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Volumn 14, Issue 3, 2009, Pages 274-280

Improvement of soluble recombinant interferon-α expression by methyl α-D-glucopyranoside in araBAD promoter system of Escherichia coli

Author keywords

araBAD promoter; Escherichia coli; Methyl D glucopyranoside; Modulation of transcription; Soluble expression of interferon

Indexed keywords

ARABAD PROMOTER; FED-BATCH CULTURES; GLUCOPYRANOSIDE; INCLUSION BODIES; L-ARABINOSE; OPTIMAL TEMPERATURE; PROTEIN EXPRESSIONS; RECOMBINANT HUMAN INTERFERON; RECOMBINANT PROTEIN; SOLUBLE EXPRESSION; SOLUBLE FRACTION;

EID: 67651089535     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12257-008-0270-6     Document Type: Article
Times cited : (4)

References (45)
  • 1
    • 0029032444 scopus 로고
    • In vivo induction kinetics of the arabinose promoters in Escherichia coli
    • Johnson, C. M. and R. T. Schleif (1995) In vivo induction kinetics of the arabinose promoters in Escherichia coli. J. Bacteriol. 177:3438-3442.
    • (1995) J. Bacteriol. , vol.177 , pp. 3438-3442
    • Johnson, C.M.1    Schleif, R.T.2
  • 2
    • 0023101751 scopus 로고
    • Repression and catabolite gene activation in the araBAD operon
    • Lichenstein, H. S., E. P. Hamilton, and N. Lee (1987) Repression and catabolite gene activation in the araBAD operon. J. Bacteriol. 169:811-822.
    • (1987) J. Bacteriol. , vol.169 , pp. 811-822
    • Lichenstein, H.S.1    Hamilton, E.P.2    Lee, N.3
  • 3
    • 0034564982 scopus 로고    scopus 로고
    • Regulation of the L-arabinose operon of Escherichia coli
    • Schleif, R. (2000) Regulation of the L-arabinose operon of Escherichia coli. Trends Genet. 16:559-565.
    • (2000) Trends Genet. , vol.16 , pp. 559-565
    • Schleif, R.1
  • 4
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • Sørensen, H. P. and K. K. Mortensen (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J. Biotechnol. 115:113-128.
    • (2005) J. Biotechnol. , vol.115 , pp. 113-128
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 5
    • 0031909984 scopus 로고    scopus 로고
    • Catabolite gene activator protein mutations affecting activity of the araBAD promoter
    • Zhang, X. and R. Schleif (1998) Catabolite gene activator protein mutations affecting activity of the araBAD promoter. J. Bacteriol. 180:195-200.
    • (1998) J. Bacteriol. , vol.180 , pp. 195-200
    • Zhang, X.1    Schleif, R.2
  • 6
    • 0034791258 scopus 로고    scopus 로고
    • Development and optimization of two-stage cyclic fed-batch culture for hG-CSF production using L-arabinose promoter of Escherichia coli
    • Choi, S.-J., D.-H. Park, and K.-H. Jung (2001) Development and optimization of two-stage cyclic fed-batch culture for hG-CSF production using L-arabinose promoter of Escherichia coli. Bioproc. Biosyst. Eng. 24:51-58.
    • (2001) Bioproc. Biosyst. Eng. , vol.24 , pp. 51-58
    • Choi, S.-J.1    Park, D.-H.2    Jung, K.-H.3
  • 7
    • 0033997508 scopus 로고    scopus 로고
    • Production characteristics of interferon-α using L-arabinose promoter system in a high-cell-density culture
    • Lim, H.-K., K.-H. Jung, D.-H. Park, and S.-I. Chung (2000) Production characteristics of interferon-α using L-arabinose promoter system in a high-cell-density culture. Appl. Microbiol. Biotechnol. 53:201-208.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 201-208
    • Lim, H.-K.1    Jung, K.-H.2    Park, D.-H.3    Chung, S.-I.4
  • 8
    • 40549106156 scopus 로고    scopus 로고
    • Construction and characterization of a recombinant whole-cell biocatalyst of Escherichia coli expressing styrene monooxygenase under the control of arabinose promoter
    • Bae, J. W., S. Shin, S. M. Raj, S. E. Lee, S. G. Lee, Y. J. Jeong, and S. Park (2008) Construction and characterization of a recombinant whole-cell biocatalyst of Escherichia coli expressing styrene monooxygenase under the control of arabinose promoter. Biotechnol. Bioprocess Eng. 13:69-76.
    • (2008) Biotechnol. Bioprocess Eng. , vol.13 , pp. 69-76
    • Bae, J.W.1    Shin, S.2    Raj, S.M.3    Lee, S.E.4    Lee, S.G.5    Jeong, Y.J.6    Park, S.7
  • 9
    • 36049050959 scopus 로고    scopus 로고
    • Enhanced tolerance against freezing stress in Escherichia coli cells expressing an algal cyclophilin gene
    • Cho, E. K. (2007) Enhanced tolerance against freezing stress in Escherichia coli cells expressing an algal cyclophilin gene. Biotechnol. Bioprocess Eng. 12:502-507.
    • (2007) Biotechnol. Bioprocess Eng. , vol.12 , pp. 502-507
    • Cho, E.K.1
  • 10
    • 0032126153 scopus 로고    scopus 로고
    • Improvement of heterologous protein productivity by controlling postinduction specific growth rate in recombinant Escherichia coli under control of the PL promoter
    • Lim, H.-K. and K.-H. Jung (1998) Improvement of heterologous protein productivity by controlling postinduction specific growth rate in recombinant Escherichia coli under control of the PL promoter. Biotechnol. Prog. 14:548-553.
    • (1998) Biotechnol. Prog. , vol.14 , pp. 548-553
    • Lim, H.-K.1    Jung, K.-H.2
  • 11
    • 1542292928 scopus 로고    scopus 로고
    • Induction of the T7 promoter using lactose for production of recombinant plasminogen kringle 1-3 in Escherichia coli
    • Lim, H.-K., S.-U. Lee, S.-I. Chung, K.-H. Jung, and J.-H. Seo (2004) Induction of the T7 promoter using lactose for production of recombinant plasminogen kringle 1-3 in Escherichia coli. J. Microbiol. Biotechnol. 14:225-230.
    • (2004) J. Microbiol. Biotechnol. , vol.14 , pp. 225-230
    • Lim, H.-K.1    Lee, S.-U.2    Chung, S.-I.3    Jung, K.-H.4    Seo, J.-H.5
  • 12
    • 27844581254 scopus 로고    scopus 로고
    • Production of recombinant proteins by high cell density culture of Escherichia coli
    • Choi, J. H., K. C. Keum, and S. Y. Lee (2006) Production of recombinant proteins by high cell density culture of Escherichia coli. Chem. Eng. Sci. 61:876-885.
    • (2006) Chem. Eng. Sci. , vol.61 , pp. 876-885
    • Choi, J.H.1    Keum, K.C.2    Lee, S.Y.3
  • 13
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sørensen, H. P. and K. K. Mortensen (2005) Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb. Cell Fact. 4:1.
    • (2005) Microb. Cell Fact. , vol.4 , pp. 1
    • Sørensen, H.P.1    Mortensen, K.K.2
  • 14
    • 0442292087 scopus 로고    scopus 로고
    • Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and pilot plant scale
    • Hoffmann, F., J. van den Heuvel, N. Zidek, and U. Rinas (2004) Minimizing inclusion body formation during recombinant protein production in Escherichia coli at bench and pilot plant scale. Enzyme Microb. Technol. 34:235-241.
    • (2004) Enzyme Microb. Technol. , vol.34 , pp. 235-241
    • Hoffmann, F.1    van den Heuvel, J.2    Zidek, N.3    Rinas, U.4
  • 15
    • 34248403770 scopus 로고    scopus 로고
    • Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate
    • Koo, T. Y. and T. H. Park (2007) Expression of recombinant human growth hormone in a soluble form in Escherichia coli by slowing down the protein synthesis rate. J. Microbiol. Biotechnol. 17:579-585.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 579-585
    • Koo, T.Y.1    Park, T.H.2
  • 16
    • 33746744319 scopus 로고    scopus 로고
    • Enhancement of soluble protein expression through the use of fusion tags
    • Esposito, D. and D. K. Chatterjee (2006) Enhancement of soluble protein expression through the use of fusion tags. Curr. Opin. Biotechnol. 17:353-358.
    • (2006) Curr. Opin. Biotechnol. , vol.17 , pp. 353-358
    • Esposito, D.1    Chatterjee, D.K.2
  • 18
    • 18144362764 scopus 로고    scopus 로고
    • The soluble expression of the human renin binding protein using fusion partners: A comparison of ubiquitin, thioredoxin, maltose binding protein, and NusA
    • Lee, C., S. G. Lee, and S. Takahashi (2003) The soluble expression of the human renin binding protein using fusion partners: A comparison of ubiquitin, thioredoxin, maltose binding protein, and NusA. Biotechnol. Bioprocess Eng. 8:89-93.
    • (2003) Biotechnol. Bioprocess Eng. , vol.8 , pp. 89-93
    • Lee, C.1    Lee, S.G.2    Takahashi, S.3
  • 19
    • 0036905705 scopus 로고    scopus 로고
    • Mechanisms of protein folding: Molecular chaperones and their application in biotechnology
    • Mogk, A., M. P. Mayer, and E. Deuerling (2002) Mechanisms of protein folding: Molecular chaperones and their application in biotechnology. Chembiochem. 3:807-814.
    • (2002) Chembiochem. , vol.3 , pp. 807-814
    • Mogk, A.1    Mayer, M.P.2    Deuerling, E.3
  • 21
    • 0033920414 scopus 로고    scopus 로고
    • Production of interferon-α in high cell density cultures of recombinant Escherichia coli and its single step purification from refolded inclusion body proteins
    • Babu, K. R., S. Swaminathan, S. Marten, N. Khanna, and U. Rinas (2000) Production of interferon-α in high cell density cultures of recombinant Escherichia coli and its single step purification from refolded inclusion body proteins. Appl. Microbiol. Biotechnol. 53:655-660.
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 655-660
    • Babu, K.R.1    Swaminathan, S.2    Marten, S.3    Khanna, N.4    Rinas, U.5
  • 23
    • 0141831834 scopus 로고    scopus 로고
    • Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli
    • Panda, A. K. (2003) Bioprocessing of therapeutic proteins from the inclusion bodies of Escherichia coli. Adv. Biochem. Eng. Biotechnol. 85:43-93.
    • (2003) Adv. Biochem. Eng. Biotechnol. , vol.85 , pp. 43-93
    • Panda, A.K.1
  • 24
    • 0032874214 scopus 로고    scopus 로고
    • Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone
    • Panda, A. K., R. H. Khan, K. B. C. Appa Rao, and S. M. Totey (1999) Kinetics of inclusion body production in batch and high cell density fed-batch culture of Escherichia coli expressing ovine growth hormone. J. Biotechnol. 75:161-172.
    • (1999) J. Biotechnol. , vol.75 , pp. 161-172
    • Panda, A.K.1    Khan, R.H.2    Appa Rao, K.B.C.3    Totey, S.M.4
  • 25
    • 0032970060 scopus 로고    scopus 로고
    • Temperature-induced production of recombinant human insulin in high-cell density cultures of recombinant Escherichia coli
    • Schmidt, M., K. R. Babu, N. Khanna, S. Marten, and U. Rinas (1999) Temperature-induced production of recombinant human insulin in high-cell density cultures of recombinant Escherichia coli. J. Biotechnol. 68:71-83.
    • (1999) J. Biotechnol. , vol.68 , pp. 71-83
    • Schmidt, M.1    Babu, K.R.2    Khanna, N.3    Marten, S.4    Rinas, U.5
  • 26
    • 19644389665 scopus 로고    scopus 로고
    • Solubilization and refolding of bacterial inclusion body proteins
    • Singh, S. M. and A. K. Panda (2005) Solubilization and refolding of bacterial inclusion body proteins. J. Biosci. Bioeng. 99:303-310.
    • (2005) J. Biosci. Bioeng. , vol.99 , pp. 303-310
    • Singh, S.M.1    Panda, A.K.2
  • 27
    • 0037187447 scopus 로고    scopus 로고
    • Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli
    • Vallejo, L. F., M. Brokelmann, S. Marten, S. Trappe, J. Cabrera-Crespo, A. Hoffmann, G. Gross, H. A. Weich, and U. Rinas (2002) Renaturation and purification of bone morphogenetic protein-2 produced as inclusion bodies in high-cell-density cultures of recombinant Escherichia coli. J. Biotechnol. 94:185-194.
    • (2002) J. Biotechnol. , vol.94 , pp. 185-194
    • Vallejo, L.F.1    Brokelmann, M.2    Marten, S.3    Trappe, S.4    Cabrera-Crespo, J.5    Hoffmann, A.6    Gross, G.7    Weich, H.A.8    Rinas, U.9
  • 28
    • 0033572725 scopus 로고    scopus 로고
    • Effects of macromolecular crowding on protein folding and aggregation
    • van den Berg, B., R. J. Ellis, and C. M. Dobson (1999) Effects of macromolecular crowding on protein folding and aggregation. EMBO J. 18:6927-6933.
    • (1999) EMBO J. , vol.18 , pp. 6927-6933
    • van den Berg, B.1    Ellis, R.J.2    Dobson, C.M.3
  • 29
    • 23944489637 scopus 로고    scopus 로고
    • Effect of substrate feed rate on recombinant protein secretion, degradation and inclusion body formation in Escherichia coli
    • Boström, M., K. Markland, A. M. Sandén, M. Hedhammar, S. Hober, and G. Larsson (2005) Effect of substrate feed rate on recombinant protein secretion, degradation and inclusion body formation in Escherichia coli. Appl. Microbiol. Biotechnol. 68:82-90.
    • (2005) Appl. Microbiol. Biotechnol. , vol.68 , pp. 82-90
    • Boström, M.1    Markland, K.2    Sandén, A.M.3    Hedhammar, M.4    Hober, S.5    Larsson, G.6
  • 30
    • 30944434224 scopus 로고    scopus 로고
    • Production of an active recombinant Aspin antigen in Escherichia coli for identifying animals resistant to nematode infection
    • Manderson, D., R. Dempster, and Y. Chisti (2006) Production of an active recombinant Aspin antigen in Escherichia coli for identifying animals resistant to nematode infection. Enzyme Microb. Technol. 38:591-598.
    • (2006) Enzyme Microb. Technol. , vol.38 , pp. 591-598
    • Manderson, D.1    Dempster, R.2    Chisti, Y.3
  • 31
    • 17744363459 scopus 로고    scopus 로고
    • Solubility and proteolysis of the Zb-MalE and Zb-MalE31 proteins during overproduction in Escherichia coli
    • Sandén, A. M., M. Boström, K. Markland, and G. Larsson (2005) Solubility and proteolysis of the Zb-MalE and Zb-MalE31 proteins during overproduction in Escherichia coli. Biotechnol. Bioeng. 90:239-247.
    • (2005) Biotechnol. Bioeng. , vol.90 , pp. 239-247
    • Sandén, A.M.1    Boström, M.2    Markland, K.3    Larsson, G.4
  • 32
    • 1542374718 scopus 로고    scopus 로고
    • Production of the kringle fragments of human apolipoprotein(a) by continuous lactose induction strategy
    • Lim, H.-K., S.-G. Kim, K.-H. Jung, and J.-H. Seo (2004) Production of the kringle fragments of human apolipoprotein(a) by continuous lactose induction strategy. J. Biotechnol. 108:271-278.
    • (2004) J. Biotechnol. , vol.108 , pp. 271-278
    • Lim, H.-K.1    Kim, S.-G.2    Jung, K.-H.3    Seo, J.-H.4
  • 33
    • 46749083949 scopus 로고    scopus 로고
    • Enhanced enzyme activities of inclusion bodies of recombinant β-galactosidase via the addition of inducer analog after L-arabinose induction in the araBAD promoter system of Escherichia coli
    • Jung, K.-H. (2008) Enhanced enzyme activities of inclusion bodies of recombinant β-galactosidase via the addition of inducer analog after L-arabinose induction in the araBAD promoter system of Escherichia coli. J. Microbiol. Biotechnol. 18:434-442.
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 434-442
    • Jung, K.-H.1
  • 34
    • 46949107249 scopus 로고    scopus 로고
    • Methyl α-D-glucopyranoside enhances the enzymatic activity of recombinant β-galactosidase inclusion bodies in the araBAD promoter system of Escherichia coli
    • Jung, K.-H., J.-H. Yeon, S.-K. Moon, and J. H. Choi (2008) Methyl α-D-glucopyranoside enhances the enzymatic activity of recombinant β-galactosidase inclusion bodies in the araBAD promoter system of Escherichia coli. J. Ind. Microbiol. Biotechnol. 35:695-701.
    • (2008) J. Ind. Microbiol. Biotechnol. , vol.35 , pp. 695-701
    • Jung, K.-H.1    Yeon, J.-H.2    Moon, S.-K.3    Choi, J.H.4
  • 35
    • 36948999407 scopus 로고    scopus 로고
    • Modulation of the tendency towards inclusion body formation of recombinant protein by the addition of glucose in the araBAD promoter system of Escherichia coli
    • Lee, Y.-J. and K.-H. Jung (2007) Modulation of the tendency towards inclusion body formation of recombinant protein by the addition of glucose in the araBAD promoter system of Escherichia coli. J. Microbiol. Biotechnol. 17:1898-1903.
    • (2007) J. Microbiol. Biotechnol. , vol.17 , pp. 1898-1903
    • Lee, Y.-J.1    Jung, K.-H.2
  • 36
    • 0029018327 scopus 로고
    • Tight regulation, modulation, and high-level expression by vectors containing the arabinose P BAD promoter
    • Guzman, L. M., D. Belin, M. J. Carson, and J. Beckwith (1995) Tight regulation, modulation, and high-level expression by vectors containing the arabinose P BAD promoter. J. Bacteriol. 177:4121-4130.
    • (1995) J. Bacteriol. , vol.177 , pp. 4121-4130
    • Guzman, L.M.1    Belin, D.2    Carson, M.J.3    Beckwith, J.4
  • 37
    • 0033580277 scopus 로고    scopus 로고
    • Broad-host-range expression vectors that carry the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator
    • Newman, J. R. and C. Fuqua (1999) Broad-host-range expression vectors that carry the L-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator. Gene 227:197-203.
    • (1999) Gene , vol.227 , pp. 197-203
    • Newman, J.R.1    Fuqua, C.2
  • 38
    • 0037186259 scopus 로고    scopus 로고
    • Flow cytometry as a useful tool for process development: Rapid evaluation of expression systems
    • Patkar, A., N. Vijayasankaran, D. W. Urry, and F. Srienc (2002) Flow cytometry as a useful tool for process development: Rapid evaluation of expression systems. J. Biotechnol. 93:217-229.
    • (2002) J. Biotechnol. , vol.93 , pp. 217-229
    • Patkar, A.1    Vijayasankaran, N.2    Urry, D.W.3    Srienc, F.4
  • 39
    • 0033987659 scopus 로고    scopus 로고
    • Generation of an AraC-araBAD promoter-regulated T7 expression system
    • Wycuff, D. R. and K. S. Matthews (2002) Generation of an AraC-araBAD promoter-regulated T7 expression system. Anal. Biochem. 277:67-73.
    • (2002) Anal. Biochem. , vol.277 , pp. 67-73
    • Wycuff, D.R.1    Matthews, K.S.2
  • 40
    • 0015957493 scopus 로고
    • Mutations in the L-arabinose operon of Escherichia coli B/r that results in hypersensitivity to catabolite repression
    • Gendron, R. P. and D. E. Sheppard (1974) Mutations in the L-arabinose operon of Escherichia coli B/r that results in hypersensitivity to catabolite repression. J. Bacteriol. 117:417-421.
    • (1974) J. Bacteriol. , vol.117 , pp. 417-421
    • Gendron, R.P.1    Sheppard, D.E.2
  • 41
    • 0014789269 scopus 로고
    • Physiological basis of transient repression of catabolite enzymes in Escherichia coli
    • Tyler, B. and B. Magasanik (1970) Physiological basis of transient repression of catabolite enzymes in Escherichia coli. J. Bacteriol. 102:411-422.
    • (1970) J. Bacteriol. , vol.102 , pp. 411-422
    • Tyler, B.1    Magasanik, B.2
  • 42
    • 0342656712 scopus 로고    scopus 로고
    • Effect of glucose analog supplementation on metabolic flux distribution in ananerobic chemostat cultures of Escherichia coli
    • Barríos-Rivera, S. J., Y. T. Yang, G. N. Bennett, and K. Y. San (2000) Effect of glucose analog supplementation on metabolic flux distribution in ananerobic chemostat cultures of Escherichia coli. Metabolic Eng. 2:149-154.
    • (2000) Metabolic Eng. , vol.2 , pp. 149-154
    • Barríos-Rivera, S.J.1    Yang, Y.T.2    Bennett, G.N.3    San, K.Y.4
  • 43
    • 0028535143 scopus 로고
    • Effect of modulated glucose uptake on high-level recombinant protein production in a dense Escherichia coli culture
    • Chou, C. H., G. N. Bennett, and K. Y. San (1994) Effect of modulated glucose uptake on high-level recombinant protein production in a dense Escherichia coli culture. Biotechnol. Prog. 10:644-647.
    • (1994) Biotechnol. Prog. , vol.10 , pp. 644-647
    • Chou, C.H.1    Bennett, G.N.2    San, K.Y.3
  • 44
    • 33344463263 scopus 로고    scopus 로고
    • Continuous production of recombinant interferon-α in Escherichia coli via the derepression of trp promoter using casamino acid
    • Jung, K.-H. (2006) Continuous production of recombinant interferon-α in Escherichia coli via the derepression of trp promoter using casamino acid. Process Biochem. 41:809-814.
    • (2006) Process Biochem. , vol.41 , pp. 809-814
    • Jung, K.-H.1
  • 45
    • 34548045980 scopus 로고    scopus 로고
    • A strategy for high-level expression of soluble and functional human interferon alpha as a GST-fusion protein in E. coli
    • Rabhi-Essafi, I., A. Sadok, N. Khalaf, and D. M. Fathallah (2007) A strategy for high-level expression of soluble and functional human interferon alpha as a GST-fusion protein in E. coli. Protein Eng. Des. Sel. 20:201-209.
    • (2007) Protein Eng. Des. Sel. , vol.20 , pp. 201-209
    • Rabhi-Essafi, I.1    Sadok, A.2    Khalaf, N.3    Fathallah, D.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.