메뉴 건너뛰기




Volumn 13, Issue 1, 2008, Pages 7-13

Optimization of human interferon gamma production in Escherichia coli by response surface methodology

Author keywords

Escherichia coli BL21 SI; Minimum medium; Synthetic gene; Therapeutic protein

Indexed keywords

RECOMBINANT GAMMA INTERFERON; SODIUM CHLORIDE; SYNTHETIC DNA;

EID: 40549087966     PISSN: 12268372     EISSN: None     Source Type: Journal    
DOI: 10.1007/s12257-007-0126-5     Document Type: Article
Times cited : (13)

References (38)
  • 1
    • 0344664014 scopus 로고    scopus 로고
    • Over-expression of recombinant human interferon-gamma in high cell density fermentation of Escherichia coli
    • Khalilzadeh, R., S. A. Shojaosadati, A. Bahrami, and N. Maghsoudi (2003) Over-expression of recombinant human interferon-gamma in high cell density fermentation of Escherichia coli. Biotechnol. Lett. 25: 1989-1992.
    • (2003) Biotechnol. Lett , vol.25 , pp. 1989-1992
    • Khalilzadeh, R.1    Shojaosadati, S.A.2    Bahrami, A.3    Maghsoudi, N.4
  • 2
    • 0842266786 scopus 로고    scopus 로고
    • Interferon-γ: An overview of signals, mechanisms and functions
    • Schroder, K., P. J. Hertzog, T. Ravasi, and D. A. Hume (2004) Interferon-γ: an overview of signals, mechanisms and functions. J. Leukoc. Biol. 75: 163-189.
    • (2004) J. Leukoc. Biol , vol.75 , pp. 163-189
    • Schroder, K.1    Hertzog, P.J.2    Ravasi, T.3    Hume, D.A.4
  • 3
    • 14844348752 scopus 로고    scopus 로고
    • Whiteside, T. L. (2005) IFN-γ: Detection and prevention of release. Curr. Med. Chem. Anti Inflamm. Anti Allergy Agents. 4: 121-131.
    • Whiteside, T. L. (2005) IFN-γ: Detection and prevention of release. Curr. Med. Chem. Anti Inflamm. Anti Allergy Agents. 4: 121-131.
  • 4
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides, S. C. (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol. Rev. 60: 512-538.
    • (1996) Microbiol. Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 5
    • 0035313153 scopus 로고    scopus 로고
    • Advances in Escherichia coli production of therapeutic proteins
    • Swartz, J. R. (2001) Advances in Escherichia coli production of therapeutic proteins. Curr. Opin. Biotechnol. 12: 195-201.
    • (2001) Curr. Opin. Biotechnol , vol.12 , pp. 195-201
    • Swartz, J.R.1
  • 6
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression systems in the pharmaceutical industry
    • Schmidt, F. R. (2004) Recombinant expression systems in the pharmaceutical industry. Appl. Microbiol. Biotechnol. 65: 363-372.
    • (2004) Appl. Microbiol. Biotechnol , vol.65 , pp. 363-372
    • Schmidt, F.R.1
  • 7
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by autoinduction in high density shaking cultures
    • Studier, F. W. (2005) Protein production by autoinduction in high density shaking cultures. Protein Expr. Purif. 41: 207-234.
    • (2005) Protein Expr. Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 8
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig, G. and S. C. Makrides (1998) Strategies for optimizing heterologous protein expression in Escherichia coli. Trends Biotechnol. 16: 54-60.
    • (1998) Trends Biotechnol , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2
  • 9
    • 18844362113 scopus 로고    scopus 로고
    • Strategies for efficient production of heterologous proteins in Escherichia coli
    • Jana, S. and J. K. Deb (2005) Strategies for efficient production of heterologous proteins in Escherichia coli. Appl. Microbiol. Biotechnol. 67: 289-298.
    • (2005) Appl. Microbiol. Biotechnol , vol.67 , pp. 289-298
    • Jana, S.1    Deb, J.K.2
  • 10
    • 33646582374 scopus 로고    scopus 로고
    • The synthetic gene designer: A flexible web platform to explore sequence manipulation for heterologous expression
    • Wu, G., N. Bashir-Bello, and S. J. Freeland (2006) The synthetic gene designer: A flexible web platform to explore sequence manipulation for heterologous expression. Protein Expr. Purif. 47: 441-445.
    • (2006) Protein Expr. Purif , vol.47 , pp. 441-445
    • Wu, G.1    Bashir-Bello, N.2    Freeland, S.J.3
  • 11
    • 13844281604 scopus 로고    scopus 로고
    • Optimizing medium composition for TaqI endonuclease production by recombinant Escherichia coli cells using response surface methodology
    • Nikerel, I. E., E. Toksoy, B. Kirdar, and R. Yildirim (2005) Optimizing medium composition for TaqI endonuclease production by recombinant Escherichia coli cells using response surface methodology. Process Biochem. 40: 1633-1639.
    • (2005) Process Biochem , vol.40 , pp. 1633-1639
    • Nikerel, I.E.1    Toksoy, E.2    Kirdar, B.3    Yildirim, R.4
  • 12
    • 34447280837 scopus 로고    scopus 로고
    • Optimization of medium of components for plasmid production by recombinant E. coli DH5α pUK21CMVβ1.2
    • Zheng, S., K. Friehs, N. He, X. Deng, Q. Li, Z. He, C. Xu, and Y. Lu (2007) Optimization of medium of components for plasmid production by recombinant E. coli DH5α pUK21CMVβ1.2. Biotechnol. Bioprocess Eng. 12: 213-221.
    • (2007) Biotechnol. Bioprocess Eng , vol.12 , pp. 213-221
    • Zheng, S.1    Friehs, K.2    He, N.3    Deng, X.4    Li, Q.5    He, Z.6    Xu, C.7    Lu, Y.8
  • 13
    • 0347753711 scopus 로고    scopus 로고
    • Production of recombinant serpins in Escherichia coli
    • Bird, P. I., S. C. Pak, D. M. Worrall, and S. P. Bottomley (2004) Production of recombinant serpins in Escherichia coli. Methods 32: 169-176.
    • (2004) Methods , vol.32 , pp. 169-176
    • Bird, P.I.1    Pak, S.C.2    Worrall, D.M.3    Bottomley, S.P.4
  • 14
    • 33747834066 scopus 로고    scopus 로고
    • Optimization and high-level expression of a functional GST-tagged rHLT-B in Escherichia coli and GM1 binding ability of purified rHLT-B
    • Ma, X., W. Zheng, T. Wang, D. Wei, and Y. Ma (2006) Optimization and high-level expression of a functional GST-tagged rHLT-B in Escherichia coli and GM1 binding ability of purified rHLT-B. J. Microbiol. 44: 293-300.
    • (2006) J. Microbiol , vol.44 , pp. 293-300
    • Ma, X.1    Zheng, W.2    Wang, T.3    Wei, D.4    Ma, Y.5
  • 15
    • 46949087369 scopus 로고    scopus 로고
    • Modeling and optimization I: Usability of response surface methodology
    • Baş, D. and I. H. Boyacy (2007) Modeling and optimization I: Usability of response surface methodology. J. Food Eng. 78: 836-845.
    • (2007) J. Food Eng , vol.78 , pp. 836-845
    • Baş, D.1    Boyacy, I.H.2
  • 16
    • 0345669380 scopus 로고    scopus 로고
    • BL21-SI competent cells for protein expression in E. coli
    • Donahue, R. A., Jr. and R. L. Bebee (1999) BL21-SI competent cells for protein expression in E. coli. Focus 21: 49-51.
    • (1999) Focus , vol.21 , pp. 49-51
    • Donahue Jr., R.A.1    Bebee, R.L.2
  • 17
    • 84946657020 scopus 로고
    • Some new three level designs for the study of quantitative variables
    • Box, G. E. P. and D. W. Behnken (1960) Some new three level designs for the study of quantitative variables. Technometrics 2: 455-475.
    • (1960) Technometrics , vol.2 , pp. 455-475
    • Box, G.E.P.1    Behnken, D.W.2
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0028804911 scopus 로고
    • Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli
    • Kane, J. F. (1995) Effects of rare codon clusters on high-level expression of heterologous proteins in Escherichia coli. Curr. Opin. Biotechnol. 6: 494-500.
    • (1995) Curr. Opin. Biotechnol , vol.6 , pp. 494-500
    • Kane, J.F.1
  • 22
    • 0348013051 scopus 로고    scopus 로고
    • Hierarchy of sequence-dependent features associated with prokaryotic translation
    • Lithwick, G. and H. Margalit (2003) Hierarchy of sequence-dependent features associated with prokaryotic translation. Genome Res. 13: 2665-2673.
    • (2003) Genome Res , vol.13 , pp. 2665-2673
    • Lithwick, G.1    Margalit, H.2
  • 24
    • 0031006153 scopus 로고    scopus 로고
    • Bacterial expression and purification of biologically active mouse c-Fos proteins by selective codon optimization
    • Deng, T. (1997) Bacterial expression and purification of biologically active mouse c-Fos proteins by selective codon optimization. FEBS Lett. 409: 269-272.
    • (1997) FEBS Lett , vol.409 , pp. 269-272
    • Deng, T.1
  • 25
    • 0032030138 scopus 로고    scopus 로고
    • Codon optimization of the gene encoding a domain from human Type 1 neurofibromin protein results in a threefold improvement in expression level in Escherichia coli
    • Hale, R. S. and G. Thompson (1998) Codon optimization of the gene encoding a domain from human Type 1 neurofibromin protein results in a threefold improvement in expression level in Escherichia coli. Protein Expr. Purif. 12: 185-188.
    • (1998) Protein Expr. Purif , vol.12 , pp. 185-188
    • Hale, R.S.1    Thompson, G.2
  • 26
    • 0034687723 scopus 로고    scopus 로고
    • High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: Evidence for a C-terminal membrane binding domain
    • Feng, L., W. W. Chan, S. L. Roderick, and D. E. Cohen (2000) High-level expression and mutagenesis of recombinant human phosphatidylcholine transfer protein using a synthetic gene: evidence for a C-terminal membrane binding domain. Biochemistry 39: 15399-15409.
    • (2000) Biochemistry , vol.39 , pp. 15399-15409
    • Feng, L.1    Chan, W.W.2    Roderick, S.L.3    Cohen, D.E.4
  • 28
    • 1842581995 scopus 로고    scopus 로고
    • Codon optimization and mRNA amplification effectively enhances the immunogenicity of the hepatitis C virus nonstructural 3/4A gene
    • Frelin, L., G. Ahlen, M. Alheim, O. Weiland, C. Barnfield, P. Liljestrom, and M. Sallberg (2004) Codon optimization and mRNA amplification effectively enhances the immunogenicity of the hepatitis C virus nonstructural 3/4A gene. Gene Ther. 11: 522-533.
    • (2004) Gene Ther , vol.11 , pp. 522-533
    • Frelin, L.1    Ahlen, G.2    Alheim, M.3    Weiland, O.4    Barnfield, C.5    Liljestrom, P.6    Sallberg, M.7
  • 29
    • 34249332439 scopus 로고    scopus 로고
    • Paz Maldonado, L. M. T., V. E. B. Hernandez, E. M. Rivero, A. P. Barba de ka Rosa, J. L. Pores, L. G. O. Acevedo, and A. De León (2007) Optimization of culture conditions for a synthetic gene expression in Escherichia coli using response surface methodology: The case of human interferon beta. Biomol. Eng. 24: 217-222.
    • Paz Maldonado, L. M. T., V. E. B. Hernandez, E. M. Rivero, A. P. Barba de ka Rosa, J. L. Pores, L. G. O. Acevedo, and A. De León (2007) Optimization of culture conditions for a synthetic gene expression in Escherichia coli using response surface methodology: The case of human interferon beta. Biomol. Eng. 24: 217-222.
  • 30
    • 25644440059 scopus 로고    scopus 로고
    • Modelling of translation of human protein disulfide isomerase in Escherichia coli - A case study of gene optimization
    • Niemitalo, O., A. Neubauer, U. Liebal, J. Myllyharju, A. H. Juffer, and P. Neubauer (2005) Modelling of translation of human protein disulfide isomerase in Escherichia coli - A case study of gene optimization. J. Biotechnol. 120: 11-24.
    • (2005) J. Biotechnol , vol.120 , pp. 11-24
    • Niemitalo, O.1    Neubauer, A.2    Liebal, U.3    Myllyharju, J.4    Juffer, A.H.5    Neubauer, P.6
  • 31
    • 0030758194 scopus 로고    scopus 로고
    • An Escherichia coli host strain useful for efficient overproduction of cloned gene products with NaCl as the inducer
    • Bhandari, P. and J. Gowrishankar (1997) An Escherichia coli host strain useful for efficient overproduction of cloned gene products with NaCl as the inducer. J. Bacteriol. 179: 4403-4406.
    • (1997) J. Bacteriol , vol.179 , pp. 4403-4406
    • Bhandari, P.1    Gowrishankar, J.2
  • 32
    • 40549090189 scopus 로고    scopus 로고
    • Ling, H. (2002) Physiology of Escherichia coli in batch and fed-batch cultures with special emphasis on amino acid and glucose metabolism. Doctoral thesis. Department of Biotechnology, Royal Institute of Technology, Stockholm, Sweden (http://media.lib.kth.se:8080/ dissengrefhit.asp?dissnr=3334).
    • Ling, H. (2002) Physiology of Escherichia coli in batch and fed-batch cultures with special emphasis on amino acid and glucose metabolism. Doctoral thesis. Department of Biotechnology, Royal Institute of Technology, Stockholm, Sweden (http://media.lib.kth.se:8080/ dissengrefhit.asp?dissnr=3334).
  • 33
    • 0037315336 scopus 로고    scopus 로고
    • Improvement of posttranslational bottlenecks in the production of penicillin amidase in recombinant Escherichia coli strains
    • Ignatova, Z., A. Mahsunah, M. Georgieva, and V. Kasche (2003) Improvement of posttranslational bottlenecks in the production of penicillin amidase in recombinant Escherichia coli strains. Appl. Environ. Microbiol. 69: 1237-1245.
    • (2003) Appl. Environ. Microbiol , vol.69 , pp. 1237-1245
    • Ignatova, Z.1    Mahsunah, A.2    Georgieva, M.3    Kasche, V.4
  • 34
    • 0026510132 scopus 로고
    • Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as inducer
    • Neubauer, P., K. Hofmann, O. Holst, B. Mattiansson, and P. Kruschke (1992) Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as inducer. Appl. Microbiol. Biotechnol. 36: 739-744.
    • (1992) Appl. Microbiol. Biotechnol , vol.36 , pp. 739-744
    • Neubauer, P.1    Hofmann, K.2    Holst, O.3    Mattiansson, B.4    Kruschke, P.5
  • 35
    • 0029892121 scopus 로고    scopus 로고
    • Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter
    • Donovan, R. S., C. W. Robinson, and B. R. Glick (1996) Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter. J. Ind. Microbiol. 16: 145-154.
    • (1996) J. Ind. Microbiol , vol.16 , pp. 145-154
    • Donovan, R.S.1    Robinson, C.W.2    Glick, B.R.3
  • 36
    • 4344578159 scopus 로고    scopus 로고
    • Analysis of the expression of the Trichoderma harzianum ech42 gene in two isogenic clones of Escherichia coli by surface response methodology
    • De Léon, A., H. Jiménez-Islas, M. González-Cuevas, and A. P. Barba de la Rosa (2004) Analysis of the expression of the Trichoderma harzianum ech42 gene in two isogenic clones of Escherichia coli by surface response methodology. Process Biochem. 39: 2173-2178.
    • (2004) Process Biochem , vol.39 , pp. 2173-2178
    • De Léon, A.1    Jiménez-Islas, H.2    González-Cuevas, M.3    Barba de la Rosa, A.P.4
  • 37
    • 0026637585 scopus 로고
    • Production, purification and characterization of recombinant human interferon-γ
    • Zhang, Z., K. T. Tong, M. Belew, T. Pettersson, and J. C. Janson (1992) Production, purification and characterization of recombinant human interferon-γ. J. Chromatogr. 604: 143-155.
    • (1992) J. Chromatogr , vol.604 , pp. 143-155
    • Zhang, Z.1    Tong, K.T.2    Belew, M.3    Pettersson, T.4    Janson, J.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.