메뉴 건너뛰기




Volumn 38, Issue 3-4, 2006, Pages 465-469

Optimization of the overexpression of glutamate mutase S component under the control of T7 system by using lactose and IPTG as the inducers

Author keywords

Expression; Glutamate mutase S component; Lactose; T7 system

Indexed keywords

ESCHERICHIA COLI; GENETIC ENGINEERING; OPTIMIZATION; SUGARS;

EID: 28844474898     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.07.002     Document Type: Article
Times cited : (29)

References (18)
  • 2
    • 0024429732 scopus 로고
    • Production of soluble recombinant proteins in bacteria
    • C.H. Schein Production of soluble recombinant proteins in bacteria Biotechnology 7 1989 1141 1149
    • (1989) Biotechnology , vol.7 , pp. 1141-1149
    • Schein, C.H.1
  • 3
    • 0024851846 scopus 로고
    • Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments in Escherichia coli
    • S. Cabilly Growth at sub-optimal temperatures allows the production of functional, antigen-binding Fab fragments in Escherichia coli Gene 85 1989 553 557
    • (1989) Gene , vol.85 , pp. 553-557
    • Cabilly, S.1
  • 4
    • 0027263490 scopus 로고
    • Expression and mutation of soybean beta-amylase in Escherichia coli
    • A. Totsuka, and C. Fukazawa Expression and mutation of soybean beta-amylase in Escherichia coli Eur J Biochem 214 1993 787 794
    • (1993) Eur J Biochem , vol.214 , pp. 787-794
    • Totsuka, A.1    Fukazawa, C.2
  • 5
    • 8644268726 scopus 로고    scopus 로고
    • 6 dependent Clostridium sticklandii d-ornithine aminomutase in Escherichia coli
    • 6 dependent Clostridium sticklandii d-ornithine aminomutase in Escherichia coli Eur J Biochem 271 2004 4293 4297
    • (2004) Eur J Biochem , vol.271 , pp. 4293-4297
    • Chen, H.P.1    Hsui, F.C.2    Lin, L.Y.3    Ren, C.T.4    Wu, S.H.5
  • 6
    • 0026510132 scopus 로고
    • Maximizing the expression of a recombinant gene in Escherichia coli by manipulation of induction time using lactose as inducer
    • P. Neubauer, K. Hofmann, O. Holst, B. Mattiasson, and P. Kruschke 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    Mattiasson, B.4    Kruschke, P.5
  • 7
    • 0028307458 scopus 로고
    • Efficient use of lactose for the lac promoter-controlled overexpression of the main antigenic protein of the foot and mouth disease virus in Escherichia coli under fed-batch fermentation conditions
    • P. Neubauer, and K. Hofmann Efficient use of lactose for the lac promoter-controlled overexpression of the main antigenic protein of the foot and mouth disease virus in Escherichia coli under fed-batch fermentation conditions FEMS Microbiol Rev 14 1994 99 102
    • (1994) FEMS Microbiol Rev , vol.14 , pp. 99-102
    • Neubauer, P.1    Hofmann, K.2
  • 8
    • 0027301989 scopus 로고
    • Production of L-dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola
    • F. Foor, N. Morin, and K.A. Bostian Production of L- dihydroxyphenylalanine in Escherichia coli with the tyrosine phenol-lyase gene cloned from Erwinia herbicola Appl Environ Microbiol 59 1993 3070 3075
    • (1993) Appl Environ Microbiol , vol.59 , pp. 3070-3075
    • Foor, F.1    Morin, N.2    Bostian, K.A.3
  • 9
    • 0033668824 scopus 로고    scopus 로고
    • Use of lactose to induce expression of soluble NifA protein domains of Herbaspirillum seropedicae in Escherichia coli
    • R. Monteiro, E.M. Souza, M.G. Yates, F.O. Pedrosa, and L.S. Chubatsu Use of lactose to induce expression of soluble NifA protein domains of Herbaspirillum seropedicae in Escherichia coli Can J Microbiol 46 2000 1087 1090
    • (2000) Can J Microbiol , vol.46 , pp. 1087-1090
    • Monteiro, R.1    Souza, E.M.2    Yates, M.G.3    Pedrosa, F.O.4    Chubatsu, L.S.5
  • 10
    • 0026701740 scopus 로고
    • Cloning and sequencing of glutamate mutase component e from Clostridium tetanomorphum. Organization of the mut genes
    • E.N.G. Marsh, and D.E. Holloway Cloning and sequencing of glutamate mutase component E from Clostridium tetanomorphum. Organization of the mut genes FEBS Lett. 310 1992 167 170
    • (1992) FEBS Lett. , vol.310 , pp. 167-170
    • Marsh, E.N.G.1    Holloway, D.E.2
  • 11
    • 0028088469 scopus 로고
    • Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme
    • D.E. Holloway, and E.N.G. Marsh Adenosylcobalamin-dependent glutamate mutase from Clostridium tetanomorphum. Overexpression in Escherichia coli, purification, and characterization of the recombinant enzyme J Biol Chem 269 1994 20425 20430
    • (1994) J Biol Chem , vol.269 , pp. 20425-20430
    • Holloway, D.E.1    Marsh, E.N.G.2
  • 12
    • 0029892121 scopus 로고    scopus 로고
    • Review: Optimizing inducer and culture conditions for expression of foreign proteins under the control of the lac promoter
    • R.S. Donovan, C.W. Robinson, and B.R. Glick Review: 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
  • 13
    • 0026417070 scopus 로고
    • Effect of chemically induced, cloned gene expression on protein synthesis in E. coli
    • T.K. Wood, and S.W. Peretti 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
    • 14744305361 scopus 로고
    • The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli
    • A. Knappik, C. Krebber, and A. Pluckthun The effect of folding catalysts on the in vivo folding process of different antibody fragments expressed in Escherichia coli Biotechnology 11 1993 77 83
    • (1993) Biotechnology , vol.11 , pp. 77-83
    • Knappik, A.1    Krebber, C.2    Pluckthun, A.3
  • 16
    • 0025969480 scopus 로고
    • Temperature and induction effects on the degradation rate of an abnormal beta-galactosidase in Escherichia coli
    • M.J. Kosinski, and J.E. Bailey Temperature and induction effects on the degradation rate of an abnormal beta-galactosidase in Escherichia coli J Biotechnol 18 1991 55 68
    • (1991) J Biotechnol , vol.18 , pp. 55-68
    • Kosinski, M.J.1    Bailey, J.E.2
  • 17
    • 0000550920 scopus 로고
    • F.C. Neidhardi J.L. Ingraham K.B. Low B. Magasanik M. Schaechter H.E. Umbarger American Society for Microbiology Washington, DC
    • J.R. Beckwith F.C. Neidhardi J.L. Ingraham K.B. Low B. Magasanik M. Schaechter H.E. Umbarger Esherichia coli and Salminella typhimurium. Cellular and molecular biology vol. 2 1987 American Society for Microbiology Washington, DC 1444 1452
    • (1987) Esherichia Coli and Salminella Typhimurium. Cellular and Molecular Biology , vol.2 , pp. 1444-1452
    • Beckwith, J.R.1
  • 18
    • 0035976954 scopus 로고    scopus 로고
    • Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent d-ornithine aminomutase from Clostridium sticklandii
    • H.P. Chen, S.H. Wu, Y.L. Lin, C.M. Chen, and S.S. Tsay Cloning, sequencing, heterologous expression, purification, and characterization of adenosylcobalamin-dependent d-ornithine aminomutase from Clostridium sticklandii J Biol Chem 276 2001 44744 44750
    • (2001) J Biol Chem , vol.276 , pp. 44744-44750
    • Chen, H.P.1    Wu, S.H.2    Lin, Y.L.3    Chen, C.M.4    Tsay, S.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.