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Volumn 84, Issue 1, 2012, Pages 161-166

Optimization of an extracellular zinc-metalloprotease (SVP2) expression in Escherichia coli BL21 (DE3) using response surface methodology

Author keywords

Escherichia coli BL21 (DE3); Recombinant neutral zinc metalloprotease; Response surface methodology; Salinivibrio proteolyticus; SVP2

Indexed keywords

METALLOPROTEINASE; RECOMBINANT PROTEIN;

EID: 84861810645     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2012.05.004     Document Type: Article
Times cited : (25)

References (31)
  • 1
    • 84934436279 scopus 로고    scopus 로고
    • High-throughput protein production (HTPP): A review of enabling technologies to expedite protein production
    • J. Koehn, and I. Hunt High-throughput protein production (HTPP): a review of enabling technologies to expedite protein production Methods Mol. Biol. 498 2009 1 18
    • (2009) Methods Mol. Biol. , vol.498 , pp. 1-18
    • Koehn, J.1    Hunt, I.2
  • 3
    • 60949093998 scopus 로고    scopus 로고
    • Enhancement of over expression and chaperone assisted yield of folded recombinant aconitase in Escherichia coli in bioreactor cultures
    • P. Gupta, A. Ghosalkar, S. Mishra, and T.K. Chaudhuri Enhancement of over expression and chaperone assisted yield of folded recombinant aconitase in Escherichia coli in bioreactor cultures J. Biosci. Bioeng. 107 2009 102 107
    • (2009) J. Biosci. Bioeng. , vol.107 , pp. 102-107
    • Gupta, P.1    Ghosalkar, A.2    Mishra, S.3    Chaudhuri, T.K.4
  • 5
    • 0029864566 scopus 로고    scopus 로고
    • Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus
    • S.B. Halio, Blumentals II, S.A. Short, B.M. Merrill, and R.M. Kelly Sequence, expression in Escherichia coli, and analysis of the gene encoding a novel intracellular protease (PfpI) from the hyperthermophilic archaeon Pyrococcus furiosus J. Bacteriol. 178 1996 2605 2612 (Pubitemid 26134486)
    • (1996) Journal of Bacteriology , vol.178 , Issue.9 , pp. 2605-2612
    • Halio, S.B.1    Blumentals, I.I.2    Short, S.A.3    Merrill, B.M.4    Kelly, R.M.5
  • 6
    • 0031930829 scopus 로고    scopus 로고
    • Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes
    • S. Gubba, D.E. Low, and J.M. Musser Expression and characterization of group A Streptococcus extracellular cysteine protease recombinant mutant proteins and documentation of seroconversion during human invasive disease episodes Infect. Immun. 66 1998 765 770 (Pubitemid 28074225)
    • (1998) Infection and Immunity , vol.66 , Issue.2 , pp. 765-770
    • Gubba, S.1    Low, D.E.2    Musser, J.M.3
  • 7
    • 0032775329 scopus 로고    scopus 로고
    • Molecular cloning and expression in Escherichia coli of the extracellular endoprotease of Aeromonas caviae T-64, a pro-aminopeptidase processing enzyme
    • DOI 10.1016/S0167-4838(99)00158-2, PII S0167483899001582
    • S. Nirasawa, Y. Nakajima, Z. Zhang, M. Yoshida, and K. Hayashi Molecular cloning and expression in Escherichia coli of the extracellular endoprotease of Aeromonas caviae T-64, a pro-aminopeptidase processing enzyme Biochim. Biophys. Acta 1433 1999 335 342 (Pubitemid 29369068)
    • (1999) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1433 , Issue.1-2 , pp. 335-342
    • Nirasawa, S.1    Nakajima, Y.2    Zhang, Z.-Z.3    Yoshida, M.4    Hayashi, K.5
  • 8
    • 0034089313 scopus 로고    scopus 로고
    • Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli
    • DOI 10.1006/prep.2000.1193
    • M.B. Margetts, I.G. Barr, and E.A. Webb Overexpression, purification, and refolding of a Porphyromonas gingivalis cysteine protease from Escherichia coli Protein Expr. Purif. 18 2000 262 268 (Pubitemid 30213442)
    • (2000) Protein Expression and Purification , vol.18 , Issue.3 , pp. 262-268
    • Margetts, M.B.1    Barr, I.G.2    Webb, E.A.3
  • 10
    • 33746268510 scopus 로고    scopus 로고
    • A neutral protease from Bacillus nematocida, another potential virulence factor in the infection against nematodes
    • DOI 10.1007/s00203-006-0112-x
    • Q. Niu, X. Huang, L. Zhang, Y. Li, J. Li, J. Yang, and K. Zhang A neutral protease from Bacillus nematocida, another potential virulence factor in the infection against nematodes Arch. Microbiol. 185 2006 439 448 (Pubitemid 44088138)
    • (2006) Archives of Microbiology , vol.185 , Issue.6 , pp. 439-448
    • Niu, Q.1    Huang, X.2    Zhang, L.3    Li, Y.4    Li, J.5    Yang, J.6    Zhang, K.7
  • 11
    • 37549005219 scopus 로고    scopus 로고
    • Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli
    • H.R. Karbalaei-Heidari, A.A. Ziaee, M.A. Amoozegar, Y. Cheburkin, and N. Budisa Molecular cloning and sequence analysis of a novel zinc-metalloprotease gene from the Salinivibrio sp. strain AF-2004 and its extracellular expression in E. coli Gene 408 2008 196 203
    • (2008) Gene , vol.408 , pp. 196-203
    • Karbalaei-Heidari, H.R.1    Ziaee, A.A.2    Amoozegar, M.A.3    Cheburkin, Y.4    Budisa, N.5
  • 12
    • 0032712358 scopus 로고    scopus 로고
    • Alkaliphiles: Some applications of their products for biotechnology
    • K. Horikoshi Alkaliphiles: some applications of their products for biotechnology Microbiol. Mol. Biol. Rev. 63 1999 735 750
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 735-750
    • Horikoshi, K.1
  • 13
    • 77955207297 scopus 로고    scopus 로고
    • Enhanced activity and stability in the presence of organic solvents by increased active site polarity and stabilization of a surface loop in a metalloprotease
    • A. Badoei-Dalfard, K. Khajeh, S.M. Asghari, B. Ranjbar, and H.R. Karbalaei-Heidari Enhanced activity and stability in the presence of organic solvents by increased active site polarity and stabilization of a surface loop in a metalloprotease J. Biochem. 148 2010 231 238
    • (2010) J. Biochem. , vol.148 , pp. 231-238
    • Badoei-Dalfard, A.1    Khajeh, K.2    Asghari, S.M.3    Ranjbar, B.4    Karbalaei-Heidari, H.R.5
  • 15
    • 43049167225 scopus 로고    scopus 로고
    • Response surface optimization of medium composition for alkaline protease production by Bacillus clausii
    • DOI 10.1016/j.bej.2007.08.016, PII S1369703X07002963
    • S.F. Ghaemi-Oskouie, F. Tabandeh, B. Yakhchali, and F. Eftekhar Response surface optimization of medium composition for alkaline protease production by Bacillus clausii Biochem. Eng. J. 39 2008 37 42 (Pubitemid 351635729)
    • (2008) Biochemical Engineering Journal , vol.39 , Issue.1 , pp. 37-42
    • Oskouie, S.F.G.1    Tabandeh, F.2    Yakhchali, B.3    Eftekhar, F.4
  • 16
    • 70449507927 scopus 로고    scopus 로고
    • Optimization of medium constituents for improved chitinase production by Paenibacillus sp. D1 using statistical approach
    • A.K. Singh, G. Mehta, and H.S. Chhatpar Optimization of medium constituents for improved chitinase production by Paenibacillus sp. D1 using statistical approach Lett. Appl. Microbiol. 49 2009 708 714
    • (2009) Lett. Appl. Microbiol. , vol.49 , pp. 708-714
    • Singh, A.K.1    Mehta, G.2    Chhatpar, H.S.3
  • 18
    • 1442350510 scopus 로고    scopus 로고
    • Application of Plackett-Burman Design and Response Surface Methodology to Achieve Exponential Growth for Aggregated Shipworm Bacterium
    • DOI 10.1002/bit.10880
    • S.K. Ahuja, G.M. Ferreira, and A.R. Moreira Application of Plackett-Burman design and response surface methodology to achieve exponential growth for aggregated shipworm bacterium Biotechnol. Bioeng. 85 2004 666 675 (Pubitemid 38270499)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.6 , pp. 666-675
    • Ahuja, S.K.1    Ferreira, G.M.2    Moreira, A.R.3
  • 20
    • 1942521189 scopus 로고    scopus 로고
    • Xylitol production by Candida sp.: Parameter optimization using Taguchi approach
    • DOI 10.1016/S0032-9592(03)00207-3, PII S0032959203002073
    • R.S. Rao, R.S. Prakasham, K.K. Prasad, S. Rajesham, P.N. Sarma, and L.V. Rao Xylitol production by Candida sp.: parameter optimization using Taguchi approach Process Biochem. 39 2004 951 956 (Pubitemid 38503489)
    • (2004) Process Biochemistry , vol.39 , Issue.8 , pp. 951-956
    • Rao, R.S.1    Prakasham, R.S.2    Prasad, K.K.3    Rajesham, S.4    Sarma, P.N.5    Rao, L.V.6
  • 21
    • 0001133849 scopus 로고
    • Experimental designs
    • A. Baron Experimental designs Behav. Anal. 13 1990 167 171
    • (1990) Behav. Anal. , vol.13 , pp. 167-171
    • Baron, A.1
  • 22
    • 33751196772 scopus 로고    scopus 로고
    • Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004
    • DOI 10.1016/j.enzmictec.2006.04.006, PII S0141022906002031
    • H.R. Karbalaei-Heidari, A.-A. Ziaee, J. Schaller, and M.A. Amoozegar Purification and characterization of an extracellular haloalkaline protease produced by the moderately halophilic bacterium, Salinivibrio sp. strain AF-2004 Enzyme Microb. Tech. 40 2007 266 272 (Pubitemid 44779781)
    • (2007) Enzyme and Microbial Technology , vol.40 , Issue.2 , pp. 266-272
    • Karbalaei-Heidari, H.R.1    Ziaee, A.-A.2    Schaller, J.3    Amoozegar, M.A.4
  • 24
    • 17844367620 scopus 로고    scopus 로고
    • Effect of culture conditions on production of 5-aminolevulinic acid by recombinant Escherichia coli
    • D.H. Lee, W.J. Jun, D.H. Shin, H.Y. Cho, and B.S. Hong Effect of culture conditions on production of 5-aminolevulinic acid by recombinant Escherichia coli Biosci. Biotechnol. Biochem. 69 2005 470 476
    • (2005) Biosci. Biotechnol. Biochem. , vol.69 , pp. 470-476
    • Lee, D.H.1    Jun, W.J.2    Shin, D.H.3    Cho, H.Y.4    Hong, B.S.5
  • 25
    • 79955617148 scopus 로고    scopus 로고
    • Cloning and optimization of induction conditions for mature PsaA (pneumococcal surface adhesin A) expression in Escherichia coli and recombinant protein stability during long-term storage
    • A.L. Larentis, A.P. Argondizzo, S. Esteves Gdos, E. Jessouron, R. Galler, and M.A. Medeiros Cloning and optimization of induction conditions for mature PsaA (pneumococcal surface adhesin A) expression in Escherichia coli and recombinant protein stability during long-term storage Protein Expr. Purif. 78 2011 38 47
    • (2011) Protein Expr. Purif. , vol.78 , pp. 38-47
    • Larentis, A.L.1    Argondizzo, A.P.2    Esteves Gdos, S.3    Jessouron, E.4    Galler, R.5    Medeiros, M.A.6
  • 26
    • 33747735624 scopus 로고    scopus 로고
    • High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression
    • DOI 10.1016/j.reactfunctpolym.2005.10.008
    • Z. Xu, Z. Zhong, L. Huang, L. Peng, F. Wang, and P. Cen High-level production of bioactive human beta-defensin-4 in Escherichia coli by soluble fusion expression Appl. Microbiol. Biotechnol. 72 2006 471 479 (Pubitemid 44273072)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.3 , pp. 471-479
    • Xu, Z.1    Zhong, Z.2    Huang, L.3    Peng, L.4    Wang, F.5    Cen, P.6
  • 27
    • 33847287768 scopus 로고    scopus 로고
    • Production of GDP-l-fucose, l-fucose donor for fucosyloligosaccharide synthesis, in recombinant Escherichia coli
    • S.G. Byun, M.D. Kim, W.H. Lee, K.J. Lee, N.S. Han, and J.H. Seo Production of GDP-l-fucose, l-fucose donor for fucosyloligosaccharide synthesis, in recombinant Escherichia coli Appl. Microbiol. Biotechnol. 74 2007 768 775
    • (2007) Appl. Microbiol. Biotechnol. , vol.74 , pp. 768-775
    • Byun, S.G.1    Kim, M.D.2    Lee, W.H.3    Lee, K.J.4    Han, N.S.5    Seo, J.H.6
  • 29
    • 0028061161 scopus 로고
    • Toxic responses to defined chemical mixtures: Mathematical models and experimental designs
    • DOI 10.1016/0024-3205(94)00670-9
    • J.P. Michaud, A.J. Gandolfi, and K. Brendel Toxic responses to defined chemical mixtures: mathematical models and experimental designs Life Sci. 55 1994 635 651 (Pubitemid 24250023)
    • (1994) Life Sciences , vol.55 , Issue.9 , pp. 635-651
    • Michaud, J.P.1    Gandolfi, A.J.2    Brendel, K.3
  • 30
    • 3042596177 scopus 로고    scopus 로고
    • Optimization of expression of an Annexin V-Hirudin chimeric protein in Escherichia coli
    • DOI 10.1016/j.micres.2004.02.002, PII S0944501304000205
    • H. Yuan, X. Yang, and Z.-C. Hua Optimization of expression of an Annexin V-Hirudin chimeric protein in Escherichia coli Microbiol. Res. 159 2004 147 156 (Pubitemid 38836809)
    • (2004) Microbiological Research , vol.159 , Issue.2 , pp. 147-156
    • Yuan, H.1    Yang, X.2    Hua, Z.-C.3
  • 31
    • 27844581254 scopus 로고    scopus 로고
    • Production of recombinant proteins by high cell density culture of Escherichia coli
    • DOI 10.1016/j.ces.2005.03.031, PII S0009250905002691, Biomolecular Engineering
    • J.H. Choi, K.C. Keum, and S.Y. Lee Production of recombinant proteins by high cell density culture of Escherichia coli Chem. Eng. Sci. 61 2006 876 885 (Pubitemid 41650182)
    • (2006) Chemical Engineering Science , vol.61 , Issue.3 , pp. 876-885
    • Choi, J.H.1    Keum, K.C.2    Lee, S.Y.3


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