메뉴 건너뛰기




Volumn 39, Issue 1, 2005, Pages 54-60

Optimized expression of soluble cyclomaltodextrinase of thermophilic origin in Escherichia coli by using a soluble fusion-tag and by tuning of inducer concentration

Author keywords

Anoxybacillus; Cyclomaltodextrinase; NusA

Indexed keywords

CYCLOMALTODEXTRINASE; ELONGATION FACTOR; ESCHERICHIA COLI PROTEIN; GLYCOSIDASE; HYBRID PROTEIN; NUSA PROTEIN, E COLI; TRANSCRIPTION FACTOR;

EID: 10644275363     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.09.012     Document Type: Article
Times cited : (57)

References (20)
  • 1
    • 0029989229 scopus 로고    scopus 로고
    • Expression of correctly folded proteins in Escherichia coli
    • G. Georgiou, and P. Valax Expression of correctly folded proteins in Escherichia coli Curr. Opin. Biotechnol. 7 1996 190 197
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 190-197
    • Georgiou, G.1    Valax, P.2
  • 3
    • 0029240270 scopus 로고
    • In vitro refolding of cyclomaltodextrin glucanotransferase from cytoplasmic inclusion bodies formed upon expression in Escherichia coli
    • J. Hellman, P. Lassila, and P. Maentsaelae In vitro refolding of cyclomaltodextrin glucanotransferase from cytoplasmic inclusion bodies formed upon expression in Escherichia coli Protein Expr. Purif. 6 1995 56 62
    • (1995) Protein Expr. Purif. , vol.6 , pp. 56-62
    • Hellman, J.1    Lassila, P.2    Maentsaelae, P.3
  • 4
    • 0141525436 scopus 로고    scopus 로고
    • Sequence analysis of cyclodextrin glycosyltransferase from the alkaliphilic Bacillus agaradhaerens
    • R. Martins, O. Delgado, and R. Hatti-Kaul Sequence analysis of cyclodextrin glycosyltransferase from the alkaliphilic Bacillus agaradhaerens Biotechnol. Lett. 25 2003 1555 1562
    • (2003) Biotechnol. Lett. , vol.25 , pp. 1555-1562
    • Martins, R.1    Delgado, O.2    Hatti-Kaul, R.3
  • 5
    • 15844395096 scopus 로고    scopus 로고
    • Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins
    • J.G. Thomas, and F. Baneyx Protein misfolding and inclusion body formation in recombinant Escherichia coli cells overexpressing heat-shock proteins J. Biol. Chem. 271 1996 11141 11147
    • (1996) J. Biol. Chem. , vol.271 , pp. 11141-11147
    • Thomas, J.G.1    Baneyx, F.2
  • 6
    • 0031105876 scopus 로고    scopus 로고
    • Expression of aggregation-prone recombinant proteins at low temperatures: A comparative study of the Escherichia coli cspA and tac promoter systems
    • J.A. Vasina, and F. Baneyx Expression of aggregation-prone recombinant proteins at low temperatures: a comparative study of the Escherichia coli cspA and tac promoter systems Protein Expr. Purif. 9 1997 211 218
    • (1997) Protein Expr. Purif. , vol.9 , pp. 211-218
    • Vasina, J.A.1    Baneyx, F.2
  • 7
    • 0037434442 scopus 로고    scopus 로고
    • Evaluation of different promoters and host strains for the high-level expression of collagen-like polymer in Escherichia coli
    • J. Yin, J.-h. Lin, W.-t. Li, and D.I.C. Wang Evaluation of different promoters and host strains for the high-level expression of collagen-like polymer in Escherichia coli J. Biotechnol. 100 2003 181 191
    • (2003) J. Biotechnol. , vol.100 , pp. 181-191
    • Yin, J.1    Lin, J.-H.2    Li, W.-T.3    Wang, D.I.C.4
  • 8
    • 0036010292 scopus 로고    scopus 로고
    • Stringent regulation and high-level expression of heterologous genes in Escherichia coli using T7 system controllable by the araBAD promoter
    • Y.-P. Chao, C.-J. Chiang, and W.-B. Hung Stringent regulation and high-level expression of heterologous genes in Escherichia coli using T7 system controllable by the araBAD promoter Biotechnol. Prog. 18 2002 394 400
    • (2002) Biotechnol. Prog. , vol.18 , pp. 394-400
    • Chao, Y.-P.1    Chiang, C.-J.2    Hung, W.-B.3
  • 9
    • 0033580277 scopus 로고    scopus 로고
    • Broad-host-range expression vectors that carry the l-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator
    • J.R. Newman, and C. Fuqua Broad-host-range expression vectors that carry the l-arabinose-inducible Escherichia coli araBAD promoter and the araC regulator Gene 227 1999 197 203
    • (1999) Gene , vol.227 , pp. 197-203
    • Newman, J.R.1    Fuqua, C.2
  • 10
    • 0030940137 scopus 로고    scopus 로고
    • The chloroplast psbA promoter is more efficient in Escherichia coli than the T7 promoter for hyperexpression of a foreign protein
    • P.J. Brixey, C. Guda, and H. Daniell The chloroplast psbA promoter is more efficient in Escherichia coli than the T7 promoter for hyperexpression of a foreign protein Biotechnol. Lett. 19 1997 395 399
    • (1997) Biotechnol. Lett. , vol.19 , pp. 395-399
    • Brixey, P.J.1    Guda, C.2    Daniell, H.3
  • 11
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • R.B. Kapust, and D.S. Waugh Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused Protein Sci. 8 1999 1668 1674
    • (1999) Protein Sci. , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 12
    • 0011962568 scopus 로고    scopus 로고
    • Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli
    • E.R. La Vallie, Z. Lu, E.A. Diblasio-Smith, L.A. Collins-Racie, and J.M. McCoy Thioredoxin as a fusion partner for production of soluble recombinant proteins in Escherichia coli Methods Enzymol. 326 2000 322 340
    • (2000) Methods Enzymol. , vol.326 , pp. 322-340
    • La Vallie, E.R.1    Lu, Z.2    Diblasio-Smith, E.A.3    Collins-Racie, L.A.4    McCoy, J.M.5
  • 14
    • 0032509329 scopus 로고    scopus 로고
    • High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D
    • P. Forrer, and R. Jaussi High-level expression of soluble heterologous proteins in the cytoplasm of Escherichia coli by fusion to the bacteriophage lambda head protein D Gene 224 1998 45 52
    • (1998) Gene , vol.224 , pp. 45-52
    • Forrer, P.1    Jaussi, R.2
  • 15
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • G.D. Davis, C. Elisee, D.M. Newham, and R.G. Harrison New fusion protein systems designed to give soluble expression in Escherichia coli Biotechnol. Bioeng. 65 1999 382 388
    • (1999) Biotechnol. Bioeng. , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 16
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • G.L. Miller Use of dinitrosalicylic acid reagent for determination of reducing sugar Anal. Chem. 31 1959 426 428
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • U. Laemmli Cleavage of structural proteins during assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 18
    • 0005778409 scopus 로고    scopus 로고
    • The multisubstrate specificity and the quaternary structure of cyclodextrin-/pullulan-degrading enzymes
    • K.H. Park The multisubstrate specificity and the quaternary structure of cyclodextrin-/pullulan-degrading enzymes J. Appl. Glycosci. 48 2001 293 299
    • (2001) J. Appl. Glycosci. , vol.48 , pp. 293-299
    • Park, K.H.1
  • 19
    • 0025953577 scopus 로고
    • Predicting the solubility of recombinant proteins in Escherichia coli
    • D.L. Wilkinson, and R.G. Harrison Predicting the solubility of recombinant proteins in Escherichia coli Bio/Technology 9 1991 443 448
    • (1991) Bio/Technology , vol.9 , pp. 443-448
    • Wilkinson, D.L.1    Harrison, R.G.2
  • 20
    • 0036145552 scopus 로고    scopus 로고
    • Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli
    • M. Hammarström, N. Hellgren, S. Van Den Berg, H. Berglund, and T. Härd Rapid screening for improved solubility of small human proteins produced as fusion proteins in Escherichia coli Protein Sci. 11 2002 313 321
    • (2002) Protein Sci. , vol.11 , pp. 313-321
    • Hammarström, M.1    Hellgren, N.2    Van Den Berg, S.3    Berglund, H.4    Härd, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.