메뉴 건너뛰기




Volumn 40, Issue 2, 2005, Pages 717-722

Optimization of enterokinase fermentation using a recombinant Saccharomyces cerevisiae

Author keywords

DO stat; Enterokinase fermentation; Recombinant Saccharomyces cerevisiae; Scale up

Indexed keywords

ETHANOL; NITROGEN; OPTIMIZATION; YEAST;

EID: 7444251677     PISSN: 00329592     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2004.01.055     Document Type: Article
Times cited : (7)

References (21)
  • 3
    • 0018171277 scopus 로고
    • Characterization of a trypsin-like enzyme in the duodenal mucosa of urodela and its significance for the activation of pancreatic zymogens
    • Hofer R., Steidl-Schennach D. Characterization of a trypsin-like enzyme in the duodenal mucosa of urodela and its significance for the activation of pancreatic zymogens. Comp. Biochem. Phys. B. 61:1978;459-461
    • (1978) Comp. Biochem. Phys. B , vol.61 , pp. 459-461
    • Hofer, R.1    Steidl-Schennach, D.2
  • 4
    • 0031466897 scopus 로고    scopus 로고
    • Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain
    • Lu D., Yuan X., Zheng X., Sadler E. Bovine proenteropeptidase is activated by trypsin, and the specificity of enteropeptidase depends on the heavy chain. J. Biol. Chem. 272:1997;31293-31300
    • (1997) J. Biol. Chem. , vol.272 , pp. 31293-31300
    • Lu, D.1    Yuan, X.2    Zheng, X.3    Sadler, E.4
  • 5
    • 0344631102 scopus 로고    scopus 로고
    • Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide
    • Lu D., Fütterer K., Korolev S., Zheng X., Tan K., Waksman G., et al. Crystal structure of enteropeptidase light chain complexed with an analog of the trypsinogen activation peptide. J. Mol. Biol. 292:1999;361-373
    • (1999) J. Mol. Biol. , vol.292 , pp. 361-373
    • Lu, D.1    Fütterer, K.2    Korolev, S.3    Zheng, X.4    Tan, K.5    Waksman, G.6
  • 6
    • 0021750643 scopus 로고
    • The preparation and properties of the catalytic subunit of bovine enterokinase
    • Light A., Fonseca P. The preparation and properties of the catalytic subunit of bovine enterokinase. J. Biol. Chem. 259:1984;13195-13198
    • (1984) J. Biol. Chem. , vol.259 , pp. 13195-13198
    • Light, A.1    Fonseca, P.2
  • 7
    • 0029115204 scopus 로고
    • Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA
    • Collins-Racie L.A., McColgan J.M., Grant K.L., DiBlasio-Smith E.A., McCoy J.M., LaVallie E.R. Production of recombinant bovine enterokinase catalytic subunit in Escherichia coli using the novel secretory fusion partner DsbA. Biotechnology. 13:1995;982-987
    • (1995) Biotechnology , vol.13 , pp. 982-987
    • Collins-Racie, L.A.1    McColgan, J.M.2    Grant, K.L.3    Diblasio-Smith, E.A.4    McCoy, J.M.5    Lavallie, E.R.6
  • 8
    • 0030040517 scopus 로고    scopus 로고
    • Production of a recombinant bovine enterokinase catalytic subunit in the methylotrophic yeast Pichia pastoris
    • Vozza L.A., Wittwer L., Higgins D.R., Purcell T.J., Bergseid M., Collins-Racie L.A., et al. Production of a recombinant bovine enterokinase catalytic subunit in the methylotrophic yeast Pichia pastoris. Biotechnology. 14:1996;77-81
    • (1996) Biotechnology , vol.14 , pp. 77-81
    • Vozza, L.A.1    Wittwer, L.2    Higgins, D.R.3    Purcell, T.J.4    Bergseid, M.5    Collins-Racie, L.A.6
  • 9
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • Cereghino G.P.L., Cereghino J.L., Ilgen C., Cregg J.M. Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr. Opin. Biotechnol. 13:2002;329-332
    • (2002) Curr. Opin. Biotechnol. , vol.13 , pp. 329-332
    • Cereghino, G.P.L.1    Cereghino, J.L.2    Ilgen, C.3    Cregg, J.M.4
  • 10
    • 0028042090 scopus 로고
    • Enhanced productivity through gratuitous induction in recombinant yeast fermentations
    • Napp S.J., Da Silva N.A. Enhanced productivity through gratuitous induction in recombinant yeast fermentations. Biotechnol. Prog. 10:1994;125-128
    • (1994) Biotechnol. Prog. , vol.10 , pp. 125-128
    • Napp, S.J.1    Da Silva, N.A.2
  • 12
    • 0030308931 scopus 로고    scopus 로고
    • Plasmid stability in recombinant Saccharomyces cerevisiae
    • Zhang Z., Moo-Young M., Chisti Y. Plasmid stability in recombinant Saccharomyces cerevisiae. Biotechnol. Adv. 14:1996;401-435
    • (1996) Biotechnol. Adv. , vol.14 , pp. 401-435
    • Zhang, Z.1    Moo-Young, M.2    Chisti, Y.3
  • 13
    • 0343907282 scopus 로고    scopus 로고
    • Plasmid instability kinetics in continuous culture of a recombinant Saccharomyces cerevisiae in airlift bioreactor
    • Zhang Z., Scharer J.M., Moo-Young M. Plasmid instability kinetics in continuous culture of a recombinant Saccharomyces cerevisiae in airlift bioreactor. J. Biotechnol. 55:1997;31-41
    • (1997) J. Biotechnol. , vol.55 , pp. 31-41
    • Zhang, Z.1    Scharer, J.M.2    Moo-Young, M.3
  • 14
    • 0037137907 scopus 로고    scopus 로고
    • Stabilizing plasmid copy number to improve recombinant protein production
    • Grabherr R., Nilsson E., Striendner G., Bayer K. Stabilizing plasmid copy number to improve recombinant protein production. Biotechnol. Bioeng. 77:2002;142-147
    • (2002) Biotechnol. Bioeng. , vol.77 , pp. 142-147
    • Grabherr, R.1    Nilsson, E.2    Striendner, G.3    Bayer, K.4
  • 15
  • 16
    • 0035793161 scopus 로고    scopus 로고
    • Two-stage cultivation of recombinant Saccharomyces cerevisiae to enhance plasmid stability under non-selective conditions: Experimental study and modeling
    • Gupta J.C., Pandey G., Mukherjee K.J. Two-stage cultivation of recombinant Saccharomyces cerevisiae to enhance plasmid stability under non-selective conditions: experimental study and modeling. Enzyme Microb. Technol. 28:2001;89-99
    • (2001) Enzyme Microb. Technol. , vol.28 , pp. 89-99
    • Gupta, J.C.1    Pandey, G.2    Mukherjee, K.J.3
  • 17
    • 0035170179 scopus 로고    scopus 로고
    • Stable maintenance of plasmid in continuous culture of yeast under non-selective conditions
    • Gupta J.C., Mukherjee K.J. Stable maintenance of plasmid in continuous culture of yeast under non-selective conditions. J. Biosci. Bioeng. 92:2001;317-323
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 317-323
    • Gupta, J.C.1    Mukherjee, K.J.2
  • 18
    • 0343487769 scopus 로고    scopus 로고
    • A novel feeding strategy for enhanced plasmid stability and protein production in recombinant yeast fedbatch fermentation
    • Cheng C., Huang Y.L., Yang S. A novel feeding strategy for enhanced plasmid stability and protein production in recombinant yeast fedbatch fermentation. Biotechnol. Bioeng. 56:1997;23-31
    • (1997) Biotechnol. Bioeng. , vol.56 , pp. 23-31
    • Cheng, C.1    Huang, Y.L.2    Yang, S.3
  • 19
    • 0035924096 scopus 로고    scopus 로고
    • Recombinant enterokinase light chain with affinity tag: Expression from Saccharomyces cerevisiae and its utilities in fusion protein technology
    • Choi S.I., Song H.W., Moon J.W., Seong B.L. Recombinant enterokinase light chain with affinity tag: Expression from Saccharomyces cerevisiae and its utilities in fusion protein technology. Biotechnol. Bioeng. 75:2001;718-724
    • (2001) Biotechnol. Bioeng. , vol.75 , pp. 718-724
    • Choi, S.I.1    Song, H.W.2    Moon, J.W.3    Seong, B.L.4
  • 20
    • 0018344418 scopus 로고
    • Hydrolysis of artificial substrates by enterokinase and trypsin and the development of a sensitive specific assay for enterokinase in serum
    • Hermon-Taylor J. Hydrolysis of artificial substrates by enterokinase and trypsin and the development of a sensitive specific assay for enterokinase in serum. Biochim. Biophys. Acta. 567:1979;207-215
    • (1979) Biochim. Biophys. Acta , vol.567 , pp. 207-215
    • Hermon-Taylor, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.