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Volumn 70, Issue 4, 2000, Pages 446-455

Error-prone PCR of Vitreoscilla hemoglobin (VHb) to support the growth of microaerobic Escherichia coli

Author keywords

Error prone PCR; Escherichia coli; Microaerobic growth; VHb mutants; Vitreoscilla hemoglobin (VHb)

Indexed keywords

BIOREACTORS; CELL CULTURE; CLONING; ESCHERICHIA COLI; GROWTH KINETICS; MUTAGENESIS; PROTEINS;

EID: 0034694155     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/1097-0290(20001120)70:4<446::AID-BIT10>3.0.CO;2-K     Document Type: Article
Times cited : (22)

References (48)
  • 5
    • 0027205210 scopus 로고
    • Tuning the activity of an enzyme for unusual environments: Sequential random mutagenesis of subtilisin E for catalysis in dimethylformamide
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5618-5622
    • Chen, K.1    Arnold, F.H.2
  • 9
    • 0032853779 scopus 로고    scopus 로고
    • Directed evolution of an esterase from Pseudomonas fluorescens. Random mutagenesis by error-prone PCR or a mutator strain and identification of mutants showing enhanced enantioselectivity by a resorufin-based fluorescence assay
    • (1999) Biol Chem , vol.380 , pp. 1029-1033
    • Heneke, E.1    Bornscheuer, U.T.2
  • 11
    • 0030038319 scopus 로고    scopus 로고
    • Intracellular expression of Vitreoscilla hemoglobin (VHb) enhances total protein secretion and improves the production of α-amylase and neutral protease in Bacillus subtilis
    • (1996) Biotechnol Prog , vol.12 , pp. 31-39
    • Kallio, P.T.1    Bailey, J.E.2
  • 13
    • 0030294364 scopus 로고    scopus 로고
    • Expression of Vitreoscilla hemoglobin is superior to horse heart myoglobin and yeast flavohemoglobin expression for enhancing Escherichia coli growth in a microaerobic bioreactor
    • (1996) Biotechnol Prog , vol.12 , pp. 751-757
    • Kallio, P.T.1    Tsai, P.S.2    Bailey, J.E.3
  • 14
    • 0023874286 scopus 로고
    • Heterologous expression of a bacterial haemoglobin improves the growth properties of recombinant Escherichia coli
    • (1988) Nature , vol.331 , pp. 633-635
    • Khosla, C.1    Bailey, J.E.2
  • 15
    • 0024080671 scopus 로고
    • The Vitreoscilla hemoglobin gene: Molecular cloning, nucleotide sequence and genetic expression in Escherichia coli
    • (1988) Mol Gen Genet , vol.214 , pp. 158-161
    • Khosla, C.1    Bailey, J.E.2
  • 16
    • 0024428050 scopus 로고
    • Characterization of the oxygen-dependent promoter of the Vitreoscilla hemoglobin gene in Escherichia coli
    • (1989) J Bacteriol , vol.171 , pp. 5995-6004
    • Khosla, C.1    Bailey, J.E.2
  • 17
    • 0024449797 scopus 로고
    • Evidence for partial export of Vitreoscilla hemoglobin into the periplasmic space in Escherichia coli: Implications for protein function
    • (1989) J Mol Biol , vol.210 , pp. 79-89
    • Khosla, C.1    Bailey, J.E.2
  • 22
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0031127043 scopus 로고    scopus 로고
    • Development of the multiple sequence approximation within the Agadir model of α-helix formation. Comparison with Zimm-Bragg and Lifson-Roig formalisms
    • (1997) Biopolymers , vol.41 , pp. 495-509
    • Munoz, V.1    Serrano, L.2
  • 30
    • 0023049253 scopus 로고
    • Photodissociation of oxygenated cytochrome o(s) (Vitreoscilla) and kinetic studies of reassociation
    • (1986) J Biol Chem , vol.261 , pp. 3544-3547
    • Orii, Y.1    Webster, D.A.2
  • 31
    • 0018654083 scopus 로고
    • Regulation of oxygen affinity of hemoglobin: Influence of structure of the globin on the heme iron
    • (1979) Annu Rev Biochem , vol.48 , pp. 327-386
    • Perutz, M.F.1
  • 36
    • 0031847060 scopus 로고    scopus 로고
    • Random mutagenesis on the Pseudomonas lipase activator protein, lipB: Exploring amino acid residues required for its function
    • (1998) Protein Eng , vol.11 , pp. 467-472
    • Shibata, H.1    Kato, H.2    Oda, J.3
  • 40
    • 0029636798 scopus 로고
    • Improvement of Escherichia coli microaerobic oxygen metabolism by Vitreoscilla hemoglobin: New insights from NAD(P)H fluorescence and culture redox potential
    • (1995) Biotechnol Bioeng , vol.47 , pp. 347-354
    • Tsai, P.S.1    Rao, G.2    Bailey, J.E.3
  • 42
    • 0030034536 scopus 로고    scopus 로고
    • Intracellular expression of Vitreoscilla hemoglobin modifies microaerobic Escherichia coli metabolism through elevated concentration and specific activity of cytochrome o
    • (1996) Biotechnol Bioeng , vol.49 , pp. 151-160
    • Tsai, P.S.1    Nageli, M.2    Bailey, J.E.3
  • 44
    • 0023817336 scopus 로고
    • Structure and function of bacterial hemoglobin and related proteins
    • Eichhorn GL, Marzilli LG, editors. Advances in inorganic biochemistry,New York: Elsevier
    • (1988) , vol.7 , pp. 245-265
    • Webster, D.A.1
  • 45
    • 0001089022 scopus 로고
    • Western blotting
    • Ausubel FM, Brent R, Kingston RE, Moore DD, Seidman JG, Smith JA, Struhl K, editors. Current protocols in molecular biology. New York: Wiley
    • (1987) , pp. 1081-1086
    • Winston, S.E.1    Fuller, S.A.2    Hurrell, J.G.R.3
  • 48
    • 0029969577 scopus 로고    scopus 로고
    • Directed evolution of subtilisin E in Bacillus subtilis to enhance total aqueous dimethylformamide
    • (1996) Protein Eng , vol.9 , pp. 77-83
    • You, L.1    Arnold, F.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.