. Weigand, W. E. Bentley, Monitoring GF Poperon fusion protein expression during high cell density cultivation of Escherichia coli using an on-line optical sensor, Biotechnol. Bioeng. 1999, 65, 54-64.
    • (1999) Biotechnol. Bioeng , vol.65 , pp. 54-64
    • DeLisa, M.P.1    Li, J.2    Rao, G.3    Weigand, W.A.4    Bentley, W.E.5
  • 12
    • 0001154861 scopus 로고    scopus 로고
    • Observation of green fluorescent protein as a fusion partner in genetically engineered Escherichia coli: Monitoring protein expression and solubility
    • H. J. Cha, C.-F. Wu, J. J. Valdes, G. Rao, W. E. Bentley, Observation of green fluorescent protein as a fusion partner in genetically engineered Escherichia coli: Monitoring protein expression and solubility, Biotechnol. Bioeng. 2000, 67, 565-574.
    • (2000) Biotechnol. Bioeng , vol.67 , pp. 565-574
    • Cha, H.J.1    Wu, C.-F.2    Valdes, J.J.3    Rao, G.4    Bentley, W.E.5
  • 15
    • 0031907915 scopus 로고    scopus 로고
    • Two-dimensional fluorescence spectroscopy: A new tool for on-line bioprocess monitoring
    • S. Marose, C. Lindemann, T. Scheper, Two-dimensional fluorescence spectroscopy: A new tool for on-line bioprocess monitoring, Biotechnol. Prog. 1998, 14, 63-74.
    • (1998) Biotechnol. Prog , vol.14 , pp. 63-74
    • Marose, S.1    Lindemann, C.2    Scheper, T.3
  • 17
    • 42649133936 scopus 로고    scopus 로고
    • Deutsches Institut für Normung e. V., Deutsche Einheitsverfahren zur Wasser-, Abwasser-, und Schlammuntersuchung: Bestimmung des Ammonium-Stickstoffs (DIN 38406-E5), 1983.
    • Deutsches Institut für Normung e. V., Deutsche Einheitsverfahren zur Wasser-, Abwasser-, und Schlammuntersuchung: Bestimmung des Ammonium-Stickstoffs (DIN 38406-E5), 1983.
  • 18
    • 42649107275 scopus 로고    scopus 로고
    • O. S. Wolfbeis, The fluorescence of organic natural products, in Molecular Luminescence Spectroscopy Methods and Applications, 77, Part I (Ed: S.G. Schulman), Wiley-Interscience, New York (USA), 167-370, 1985.
    • O. S. Wolfbeis, The fluorescence of organic natural products, in Molecular Luminescence Spectroscopy Methods and Applications, Vol. 77, Part I (Ed: S.G. Schulman), Wiley-Interscience, New York (USA), 167-370, 1985.
  • 19
    • 3042511548 scopus 로고    scopus 로고
    • Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP
    • O. Zapata-Hommer, O. Griesbeck, Efficiently folding and circularly permuted variants of the Sapphire mutant of GFP, BMC Biotechnol. 2003, 3, 1-6.
    • (2003) BMC Biotechnol , vol.3 , pp. 1-6
    • Zapata-Hommer, O.1    Griesbeck, O.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U. K. Laemmli, Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 1970, 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.