메뉴 건너뛰기




Volumn 49, Issue 4, 2014, Pages 599-603

Novel insight into the secretory expression of recombinant enzymes in Escherichia coli

Author keywords

Cyclodextrin glycosyltransferase; Escherichia coli; Recombinant enzymes; Secretory expression

Indexed keywords

BIOSYNTHESIS; CYCLODEXTRINS; ESCHERICHIA COLI;

EID: 84897912663     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2014.01.029     Document Type: Article
Times cited : (19)

References (19)
  • 1
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • J.H. Choi, and S.Y. Lee Secretory and extracellular production of recombinant proteins using Escherichia coli Appl Microbiol Biotechnol 64 2004 625 635
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 2
    • 56749117745 scopus 로고    scopus 로고
    • Extracellular recombinant protein production from an Escherichia coli lpp deletion mutant
    • H.D. Shin, and R.R. Chen Extracellular recombinant protein production from an Escherichia coli lpp. deletion mutant Biotechnol Bioeng 101 2008 1288 1296
    • (2008) Biotechnol Bioeng , vol.101 , pp. 1288-1296
    • Shin, H.D.1    Chen, R.R.2
  • 3
    • 78649443670 scopus 로고    scopus 로고
    • Enhanced secretory production of hemolysin-mediated cyclodextrin glucanotransferase in Escherichia coli by random mutagenesis of the ABC transporter system
    • K.O. Low, N.M. Mahadi, R.A. Rahim, F.D. Abu Bakar, A.M.A. Murad, and R.M. Illias Enhanced secretory production of hemolysin-mediated cyclodextrin glucanotransferase in Escherichia coli by random mutagenesis of the ABC transporter system J Biotechnol 150 2010 453 459
    • (2010) J Biotechnol , vol.150 , pp. 453-459
    • Low, K.O.1    Mahadi, N.M.2    Rahim, R.A.3    Abu Bakar, F.D.4    Murad, A.M.A.5    Illias, R.M.6
  • 4
    • 79954999848 scopus 로고    scopus 로고
    • High-level extracellular production of α-cyclodextrin glycosyltransferase with recombinant Escherichia coli BL21 (DE3)
    • J. Cheng, D. Wu, S. Chen, J. Chen, and J. Wu High-level extracellular production of α-cyclodextrin glycosyltransferase with recombinant Escherichia coli BL21 (DE3) J Agric Food Chem 59 2011 3797 3802
    • (2011) J Agric Food Chem , vol.59 , pp. 3797-3802
    • Cheng, J.1    Wu, D.2    Chen, S.3    Chen, J.4    Wu, J.5
  • 5
    • 67650931139 scopus 로고    scopus 로고
    • Calcium leads to further increase in glycine-enhanced extracellular secretion of recombinant α-cyclodextrin glycosyltransferase in Escherichia coli
    • Z.F. Li, B. Li, Z.G. Liu, M. Wang, Z.B. Gu, and G.C. Du et al. Calcium leads to further increase in glycine-enhanced extracellular secretion of recombinant α-cyclodextrin glycosyltransferase in Escherichia coli J Agric Food Chem 57 2009 6231 6237
    • (2009) J Agric Food Chem , vol.57 , pp. 6231-6237
    • Li, Z.F.1    Li, B.2    Liu, Z.G.3    Wang, M.4    Gu, Z.B.5    Du, G.C.6
  • 6
    • 44849090096 scopus 로고    scopus 로고
    • Evolution toward small molecule inhibitor resistance affects native enzyme function and stability, generating acarbose-insensitive cyclodextrin glucanotransferase variants
    • R.M. Kelly, H. Leemhuis, L. Gatjen, and L. Dijkhuizen Evolution toward small molecule inhibitor resistance affects native enzyme function and stability, generating acarbose-insensitive cyclodextrin glucanotransferase variants J Biol Chem 283 2008 10727 10734
    • (2008) J Biol Chem , vol.283 , pp. 10727-10734
    • Kelly, R.M.1    Leemhuis, H.2    Gatjen, L.3    Dijkhuizen, L.4
  • 7
    • 84858438608 scopus 로고    scopus 로고
    • The residue 179 is involved in product specificity of the Bacillus circulans DF 9R cyclodextrin glycosyltransferase
    • H. Costa, A.J. Distefano, C. Marino-Buslje, A. Hidalgo, J. Berenguer, and M.B.D. Bonino et al. The residue 179 is involved in product specificity of the Bacillus circulans DF 9R cyclodextrin glycosyltransferase Appl Microbiol Biotechnol 94 2012 123 130
    • (2012) Appl Microbiol Biotechnol , vol.94 , pp. 123-130
    • Costa, H.1    Distefano, A.J.2    Marino-Buslje, C.3    Hidalgo, A.4    Berenguer, J.5    Bonino, M.B.D.6
  • 8
    • 84873133493 scopus 로고    scopus 로고
    • Potential use of folate-appended methyl-β-cyclodextrin as an anticancer agent
    • R. Onodera, K. Motoyama, A. Okamatsu, T. Higashi, and H. Arima Potential use of folate-appended methyl-β-cyclodextrin as an anticancer agent Sci Rep 3 2013 1104
    • (2013) Sci Rep , vol.3 , pp. 1104
    • Onodera, R.1    Motoyama, K.2    Okamatsu, A.3    Higashi, T.4    Arima, H.5
  • 9
    • 84862815922 scopus 로고    scopus 로고
    • Enhanced production of volatile fatty acids (VFAs) from sewage sludge by β-cyclodextrin
    • X. Yang, M. Du, D.J. Lee, C. Wan, L. Zheng, and G. Li et al. Enhanced production of volatile fatty acids (VFAs) from sewage sludge by β-cyclodextrin Bioresour Technol 110 2012 688 691
    • (2012) Bioresour Technol , vol.110 , pp. 688-691
    • Yang, X.1    Du, M.2    Lee, D.J.3    Wan, C.4    Zheng, L.5    Li, G.6
  • 10
    • 84856219989 scopus 로고    scopus 로고
    • Enzymatic synthesis of piceid glycosides by cyclodextrin glucanotransferase
    • S. Mathew, M. Hedstrom, and P. Adlercreutz Enzymatic synthesis of piceid glycosides by cyclodextrin glucanotransferase Process Biochem 47 2012 528 532
    • (2012) Process Biochem , vol.47 , pp. 528-532
    • Mathew, S.1    Hedstrom, M.2    Adlercreutz, P.3
  • 11
    • 1942470488 scopus 로고    scopus 로고
    • Cyclodextrins and their uses: A review
    • E.M.M. Del Valle Cyclodextrins and their uses: a review Process Biochem 39 2004 1033 1046
    • (2004) Process Biochem , vol.39 , pp. 1033-1046
    • Del Valle, E.M.M.1
  • 12
    • 77958590126 scopus 로고    scopus 로고
    • Expression and characterization of a fusion protein-containing cyclodextrin glycosyltransferase from Paenibacillus sp. A11
    • J. Kaulpiboon, W. Prasong, V. Rimphanitchayakit, S. Murakami, K. Aoki, and P. Pongsawasdi Expression and characterization of a fusion protein-containing cyclodextrin glycosyltransferase from Paenibacillus sp. A11 J Basic Microbiol 50 2010 427 435
    • (2010) J Basic Microbiol , vol.50 , pp. 427-435
    • Kaulpiboon, J.1    Prasong, W.2    Rimphanitchayakit, V.3    Murakami, S.4    Aoki, K.5    Pongsawasdi, P.6
  • 13
    • 23844538438 scopus 로고    scopus 로고
    • Characterization of cyclodextrin glycosyltransferase of the same gene expressed from Bacillus macerans, Bacillus subtilis, and Escherichia coli
    • C.L. Jeang, D.G. Lin, and S.H. Hsieh Characterization of cyclodextrin glycosyltransferase of the same gene expressed from Bacillus macerans, Bacillus subtilis, and Escherichia coli J Agric Food Chem 53 2005 6301 6304
    • (2005) J Agric Food Chem , vol.53 , pp. 6301-6304
    • Jeang, C.L.1    Lin, D.G.2    Hsieh, S.H.3
  • 14
    • 77950593255 scopus 로고    scopus 로고
    • Extracellular expression and biochemical characterization of α-cyclodextrin glycosyltransferase from Paenibacillus macerans
    • Z. Li, B. Li, Z. Gu, G. Du, J. Wu, and J. Chen Extracellular expression and biochemical characterization of α-cyclodextrin glycosyltransferase from Paenibacillus macerans Carbohydr Res 345 2010 886 892
    • (2010) Carbohydr Res , vol.345 , pp. 886-892
    • Li, Z.1    Li, B.2    Gu, Z.3    Du, G.4    Wu, J.5    Chen, J.6
  • 15
    • 84855608783 scopus 로고    scopus 로고
    • Extracellular overexpression of recombinant Thermobifida fusca cutinase by α-hemolysin secretion system in E coli BL21(DE3)
    • L. Su, S. Chen, L. Yi, R.W. Woodard, J. Chen, and J. Wu Extracellular overexpression of recombinant Thermobifida fusca cutinase by α-hemolysin secretion system in E. coli BL21(DE3) Microb Cell Fact 11 2012 8
    • (2012) Microb Cell Fact , vol.11 , pp. 8
    • Su, L.1    Chen, S.2    Yi, L.3    Woodard, R.W.4    Chen, J.5    Wu, J.6
  • 16
    • 0035339953 scopus 로고    scopus 로고
    • SecB, a molecular chaperone with two faces
    • A.J. Driessen SecB, a molecular chaperone with two faces Trends Microbiol 9 2001 193 196
    • (2001) Trends Microbiol , vol.9 , pp. 193-196
    • Driessen, A.J.1
  • 17
    • 0036152775 scopus 로고    scopus 로고
    • Effect of osmolytes as folding aids on creatine kinase refolding pathway
    • W.B. Ou, Y.D. Park, and H.M. Zhou Effect of osmolytes as folding aids on creatine kinase refolding pathway Int J Biochem Cell Biol 34 2002 136 147
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 136-147
    • Ou, W.B.1    Park, Y.D.2    Zhou, H.M.3
  • 18
    • 0031904157 scopus 로고    scopus 로고
    • One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-α) from Escherichia coli caused by the synergistic effects of glycine and triton X-100
    • J. Yang, T. Moyana, S. MacKenzie, Q. Xia, and J. Xiang One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-α) from Escherichia coli caused by the synergistic effects of glycine and triton X-100 Appl Environ Microbiol 64 1998 2869 2874
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2869-2874
    • Yang, J.1    Moyana, T.2    Mackenzie, S.3    Xia, Q.4    Xiang, J.5
  • 19
    • 9244231763 scopus 로고    scopus 로고
    • Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli
    • L.C. Simmons, and D.G. Yansura Translational level is a critical factor for the secretion of heterologous proteins in Escherichia coli Nat Biotechnol 14 1996 629 634
    • (1996) Nat Biotechnol , vol.14 , pp. 629-634
    • Simmons, L.C.1    Yansura, D.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.