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Volumn 76, Issue 13, 2010, Pages 4486-4496

Combined use of fluorescent dyes and flow cytometry to quantify the physiological state of Pichia pastoris during the production of heterologous proteins in high-cell-density Fed-batch cultures

Author keywords

[No Author keywords available]

Indexed keywords

BIOPROCESS DEVELOPMENT; BIOPROCESSES; COMBINED EFFECT; CULTURE BROTHS; FED-BATCH CULTURES; FLUORESCENT DYES; HETEROLOGOUS GENES; HETEROLOGOUS PROTEINS; HIGH CELL DENSITY; HORSE-RADISH PEROXIDASE; INDIVIDUAL CELLS; METHANOL UTILIZATION; PH VALUE; PHYSIOLOGICAL STATE; PHYSIOLOGICAL STRESS; PICHIA PASTORIS; PROCESS CONDITION; QUANTITATIVE ASSESSMENTS; RECOMBINANT PROTEIN; RECOMBINANT STRAINS; REPRODUCIBILITIES; STRESS FACTORS; TARGET PROTEINS; UNIFORM CELLS;

EID: 77954279954     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.02475-09     Document Type: Article
Times cited : (31)

References (59)
  • 1
    • 33745262080 scopus 로고    scopus 로고
    • Flow-cytometric study of vital cellular functions in Escherichia coli during solar disinfection (SODIS)
    • Berney, M., H. U. Weilenmann, and T. Egli. 2006. Flow-cytometric study of vital cellular functions in Escherichia coli during solar disinfection (SODIS). Microbiology 152:1719-1729.
    • (2006) Microbiology , vol.152 , pp. 1719-1729
    • Berney, M.1    Weilenmann, H.U.2    Egli, T.3
  • 3
    • 0036165047 scopus 로고    scopus 로고
    • The use of flow cytometry to detect nucleic acids attached to the surface of Escherichia coli in high cell density fed-batch processes
    • Castan, A., J. Heidrich, and S. O. Enfors. 2002. The use of flow cytometry to detect nucleic acids attached to the surface of Escherichia coli in high cell density fed-batch processes. Biotechnol. Lett. 24:219-224.
    • (2002) Biotechnol. Lett. , vol.24 , pp. 219-224
    • Castan, A.1    Heidrich, J.2    Enfors, S.O.3
  • 4
    • 0025879069 scopus 로고
    • Eukaryotic start and stop translation sites
    • Cavener, D. R., and S. C. Ray. 1991. Eukaryotic start and stop translation sites. Nucleic Acids Res. 19:3185-3192.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 3185-3192
    • Cavener, D.R.1    Ray, S.C.2
  • 6
    • 0033673087 scopus 로고    scopus 로고
    • Expression and characterization of glycosylated and catalytically active recombinant human alpha-galactosidase A produced in Pichia pastoris
    • Chen, Y., M. Jin, T. Egborge, G. Coppola, J. Andre, and D. H. Calhoun. 2000. Expression and characterization of glycosylated and catalytically active recombinant human alpha-galactosidase A produced in Pichia pastoris. Protein Expr. Purif. 20:472-484.
    • (2000) Protein Expr. Purif. , vol.20 , pp. 472-484
    • Chen, Y.1    Jin, M.2    Egborge, T.3    Coppola, G.4    Andre, J.5    Calhoun, D.H.6
  • 7
    • 0038384080 scopus 로고    scopus 로고
    • Production of savinase and population viability of Bacillus clausii during high-cell-density fed-batch cultivations
    • Christiansen, T., S. Michaelsen, M. Wumpelmann, and J. Nielsen. 2003. Production of savinase and population viability of Bacillus clausii during high-cell-density fed-batch cultivations. Biotechnol. Bioeng. 83:344-352.
    • (2003) Biotechnol. Bioeng. , vol.83 , pp. 344-352
    • Christiansen, T.1    Michaelsen, S.2    Wumpelmann, M.3    Nielsen, J.4
  • 8
    • 0026094226 scopus 로고
    • Production of mouse epidermal growth factor in yeast: High-level secretion using Pichia pastoris strains containing multiple gene copies
    • Clare, J. J., M. A. Romanos, F. B. Rayment, J. E. Rowedder, M. A. Smith, M. M. Payne, K. Sreekrishna, and C. A. Henwood. 1991. Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies. Gene 105:205-212.
    • (1991) Gene , vol.105 , pp. 205-212
    • Clare, J.J.1    Romanos, M.A.2    Rayment, F.B.3    Rowedder, J.E.4    Smith, M.A.5    Payne, M.M.6    Sreekrishna, K.7    Henwood, C.A.8
  • 10
    • 0034974699 scopus 로고    scopus 로고
    • Human chymotrypsinogen B production with Pichia pastoris by integrated development of fermentation and downstream processing. Part 1. Fermentation
    • Curvers, S., P. Brixius, T. Klauser, J. Thommes, D. Weuster-Botz, R. Takors, and C. Wandrey. 2001. Human chymotrypsinogen B production with Pichia pastoris by integrated development of fermentation and downstream processing. Part 1. Fermentation. Biotechnol. Prog. 17:495-502.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 495-502
    • Curvers, S.1    Brixius, P.2    Klauser, T.3    Thommes, J.4    Weuster-Botz, D.5    Takors, R.6    Wandrey, C.7
  • 11
    • 0034022515 scopus 로고    scopus 로고
    • Mixed-feed exponential feeding for fed-batch culture of recombinant methylotrophic yeast
    • d'Anjou, M. C., and A. J. Daugulis. 2000. Mixed-feed exponential feeding for fed-batch culture of recombinant methylotrophic yeast. Biotechnol. Lett. 22:341-346.
    • (2000) Biotechnol. Lett. , vol.22 , pp. 341-346
    • D'Anjou, M.C.1    Daugulis, A.J.2
  • 12
    • 0026709223 scopus 로고
    • Metabolic control analysis using transient metabolite concentrations. Determination of metabolite concentration control coefficients
    • Delgado, J., and J. C. Liao. 1992. Metabolic control analysis using transient metabolite concentrations. Determination of metabolite concentration control coefficients. Biochem. J. 285:965-972.
    • (1992) Biochem. J. , vol.285 , pp. 965-972
    • Delgado, J.1    Liao, J.C.2
  • 15
    • 0033214742 scopus 로고    scopus 로고
    • Plug flow cytometry: An automated coupling device for rapid sequential flow cytometric sample analysis
    • Edwards, B. S., F. Kuckuck, and L. A. Sklar. 1999. Plug flow cytometry: an automated coupling device for rapid sequential flow cytometric sample analysis. Cytometry 37:156-159.
    • (1999) Cytometry , vol.37 , pp. 156-159
    • Edwards, B.S.1    Kuckuck, F.2    Sklar, L.A.3
  • 16
    • 0020080740 scopus 로고
    • Regulatory flexibility of methylotrophic yeasts in chemostat cultures-simultaneous assimilation of glucose and methanol at a fixed dilution rate
    • Egli, T., O. Kappeli, and A. Fiechter. 1982. Regulatory flexibility of methylotrophic yeasts in chemostat cultures-simultaneous assimilation of glucose and methanol at a fixed dilution rate. Arch. Microbiol. 131:1-7.
    • (1982) Arch. Microbiol. , vol.131 , pp. 1-7
    • Egli, T.1    Kappeli, O.2    Fiechter, A.3
  • 21
    • 0035921173 scopus 로고    scopus 로고
    • Analysis of single-chain antibody production in Pichia pastoris using on-line methanol control in fed-batch and mixed-feed fermentations
    • Hellwig, S., F. Emde, N. P. G. Raven, M. Henke, P. van der Logt, and R. Fischer. 2001. Analysis of single-chain antibody production in Pichia pastoris using on-line methanol control in fed-batch and mixed-feed fermentations. Biotechnol. Bioeng. 74:344-352.
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 344-352
    • Hellwig, S.1    Emde, F.2    Raven, N.P.G.3    Henke, M.4    Van Der Logt, P.5    Fischer, R.6
  • 22
    • 3142707454 scopus 로고    scopus 로고
    • The application of multiparameter flow cytometry to monitor individual microbial cell physiological state
    • Hewitt, C. J., and G. Nebe-Von-Caron. 2004. The application of multiparameter flow cytometry to monitor individual microbial cell physiological state. Adv. Biochem. Eng. Biotechnol. 89:197-223.
    • (2004) Adv. Biochem. Eng. Biotechnol. , vol.89 , pp. 197-223
    • Hewitt, C.J.1    Nebe-Von-Caron, G.2
  • 23
    • 0035397672 scopus 로고    scopus 로고
    • An industrial application of multiparameter flow cytometry: Assessment of cell physiological state and its application to the study of microbial fermentations
    • Hewitt, C. J., and G. Nebe-Von-Caron. 2001. An industrial application of multiparameter flow cytometry: assessment of cell physiological state and its application to the study of microbial fermentations. Cytometry 44:179-187.
    • (2001) Cytometry , vol.44 , pp. 179-187
    • Hewitt, C.J.1    Nebe-Von-Caron, G.2
  • 24
    • 0032874774 scopus 로고    scopus 로고
    • The use of multi-parameter flow cytometry to compare the physiological response of Escherichia coli W3110 to glucose limitation during batch, fedbatch and continuous culture cultivations
    • Hewitt, C. J., G. Nebe-von Caron, A. W. Nienow, and C. M. McFarlane. 1999. The use of multi-parameter flow cytometry to compare the physiological response of Escherichia coli W3110 to glucose limitation during batch, fedbatch and continuous culture cultivations. J. Biotechnol. 75:251-264.
    • (1999) J. Biotechnol. , vol.75 , pp. 251-264
    • Hewitt, C.J.1    Nebe-von Caron, G.2    Nienow, A.W.3    McFarlane, C.M.4
  • 25
    • 0033587372 scopus 로고    scopus 로고
    • Use of multi-staining flow cytometry to characterise the physiological state of Escherichia coli W3110 in high cell density fed-batch cultures
    • Hewitt, C. J., G. Nebe-Von Caron, A. W. Nienow, and C. M. McFarlane. 1999. Use of multi-staining flow cytometry to characterise the physiological state of Escherichia coli W3110 in high cell density fed-batch cultures. Biotechnol. Bioeng. 63:705-711.
    • (1999) Biotechnol. Bioeng. , vol.63 , pp. 705-711
    • Hewitt, C.J.1    Nebe-Von Caron, G.2    Nienow, A.W.3    McFarlane, C.M.4
  • 26
    • 0037346720 scopus 로고    scopus 로고
    • A comparative study of carboxyfluorescein diacetate and carboxyfluorescein diacetate succinimidyl ester as indicators of bacterial activity
    • DOI 10.1016/S0167-7012(02)00207-5, PII S0167701202002075
    • Hoefel, D., W. L. Grooby, P. T. Monis, S. Andrews, and C. P. Saint. 2003. A comparative study of carboxyfluorescein diacetate and carboxyfluorescein diacetate succinimidyl ester as indicators of bacterial activity. J. Microbiol. Methods 52:379-388. (Pubitemid 36078423)
    • (2003) Journal of Microbiological Methods , vol.52 , Issue.3 , pp. 379-388
    • Hoefel, D.1    Grooby, W.L.2    Monis, P.T.3    Andrews, S.4    Saint, C.P.5
  • 27
    • 0038364057 scopus 로고    scopus 로고
    • Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry
    • Hohenblum, H., N. Borth, and D. Mattanovich. 2003. Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry. J. Biotechnol. 102:281-290.
    • (2003) J. Biotechnol. , vol.102 , pp. 281-290
    • Hohenblum, H.1    Borth, N.2    Mattanovich, D.3
  • 28
    • 0442309687 scopus 로고    scopus 로고
    • Effects of Gene Dosage, Promoters, and Substrates on Unfolded Protein Stress of Recombinant Pichia pastoris
    • DOI 10.1002/bit.10904
    • Hohenblum, H., B. Gasser, M. Maurer, N. Borth, and D. Mattanovich. 2004. Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris. Biotechnol. Bioeng. 85:367-375. (Pubitemid 38186091)
    • (2004) Biotechnology and Bioengineering , vol.85 , Issue.4 , pp. 367-375
    • Hohenblum, H.1    Gasser, B.2    Maurer, M.3    Borth, N.4    Mattanovich, D.5
  • 29
    • 0037143788 scopus 로고    scopus 로고
    • Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
    • DOI 10.1002/bit.10297
    • Hong, F., N. Q. Meinander, and L. J. Jonsson. 2002. Fermentation strategies for improved heterologous expression of lacease in Pichia pastoris. Biotechnol. Bioeng. 79:438-449. (Pubitemid 34847321)
    • (2002) Biotechnology and Bioengineering , vol.79 , Issue.4 , pp. 438-449
    • Hong, F.1    Meinander, N.Q.2    Jonsson, L.J.3
  • 30
    • 27744437468 scopus 로고    scopus 로고
    • A study of the physiological response of Pichia pastoris growing in a continuous culture to an induced stress situation
    • Hyka, P., L. Paulova, M. Egger, and K. Melzoch. 2005. A study of the physiological response of Pichia pastoris growing in a continuous culture to an induced stress situation. Chimia 59:741-744.
    • (2005) Chimia , vol.59 , pp. 741-744
    • Hyka, P.1    Paulova, L.2    Egger, M.3    Melzoch, K.4
  • 31
    • 77954306498 scopus 로고    scopus 로고
    • Invitrogen
    • version B 053002, Invitrogen, Carlsbad, CA
    • Invitrogen. 2002. Pichia fermentation process guidelines, version B 053002, p. 1-11. Invitrogen, Carlsbad, CA.
    • (2002) Pichia Fermentation Process Guidelines , pp. 1-11
  • 32
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • Jahic, M., M. Gustavsson, A. K. Jansen, M. Martinelle, and S. O. Enfors. 2003. Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J. Biotechnol. 102:45-53.
    • (2003) J. Biotechnol. , vol.102 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.K.3    Martinelle, M.4    Enfors, S.O.5
  • 33
    • 33845497166 scopus 로고    scopus 로고
    • Process technology for production and recovery of heterologous proteins with Pichia pastoris
    • DOI 10.1021/bp060171t
    • Jahic, M., A. Veide, T. Charoenrat, T. Teeri, and S. O. Enfors. 2006. Process technology for production and recovery of heterologous proteins with Pichia pastoris. Biotechnol. Prog. 22:1465-1473. (Pubitemid 44912651)
    • (2006) Biotechnology Progress , vol.22 , Issue.6 , pp. 1465-1473
    • Jahic, M.1    Veide, A.2    Charoenrat, T.3    Teeri, T.4    Enfors, S.-O.5
  • 34
    • 0028102761 scopus 로고
    • Staining of Escherichia coli for flow cytometry: Influx and efflux of ethidium bromide
    • Jernaes, M. W., and H. B. Steen. 1994. Staining of Escherichia coli for flow cytometry: influx and efflux of ethidium bromide. Cytometry 17:302-309.
    • (1994) Cytometry , vol.17 , pp. 302-309
    • Jernaes, M.W.1    Steen, H.B.2
  • 35
    • 0031560764 scopus 로고    scopus 로고
    • Metabolic flux distributions in recombinant Saccharomyces cerevisiae during foreign protein production
    • Jin, S., K. Ye, and K. Shimizu. 1997. Metabolic flux distributions in recombinant Saccharomyces cerevisiae during foreign protein production. J. Biotechnol. 54:161-174.
    • (1997) J. Biotechnol. , vol.54 , pp. 161-174
    • Jin, S.1    Ye, K.2    Shimizu, K.3
  • 36
    • 0347093698 scopus 로고    scopus 로고
    • Recombinant cold-adapted trypsin i from Atlantic cod-expression, purification, and identification
    • Jonsdottir, G., J. B. Bjarnason, and A. Gudmundsdottir. 2004. Recombinant cold-adapted trypsin I from Atlantic cod-expression, purification, and identification. Protein Expr. Purif. 33:110-122.
    • (2004) Protein Expr. Purif. , vol.33 , pp. 110-122
    • Jonsdottir, G.1    Bjarnason, J.B.2    Gudmundsdottir, A.3
  • 37
    • 0033758509 scopus 로고    scopus 로고
    • Use of fluorescent probes to assess physiological functions of bacteria at single-cell level
    • Joux, F., and P. Lebaron. 2000. Use of fluorescent probes to assess physiological functions of bacteria at single-cell level. Microbes Infect. 2:1523-1535.
    • (2000) Microbes Infect. , vol.2 , pp. 1523-1535
    • Joux, F.1    Lebaron, P.2
  • 39
    • 1842556114 scopus 로고    scopus 로고
    • Single-cell variability in growing Saccharomyces cerevisiae cell populations measured with automated flow cytometry
    • Kacmar, J., A. Zamamiri, R. Carlson, N. R. Abu-Absi, and F. Srienc. 2004. Single-cell variability in growing Saccharomyces cerevisiae cell populations measured with automated flow cytometry. J. Biotechnol. 109:239-254.
    • (2004) J. Biotechnol. , vol.109 , pp. 239-254
    • Kacmar, J.1    Zamamiri, A.2    Carlson, R.3    Abu-Absi, N.R.4    Srienc, F.5
  • 40
    • 0035151514 scopus 로고    scopus 로고
    • Low external pH induces HOG1-dependent changes in the organization of the Saccharomyces cerevisiae cell wall
    • Kapteyn, J. C., B. ter Riet, E. Vink, S. Blad, H. De Nobel, H. Van Den Ende, and F. M. Klis. 2001. Low external pH induces HOG1-dependent changes in the organization of the Saccharomyces cerevisiae cell wall. Mol. Microbiol. 39:469-479.
    • (2001) Mol. Microbiol. , vol.39 , pp. 469-479
    • Kapteyn, J.C.1    Ter Riet, B.2    Vink, E.3    Blad, S.4    De Nobel, H.5    Van Den Ende, H.6    Klis, F.M.7
  • 41
    • 33646042890 scopus 로고    scopus 로고
    • Impact of methanol concentration on secreted protein production in oxygen-limited cultures of recombinant Pichia pastoris
    • Khatri, N. K., and F. Hoffmann. 2006. Impact of methanol concentration on secreted protein production in oxygen-limited cultures of recombinant Pichia pastoris. Biotechnol. Bioeng. 93:871-879.
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 871-879
    • Khatri, N.K.1    Hoffmann, F.2
  • 42
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • Kowalski, J. M., R. N. Parekh, J. Mao, and K. D. Wittrup. 1998. Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control. J. Biol. Chem. 273:19453-19458.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19453-19458
    • Kowalski, J.M.1    Parekh, R.N.2    Mao, J.3    Wittrup, K.D.4
  • 43
    • 0020523472 scopus 로고
    • Studies on the mechanism of the antifungal action of benzoate
    • Krebs, H. A., D. Wiggins, M. Stubbs, A. Sols, and F. Bedoya. 1983. Studies on the mechanism of the antifungal action of benzoate. Biochem. J. 214: 657-663. (Pubitemid 13023577)
    • (1983) Biochemical Journal , vol.214 , Issue.3 , pp. 657-663
    • Krebs, H.A.1    Wiggins, D.2    Stubbs, M.3
  • 44
    • 1342290473 scopus 로고    scopus 로고
    • Overexpression of ovine leptin in Pichia pastoris: Physiological yeast response to leptin production and characterization of the recombinant hormone
    • Laborde, C., P. Chemardin, F. Bigey, Y. Combarnous, G. Moulin, and H. Boze. 2004. Overexpression of ovine leptin in Pichia pastoris: physiological yeast response to leptin production and characterization of the recombinant hormone. Yeast 21:249-263.
    • (2004) Yeast , vol.21 , pp. 249-263
    • Laborde, C.1    Chemardin, P.2    Bigey, F.3    Combarnous, Y.4    Moulin, G.5    Boze, H.6
  • 45
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during assembly of head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 46
    • 27844523810 scopus 로고    scopus 로고
    • Flow-cytometric detection of changes in the physiological state of E. coli expressing a heterologous membrane protein during carbon-limited fedbatch cultivation
    • Looser, V., F. Hammes, M. Keller, M. Berney, K. Kovar, and T. Egli. 2005. Flow-cytometric detection of changes in the physiological state of E. coli expressing a heterologous membrane protein during carbon-limited fedbatch cultivation. Biotechnol. Bioeng. 92:69-78.
    • (2005) Biotechnol. Bioeng. , vol.92 , pp. 69-78
    • Looser, V.1    Hammes, F.2    Keller, M.3    Berney, M.4    Kovar, K.5    Egli, T.6
  • 47
    • 0034799275 scopus 로고    scopus 로고
    • Population dynamics of a continuous fermentation of recombinant Saccharomyces cerevisiae using flow cytometry
    • Lu Chau, T., A. Guillan, E. Roca, M. J. Nunez, and J. M. Lema. 2001. Population dynamics of a continuous fermentation of recombinant Saccharomyces cerevisiae using flow cytometry. Biotechnol. Prog. 17:951-957.
    • (2001) Biotechnol. Prog. , vol.17 , pp. 951-957
    • Lu Chau, T.1    Guillan, A.2    Roca, E.3    Nunez, M.J.4    Lema, J.M.5
  • 48
    • 4544253524 scopus 로고    scopus 로고
    • Stress in recombinant protein producing yeasts
    • DOI 10.1016/j.jbiotec.2004.04.035, PII S0168165604003104
    • Mattanovich, D., B. Gasser, H. Hohenblum, and M. Sauer. 2004. Stress in recombinant protein producing yeasts. J. Biotechnol. 113:121-135. (Pubitemid 39237075)
    • (2004) Journal of Biotechnology , vol.113 , Issue.1-3 , pp. 121-135
    • Mattanovich, D.1    Gasser, B.2    Hohenblum, H.3    Sauer, M.4
  • 49
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori, K., A. Sant, K. Kohno, K. Normington, M. J. Gething, and J. F. Sambrook. 1992. A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J. 11:2583-2593.
    • (1992) EMBO J. , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 50
    • 18444396293 scopus 로고    scopus 로고
    • Relationship between pH and medium dissolved solids in terms of growth and metabolism of lactobacilli and Saccharomyces cerevisiae during ethanol production
    • Narendranath, N. V., and R. Power. 2005. Relationship between pH and medium dissolved solids in terms of growth and metabolism of lactobacilli and Saccharomyces cerevisiae during ethanol production. Appl. Environ. Microbiol. 71:2239-2243.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2239-2243
    • Narendranath, N.V.1    Power, R.2
  • 51
    • 60849109950 scopus 로고    scopus 로고
    • Standardization in microbial cytometry
    • Nebe-von-Caron, G. 2009. Standardization in microbial cytometry. Cytometry A 75:86-89.
    • (2009) Cytometry A , vol.75 , pp. 86-89
    • Nebe-von-Caron, G.1
  • 52
    • 0035996702 scopus 로고    scopus 로고
    • Optimization of the expression of equistatin in Pichia pastoris
    • Outchkourov, N. S., W. J. Stiekema, and M. A. Jongsma. 2002. Optimization of the expression of equistatin in Pichia pastoris. Protein Expr. Purif. 24:18-24.
    • (2002) Protein Expr. Purif. , vol.24 , pp. 18-24
    • Outchkourov, N.S.1    Stiekema, W.J.2    Jongsma, M.A.3
  • 53
    • 34250832133 scopus 로고    scopus 로고
    • Application of flow cytometry to segregated kinetic modeling based on the physiological states of microorganisms
    • Quires, C., M. Herrero, L. A. Garcia, and M. Diaz. 2007. Application of flow cytometry to segregated kinetic modeling based on the physiological states of microorganisms. Appl. Environ. Microbiol. 73:3993-4000.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 3993-4000
    • Quires, C.1    Herrero, M.2    Garcia, L.A.3    Diaz, M.4
  • 54
    • 0027476379 scopus 로고
    • Saccharomyces cerevisiae, protein secretion into the growth medium depends on environmental factors
    • Rossini, D., D. Porro, L. Brambilla, M. Venturini, B. M. Ranzi, M. Vanoni, and L. Alberghina. 1993. In Saccharomyces cerevisiae, protein secretion into the growth medium depends on environmental factors. Yeast 9:77-84.
    • (1993) Yeast , vol.9 , pp. 77-84
    • Rossini, D.1    Porro, D.2    Brambilla, L.3    Venturini, M.4    Ranzi, B.M.5    Vanoni, M.6    Alberghina, L.7
  • 56
    • 0038057544 scopus 로고    scopus 로고
    • Optimal conditions for the expression of a single-chain antibody (scFv) gene in Pichia pastoris
    • DOI 10.1016/S1046-5928(02)00706-4
    • Shi, X., T. Karkut, M. Chamankhah, M. Alting-Mees, S. M. Hemmingsen, and D. Hegedus. 2003. Optimal conditions for the expression of a single-chain antibody (scFv) gene in Pichia pastoris. Protein Expr. Purif. 28:321-330. 57. Stratton, J., V. Chiruvolu, and M. Meagher. 1998. High cell-density fermentation. Methods Mol. Biol. 103:107-120. (Pubitemid 36562423)
    • (2003) Protein Expression and Purification , vol.28 , Issue.2 , pp. 321-330
    • Shi, X.1    Karkut, T.2    Chamankhah, M.3    Alting-Mees, M.4    Hemmingsen, S.M.5    Hegedus, D.6
  • 57
    • 5444226007 scopus 로고    scopus 로고
    • Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena
    • Weis, R., R. Luiten, W. Skranc, H. Schwab, M. Wubbolts, and A. Glieder. 2004. Reliable high-throughput screening with Pichia pastoris by limiting yeast cell death phenomena. FEMS Yeast Res. 5:179-189.
    • (2004) FEMS Yeast Res. , vol.5 , pp. 179-189
    • Weis, R.1    Luiten, R.2    Skranc, W.3    Schwab, H.4    Wubbolts, M.5    Glieder, A.6
  • 58
    • 33749035242 scopus 로고    scopus 로고
    • Improvement of cell viability and hirudin production by ascorbic acid in Pichia pastoris fermentation
    • Xiao, A., X. Zhou, L. Zhou, and Y. Zhang. 2006. Improvement of cell viability and hirudin production by ascorbic acid in Pichia pastoris fermentation. Appl. Microbiol. Biotechnol. 72:837-844.
    • (2006) Appl. Microbiol. Biotechnol. , vol.72 , pp. 837-844
    • Xiao, A.1    Zhou, X.2    Zhou, L.3    Zhang, Y.4
  • 59
    • 0034610097 scopus 로고    scopus 로고
    • Modeling Pichia pastoris growth on methanol and optimizing the production of a recombinant protein, the heavy-chain fragment C of botulinum neurotoxin, serotype A
    • Zhang, W., M. A. Bevins, B. A. Plantz, L. A. Smith, and M. M. Meagher. 2000. Modeling Pichia pastoris growth on methanol and optimizing the production of a recombinant protein, the heavy-chain fragment C of botulinum neurotoxin, serotype A. Biotechnol. Bioeng. 70:1-8.
    • (2000) Biotechnol. Bioeng. , vol.70 , pp. 1-8
    • Zhang, W.1    Bevins, M.A.2    Plantz, B.A.3    Smith, L.A.4    Meagher, M.M.5


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