메뉴 건너뛰기




Volumn 35, Issue 9, 2000, Pages 1019-1025

Process strategies to improve heterologous protein production in Escherichia coli under lactose or IPTG induction

Author keywords

Escherichia coli; Heterologous protein; Isopropyl D thiogalactoside; Lac UV5; Lactose; Protein stability

Indexed keywords

LACTOSE; PROTEIN; THIOGLYCOSIDE; TROPONIN C;

EID: 17544384549     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0032-9592(00)00137-0     Document Type: Article
Times cited : (56)

References (37)
  • 1
    • 0025264582 scopus 로고
    • Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations
    • Luli G.W., Strohl W.R. Comparison of growth, acetate production, and acetate inhibition of Escherichia coli strains in batch and fed-batch fermentations. Appl. Environ. Microbiol. 56:1990;1004-1011.
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 1004-1011
    • Luli, G.W.1    Strohl, W.R.2
  • 2
    • 0025700668 scopus 로고
    • Production of recombinant human growth hormone in Escherichia coli: Expression of different precursors and physiological effects of glucose, acetate and salts
    • Jensen E.B., Carlsen S. Production of recombinant human growth hormone in Escherichia coli: expression of different precursors and physiological effects of glucose, acetate and salts. Biotechnol. Bioeng. 36:1990;1-11.
    • (1990) Biotechnol. Bioeng. , vol.36 , pp. 1-11
    • Jensen, E.B.1    Carlsen, S.2
  • 3
    • 0027112178 scopus 로고
    • Fed-batch culture automated by uses of continuously measured cell concentration and culture volume
    • Yamane T., Hibino W., Ishiara K., Kadotani Y., Kominami M. Fed-batch culture automated by uses of continuously measured cell concentration and culture volume. Biotechnol. Bioeng. 39:1992;550-555.
    • (1992) Biotechnol. Bioeng. , vol.39 , pp. 550-555
    • Yamane, T.1    Hibino, W.2    Ishiara, K.3    Kadotani, Y.4    Kominami, M.5
  • 4
    • 0027015640 scopus 로고
    • Recombinant protein expression in high cell density fed-batch cultures of Escherichia coli
    • Yee L., Blanch H.W. Recombinant protein expression in high cell density fed-batch cultures of Escherichia coli. Biotechnology. 10:1992;1550-1556.
    • (1992) Biotechnology , vol.10 , pp. 1550-1556
    • Yee, L.1    Blanch, H.W.2
  • 5
    • 0031162086 scopus 로고    scopus 로고
    • A simple way of achieving high cell concentration in recombinant Escherichia coli cultivation
    • Gombert A.K., Kilikian B.V. A simple way of achieving high cell concentration in recombinant Escherichia coli cultivation. Braz. J. Chem. Eng. 14:1997;185-190.
    • (1997) Braz. J. Chem. Eng. , vol.14 , pp. 185-190
    • Gombert, A.K.1    Kilikian, B.V.2
  • 6
    • 0032484705 scopus 로고    scopus 로고
    • Proposed mechanism of acetate accumulation in two recombinant Escherichia coli strains during high density fermentation
    • van deWalle M., Shiloach J. Proposed mechanism of acetate accumulation in two recombinant Escherichia coli strains during high density fermentation. Biotechnol. Bioeng. 57:1998;71-78.
    • (1998) Biotechnol. Bioeng. , vol.57 , pp. 71-78
    • Van Dewalle, M.1    Shiloach, J.2
  • 7
    • 0029328409 scopus 로고
    • Metabolic engineering of Escherichia coli to enhance recombinant protein production through acetate reduction
    • Aristidou A.A., San K.Y., Bennett G.N. Metabolic engineering of Escherichia coli to enhance recombinant protein production through acetate reduction. Biotechnol. Prog. 11:1995;475-478.
    • (1995) Biotechnol. Prog. , vol.11 , pp. 475-478
    • Aristidou, A.A.1    San, K.Y.2    Bennett, G.N.3
  • 8
    • 0032600903 scopus 로고    scopus 로고
    • Metabolic flux analysis of Escherichia coli deficient in the acetate production pathway and expressing the Bacillus subtilis acetolactate synthase
    • Yang Y.-T., Aristidou A.A., San K.-Y., Bennett G.N. Metabolic flux analysis of Escherichia coli deficient in the acetate production pathway and expressing the Bacillus subtilis acetolactate synthase. Metab. Eng. 1:1999;26-34.
    • (1999) Metab. Eng. , vol.1 , pp. 26-34
    • Yang, Y.-T.1    Aristidou, A.A.2    San, K.-Y.3    Bennett, G.N.4
  • 9
    • 0028533566 scopus 로고
    • Recent developments in heterologous protein production in Escherichia coli
    • Hockney R.C. Recent developments in heterologous protein production in Escherichia coli. TIBTECH. 12:1994;456-463.
    • (1994) TIBTECH , vol.12 , pp. 456-463
    • Hockney, R.C.1
  • 10
    • 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., Robinson C.W., Glick B.R. Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter. J. Ind. Microbiol. 16:1996;145-154.
    • (1996) J. Ind. Microbiol. , vol.16 , pp. 145-154
    • Donovan, R.S.1    Robinson, C.W.2    Glick, B.R.3
  • 11
    • 0345491422 scopus 로고    scopus 로고
    • Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli strain
    • Park S.J., Georgiou G., Lee Y.S. Secretory production of recombinant protein by a high cell density culture of a protease negative mutant Escherichia coli strain. Biotechnol. Prog. 15:1999;164-167.
    • (1999) Biotechnol. Prog. , vol.15 , pp. 164-167
    • Park, S.J.1    Georgiou, G.2    Lee, Y.S.3
  • 12
    • 0026510132 scopus 로고
    • Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as inducer
    • Neubauer P., Hofmann K., Holst O., Matiasson B., Kruschke P. Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as inducer. Appl. Microbiol. Biotechnol. 36:1992;739-744.
    • (1992) Appl. Microbiol. Biotechnol. , vol.36 , pp. 739-744
    • Neubauer, P.1    Hofmann, K.2    Holst, O.3    Matiasson, B.4    Kruschke, P.5
  • 13
    • 0031002603 scopus 로고    scopus 로고
    • Enhanced fitness of a recombinant protein synthesis in the stationary phase of Escherichia coli batch cultures
    • Vila P., Corchero J.L., Cubarsi R., Villaverde A. Enhanced fitness of a recombinant protein synthesis in the stationary phase of Escherichia coli batch cultures. Biotechnol. Lett. 19:1997;225-228.
    • (1997) Biotechnol. Lett. , vol.19 , pp. 225-228
    • Vila, P.1    Corchero, J.L.2    Cubarsi, R.3    Villaverde, A.4
  • 14
    • 0026417070 scopus 로고
    • Effect of chemically-induced cloned gene expression on protein synthesis in E. coli
    • Wood T.K., Peretti S.W. Effect of chemically-induced cloned gene expression on protein synthesis in E. coli. Biotechnol. Bioeng. 38:1991;397-412.
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 397-412
    • Wood, T.K.1    Peretti, S.W.2
  • 15
    • 0032484884 scopus 로고    scopus 로고
    • Recombinant gene expression in Escherichia coli cultivation using lactose as inducer
    • Gombert A.K., Kilikian B.V. Recombinant gene expression in Escherichia coli cultivation using lactose as inducer. J. Biotechnol. 60:1998;47-54.
    • (1998) J. Biotechnol. , vol.60 , pp. 47-54
    • Gombert, A.K.1    Kilikian, B.V.2
  • 16
    • 0025397848 scopus 로고
    • Effect of preinduction specific growth rate on recombinant alpha consensus interferon synthesis in Escherichia coli
    • Curless C., Pope J., Tsai L. Effect of preinduction specific growth rate on recombinant alpha consensus interferon synthesis in Escherichia coli. Biotechnol. Prog. 6:1990;149-152.
    • (1990) Biotechnol. Prog. , vol.6 , pp. 149-152
    • Curless, C.1    Pope, J.2    Tsai, L.3
  • 18
    • 0023277714 scopus 로고
    • Effects of fermentation feeding strategies prior to induction of expression of a recombinant malaria antigen in Escherichia coli
    • Zabriskie D.W., Warenheim D.A., Polansky M.J. Effects of fermentation feeding strategies prior to induction of expression of a recombinant malaria antigen in Escherichia coli. J. Ind. Microbiol. 2:1987;87-95.
    • (1987) J. Ind. Microbiol. , vol.2 , pp. 87-95
    • Zabriskie, D.W.1    Warenheim, D.A.2    Polansky, M.J.3
  • 19
    • 0028799815 scopus 로고
    • Enhancement of recombinant cholera toxin B subunit production in Escherichia coli by applying a fed-batch control strategy
    • Mendoza-Vega O., Buri E., Speck D. Enhancement of recombinant cholera toxin B subunit production in Escherichia coli by applying a fed-batch control strategy. Biotechnol. Lett. 17:1995;1037-1042.
    • (1995) Biotechnol. Lett. , vol.17 , pp. 1037-1042
    • Mendoza-Vega, O.1    Buri, E.2    Speck, D.3
  • 20
    • 0028408082 scopus 로고
    • Fed-batch operation of recombinant Escherichia coli containing trp promoter with controlled specific growth rate
    • Yoon S.K., Kang W.K., Park T.H. Fed-batch operation of recombinant Escherichia coli containing trp promoter with controlled specific growth rate. Biotechnol. Bioeng. 43:1994;995-999.
    • (1994) Biotechnol. Bioeng. , vol.43 , pp. 995-999
    • Yoon, S.K.1    Kang, W.K.2    Park, T.H.3
  • 21
    • 0026675533 scopus 로고
    • Control of proteolysis in fermentation of recombinant proteins
    • Enfors S.-O. Control of proteolysis in fermentation of recombinant proteins. TIBTECH. 10:1992;310-315.
    • (1992) TIBTECH , vol.10 , pp. 310-315
    • Enfors, S.-O.1
  • 22
    • 0033586454 scopus 로고    scopus 로고
    • Stabilization of a proteolytically sensitive cytoplasmic recombinant protein during transition to downstream processing
    • Rozkov A., Enfors S.-O. Stabilization of a proteolytically sensitive cytoplasmic recombinant protein during transition to downstream processing. Biotechnol. Bioeng. 62:1999;730-738.
    • (1999) Biotechnol. Bioeng. , vol.62 , pp. 730-738
    • Rozkov, A.1    Enfors, S.-O.2
  • 23
    • 0028801765 scopus 로고
    • Metabolic load and heterologous gene expression
    • Glick B.R. Metabolic load and heterologous gene expression. Biotechnol. Adv. 13:1995;247-261.
    • (1995) Biotechnol. Adv. , vol.13 , pp. 247-261
    • Glick, B.R.1
  • 25
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffat B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130.
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffat, B.A.2
  • 26
    • 0027197251 scopus 로고
    • Cloning and expression of chicken skeletal muscle troponin I in Escherichia coli: The role of rare codons on the expression level
    • Quaggio R.B., Ferro J.A., Monteiro P.B., Reinach F.C. Cloning and expression of chicken skeletal muscle troponin I in Escherichia coli: the role of rare codons on the expression level. Protein Sci. 2:1993;1053-1056.
    • (1993) Protein Sci. , vol.2 , pp. 1053-1056
    • Quaggio, R.B.1    Ferro, J.A.2    Monteiro, P.B.3    Reinach, F.C.4
  • 27
    • 0031849591 scopus 로고    scopus 로고
    • Effect of yeast extract on Escherichia coli growth and acetic acid production
    • Suárez D.C., Liria C.W., Kilikian B.V. Effect of yeast extract on Escherichia coli growth and acetic acid production. World J. Microbiol. Biotechnol. 14:1998;331-335.
    • (1998) World J. Microbiol. Biotechnol. , vol.14 , pp. 331-335
    • Suárez, D.C.1    Liria, C.W.2    Kilikian, B.V.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0343680821 scopus 로고    scopus 로고
    • Kinetics of a recombinant protein production by E. coli BL21
    • Liria C.W., Kilikian B.V. Kinetics of a recombinant protein production by E. coli BL21. Rev. Microbiol. 28:1997;172-178.
    • (1997) Rev. Microbiol. , vol.28 , pp. 172-178
    • Liria, C.W.1    Kilikian, B.V.2
  • 31
    • 0343196718 scopus 로고    scopus 로고
    • Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21 (DE3) [pET-3aT2M2]
    • Chin C.S., Hong M.S., Bae C.S., Lee J. Enhanced production of human mini-proinsulin in fed-batch cultures at high cell density of Escherichia coli BL21 (DE3) [pET-3aT2M2]. Biotechnol. Prog. 13:1997;249-257.
    • (1997) Biotechnol. Prog. , vol.13 , pp. 249-257
    • Chin, C.S.1    Hong, M.S.2    Bae, C.S.3    Lee, J.4
  • 32
    • 0026608065 scopus 로고
    • Isopropyl-β-thiogalactopyranoside influences the metabolism of Escherichia coli
    • Kosinski M.J., Rinas U., Bailey J. Isopropyl-β-thiogalactopyranoside influences the metabolism of Escherichia coli. Appl. Microbiol. Biotechnol. 36:1992;782-784.
    • (1992) Appl. Microbiol. Biotechnol. , vol.36 , pp. 782-784
    • Kosinski, M.J.1    Rinas, U.2    Bailey, J.3
  • 34
    • 0027112852 scopus 로고
    • Overexpression of cloned genes using recombinant Escherichia coli regulated by a T7 promoter. 1. Batch cultures and kinetic modeling
    • Miao F., Kompala D.S. Overexpression of cloned genes using recombinant Escherichia coli regulated by a T7 promoter. 1. Batch cultures and kinetic modeling. Biotechnol. Bioeng. 40:1992;787-796.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 787-796
    • Miao, F.1    Kompala, D.S.2
  • 35
    • 0029379752 scopus 로고
    • Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21 (DE3): Process control yielding high levels of metal-incorporated soluble protein
    • Hoffman B.J., Broadwater J.A., Johnson P., Harper J., Fox B.G., Kenealy W.R. Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21 (DE3): process control yielding high levels of metal-incorporated soluble protein. Protein Expression Purification. 6:1995;646-654.
    • (1995) Protein Expression Purification , vol.6 , pp. 646-654
    • Hoffman, B.J.1    Broadwater, J.A.2    Johnson, P.3    Harper, J.4    Fox, B.G.5    Kenealy, W.R.6
  • 36
    • 0028901398 scopus 로고
    • Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases
    • Martinez A., Krappskreg P.M., Olafsdottir S., Doskeland A.P., Eiken H.G., Screbak R.M., Apold J., Flatmark T. Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Biochem. J. 306:1995;589-597.
    • (1995) Biochem. J. , vol.306 , pp. 589-597
    • Martinez, A.1    Krappskreg, P.M.2    Olafsdottir, S.3    Doskeland, A.P.4    Eiken, H.G.5    Screbak, R.M.6    Apold, J.7    Flatmark, T.8
  • 37
    • 0032007853 scopus 로고    scopus 로고
    • Strategies for optimizing heterologous protein expression in Escherichia coli
    • Hannig G., Makrides S.C. Strategies for optimizing heterologous protein expression in Escherichia coli. TIBTECH. 16:1998;54-60.
    • (1998) TIBTECH , vol.16 , pp. 54-60
    • Hannig, G.1    Makrides, S.C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.