메뉴 건너뛰기




Volumn 46, Issue 8, 2011, Pages 1663-1669

High efficient production of recombinant human consensus interferon mutant in high cell density culture of Pichia pastoris using two phases methanol control

Author keywords

Cell physiology; Disulfide bond; Pichia pastoris; Recombinant human consensus interferon mutant; Specific growth rate

Indexed keywords

CELL PHYSIOLOGY; DISULFIDE BONDS; PICHIA PASTORIS; RECOMBINANT HUMAN CONSENSUS INTERFERON MUTANT; SPECIFIC GROWTH RATE;

EID: 79960023556     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2011.05.015     Document Type: Article
Times cited : (11)

References (45)
  • 1
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • DOI 10.1002/yea.1208
    • S. Macauley-Patrick, M.L. Fazenda, B. McNeil, and L.M. Harvey Heterologous protein production using the Pichia pastoris expression system Yeast 22 2005 249 270 (Pubitemid 40528349)
    • (2005) Yeast , vol.22 , Issue.4 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 2
    • 33748425718 scopus 로고    scopus 로고
    • A simple model-based control for Pichia pastoris allows a more efficient heterologous protein production bioprocess
    • DOI 10.1002/bit.21005
    • O. Cos, R. Ramon, J.L. Montesinos, and F. Valero A simple model-based control for Pichia pastoris allows a more efficient heterologous protein production bioprocess Biotechnol Bioeng 95 2006 145 154 (Pubitemid 44342358)
    • (2006) Biotechnology and Bioengineering , vol.95 , Issue.1 , pp. 145-154
    • Cos, O.1    Ramon, R.2    Montesinos, J.L.3    Valero, F.4
  • 3
    • 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
    • W.H. Zhang, M.A. Bevins, B.A. Plantz, L.A. Smith, and M.M. Meagher 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 2000 1 8
    • (2000) Biotechnol Bioeng , vol.70 , pp. 1-8
    • Zhang, W.H.1    Bevins, M.A.2    Plantz, B.A.3    Smith, L.A.4    Meagher, M.M.5
  • 4
    • 14744299579 scopus 로고
    • Recent advances in the expression of foreign genes in Pichia pastoris
    • DOI 10.1038/nbt0893-905
    • J.M. Cregg, T.S. Vedvick, and W.C. Raschke Recent advances in the expression of foreign genes in Pichia pastoris Biotechnology 11 1993 905 910 (Pubitemid 23218978)
    • (1993) Bio/Technology , vol.11 , Issue.8 , pp. 905-910
    • Cregg, J.M.1    Vedvick, T.S.2    Raschke, W.C.3
  • 5
    • 0037419716 scopus 로고    scopus 로고
    • Effects of methanol concentration on expression levels of recombinant protein in fed-batch cultures of Pichia methanolica
    • DOI 10.1002/bit.10464
    • B.E. Mayson, D.G. Kilburn, B.L. Zamost, C.K. Raymond, and G.J. Lesnicki Effects of methanol concentration on expression levels of recombinant protein in fed-batch cultures of Pichia methanolica Biotechnol Bioeng 81 2003 291 298 (Pubitemid 36098485)
    • (2003) Biotechnology and Bioengineering , vol.81 , Issue.3 , pp. 291-298
    • Mayson, B.E.1    Kilburn, D.G.2    Zamost, B.L.3    Raymond, C.K.4    Lesnicki, G.J.5
  • 6
    • 37049021103 scopus 로고    scopus 로고
    • Production of Single-Chain Variable Fragment Antibody (scFv) in Fed-Batch and Continuous Culture of Pichia pastoris by Two Different Methanol Feeding Methods
    • DOI 10.1263/jbb.104.403, PII S1389172307701809
    • S. Yamawaki, T. Matsumoto, Y. Ohnishi, Y. Kumada, N. Shiomi, and T. Katsuda Production of single-chain variable fragment antibody (scFv) in fed-batch and continuous culture of Pichia pastoris by two different methanol feeding methods J Biosci Bioeng 104 2007 403 407 (Pubitemid 350251295)
    • (2007) Journal of Bioscience and Bioengineering , vol.104 , Issue.5 , pp. 403-407
    • Yamawaki, S.1    Matsumoto, T.2    Ohnishi, Y.3    Kumada, Y.4    Shiomi, N.5    Katsuda, T.6    Lee, E.K.7    Katoh, S.8
  • 7
    • 0001876236 scopus 로고
    • Production, characterization and biological effects of recombinant DNA derived human IFN-α and IFN-γ analogs
    • E. De Maeyer, H. Schellekens, Elsevier Amsterdam
    • K. Alton, Y. Stabinsky, R. Richards, B. Ferguson, L. Goldstein, and B. Altrock Production, characterization and biological effects of recombinant DNA derived human IFN-α and IFN-γ analogs E. De Maeyer, H. Schellekens, The biology of the interferon system 1983 Elsevier Amsterdam 119 128
    • (1983) The Biology of the Interferon System , pp. 119-128
    • Alton, K.1    Stabinsky, Y.2    Richards, R.3    Ferguson, B.4    Goldstein, L.5    Altrock, B.6
  • 8
    • 0029833999 scopus 로고    scopus 로고
    • The biologic activity and molecular characterization of a novel synthetic interferon-alpha species, consensus interferon
    • L.M. Blatt, J.M. Davis, S.B. Klein, and M.W. Taylor The biologic activity and molecular characterization of a novel synthetic interferon-alpha species, consensus interferon J Interferon Cytokine Res 16 1996 489 499 (Pubitemid 26306949)
    • (1996) Journal of Interferon and Cytokine Research , vol.16 , Issue.7 , pp. 489-499
    • Blatt, L.M.1    Davis, J.M.2    Klein, S.B.3    Taylor, M.W.4
  • 9
    • 0027058741 scopus 로고
    • A comparison of interferon-Con1 with natural recombinant interferons-α: Antiviral, antiproliferative, and natural killer-inducing activities
    • O.N. Ozes, Z. Reiter, S. Kelin, L.M. Blatt, and M.W. Taylor A comparison of interferon-Con1 with natural recombinant interferon-α: antiviral, antiproliferative and natural killer inducing activities J Interferon Res 12 1992 55 59 (Pubitemid 23071073)
    • (1992) Journal of Interferon Research , vol.12 , Issue.1 , pp. 55-59
    • Ozes, O.N.1    Reiter, Z.2    Klein, S.3    Blatt, L.M.4    Taylor, M.W.5
  • 11
    • 24044505375 scopus 로고    scopus 로고
    • Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding
    • DOI 10.1016/j.ymben.2005.04.002, PII S1096717605000431
    • P. Xu, D. Raden, F.J. Doyle III, and A.S. Robinson Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding Metab Eng 7 2005 269 279 (Pubitemid 41225444)
    • (2005) Metabolic Engineering , vol.7 , Issue.4 , pp. 269-279
    • Xu, P.1    Raden, D.2    Doyle III, F.J.3    Robinson, A.S.4
  • 14
    • 36849034496 scopus 로고    scopus 로고
    • High level production and purification of human interferon α2b in high cell density culture of Pichia pastoris
    • DOI 10.1016/j.enzmictec.2007.09.006, PII S0141022907003080
    • A. Ayed, I. Rabhi, K. Dellagi, and H. Kallel High level production and purification of human interferon-2b in high cell density culture of Pichia pastoris Enzyme Microb Technol 42 2008 173 180 (Pubitemid 350235596)
    • (2008) Enzyme and Microbial Technology , vol.42 , Issue.2 , pp. 173-180
    • Ayed, A.1    Rabhi, I.2    Dellagi, K.3    Kallel, H.4
  • 17
    • 53249107196 scopus 로고    scopus 로고
    • Inhibition of degradation and aggregation of recombinant human consensus interferon-α mutant expressed in Pichia pastoris with complex medium in bioreactor
    • D. Wu, Y.Y. Hao, J. Chu, Y.P. Zhuang, and S.L. Zhang Inhibition of degradation and aggregation of recombinant human consensus interferon-α mutant expressed in Pichia pastoris with complex medium in bioreactor Appl Microbiol Biotechnol 80 2008 1063 1071
    • (2008) Appl Microbiol Biotechnol , vol.80 , pp. 1063-1071
    • Wu, D.1    Hao, Y.Y.2    Chu, J.3    Zhuang, Y.P.4    Zhang, S.L.5
  • 18
    • 0032416188 scopus 로고    scopus 로고
    • 2- glycoprotein I domain V by a recombinant Pichia pastoris: A simple system for the control of methanol concentration using a semiconductor gas sensor
    • DOI 10.1016/S0922-338X(98)80156-6
    • Y. Katakura, W.H. Zhang, G.Q. Zhuang, T. Omasa, M. Kishimoto, and Y.J. Goto Effect of methanol concentration on the production of human Pz-glycoprotein I domain V by a recombinant Pichia pastoris: a simple system for the control of methanol concentration using a semiconductor gas sensor J Ferment Bioeng 86 1998 482 487 (Pubitemid 29008737)
    • (1998) Journal of Fermentation and Bioengineering , vol.86 , Issue.5 , pp. 482-487
    • Katakura, Y.1    Zhang, W.2    Zhuang, G.3    Omasa, T.4    Kishimoto, M.5    Goto, Y.6    Suga, K.-I.7
  • 19
    • 0026456864 scopus 로고
    • The enhancement of specific antibody production rate in glucose- and glutamine-controlled fed-batch culture
    • T. Omasa, M. Ishimoto, K. Higashiyama, S. Shioya, and K. Suga The enhancement of specific antibody production rate in glucose- and glutamine-controlled fed-batch culture Cytotechnology 8 1992 75 84
    • (1992) Cytotechnology , vol.8 , pp. 75-84
    • Omasa, T.1    Ishimoto, M.2    Higashiyama, K.3    Shioya, S.4    Suga, K.5
  • 20
    • 0027112176 scopus 로고
    • Effects of lactate concentration on hybridoma culture in lactate-controlled fed-batch operation
    • T. Omasa, K. Higashiyama, S. Shioya, and K. Suga Effects of lactate concentration on hybridoma culture in lactate-controlled fed-batch operation Biotechnol Bioeng 39 1992 556 564
    • (1992) Biotechnol Bioeng , vol.39 , pp. 556-564
    • Omasa, T.1    Higashiyama, K.2    Shioya, S.3    Suga, K.4
  • 21
    • 0021306856 scopus 로고
    • Systems for polyacrylamide gel electrophoresis
    • P.J. Blackshear Systems for polyacrylamide gel electrophoresis Methods Enzymol 104 1984 237 255 (Pubitemid 14159520)
    • (1983) Methods in Enzymology , vol.VOL. 104 , pp. 237-255
    • Blackshear, P.J.1
  • 22
    • 76849093775 scopus 로고    scopus 로고
    • Incomplete formation of intramolecular disulfide bond triggers degradation and aggregation of human consensus interferon-α mutant by Pichia pastoris
    • D. Wu, D. Ma, Y.Y. Hao, J. Chu, Y.H. Wang, and Y.P. Zhuang Incomplete formation of intramolecular disulfide bond triggers degradation and aggregation of human consensus interferon-α mutant by Pichia pastoris Appl Microbiol Biotechnol 85 2010 1759 1767
    • (2010) Appl Microbiol Biotechnol , vol.85 , pp. 1759-1767
    • Wu, D.1    Ma, D.2    Hao, Y.Y.3    Chu, J.4    Wang, Y.H.5    Zhuang, Y.P.6
  • 23
    • 1842400660 scopus 로고
    • Screening and identification of Candida methanosorbosa as alcohol oxidase-producing methanol using yeast
    • S. Suye, A. Ogawa, S. Yokoyama, and A. Obayashi Screening and identification of Candida methanosorbosa as alcohol oxidase-producing methanol using yeast Agric Biol Chem 54 1990 1297 1298
    • (1990) Agric Biol Chem , vol.54 , pp. 1297-1298
    • Suye, S.1    Ogawa, A.2    Yokoyama, S.3    Obayashi, A.4
  • 25
    • 16344365158 scopus 로고    scopus 로고
    • Maximization of production of secreted recombinant proteins in Pichia pastoris fed-batch fermentation
    • DOI 10.1021/bp049811n
    • W.H. Zhang, J. Sinha, L.A. Smith, M. Inan, and M.M. Meagher Maximization of production of secreted recombinant proteins in Pichia pastoris fed-batch fermentation Biotechnol Prog 21 2005 386 393 (Pubitemid 40466409)
    • (2005) Biotechnology Progress , vol.21 , Issue.2 , pp. 386-393
    • Zhang, W.1    Sinha, J.2    Smith, L.A.3    Inan, M.4    Meagher, M.M.5
  • 26
    • 0001769993 scopus 로고
    • Optimization and control in fed-batch bioreactors
    • S. Shioya Optimization and control in fed-batch bioreactors Adv Biochem Eng Biotechnol 46 1992 112 142
    • (1992) Adv Biochem Eng Biotechnol , vol.46 , pp. 112-142
    • Shioya, S.1
  • 28
    • 0036734202 scopus 로고    scopus 로고
    • Decrease of proteolytic degradation of recombinant hirudin produced by Pichia pastoris by controlling the specific growth rate
    • X.S. Zhou, and Y.X. Zhang Decrease of proteolytic degradation of recombinant hirudin produced by Pichia pastoris by controlling the specific growth rate Biotechnol Lett 24 2002 1449 1453
    • (2002) Biotechnol Lett , vol.24 , pp. 1449-1453
    • Zhou, X.S.1    Zhang, Y.X.2
  • 29
    • 0032788590 scopus 로고    scopus 로고
    • Amino acid neighbours and detailed conformational analysis of cysteines in proteins
    • M.T.N. Petersen, P.H. Jonson, and S.B. Petersen Amino acid neighbours and detailed conformational analysis of cysteines in proteins Protein Eng 12 1999 535 548 (Pubitemid 29368960)
    • (1999) Protein Engineering , vol.12 , Issue.7 , pp. 535-548
    • Petersen, M.T.N.1    Jonson, P.H.2    Petersen, S.B.3
  • 30
    • 0023892436 scopus 로고
    • Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature
    • C.H. Schein, and M.H.M. Noteborn Formation of soluble recombinant proteins in Escherichia coli is favored by lower growth temperature Biotechnology 6 1988 291 294
    • (1988) Biotechnology , vol.6 , pp. 291-294
    • Schein, C.H.1    Noteborn, M.H.M.2
  • 31
    • 0036704245 scopus 로고    scopus 로고
    • Aggregate formation and the structure of the aggregates of disulfide-reduced proteins
    • DOI 10.1023/A:1021138718046
    • K. Takase, T. Higashi, and T. Omura Aggregate formation and the structure of the aggregates of disulfide-reduced proteins J Protein Chem 21 2002 427 433 (Pubitemid 35423354)
    • (2002) Journal of Protein Chemistry , vol.21 , Issue.6 , pp. 427-433
    • Takase, K.1    Higashi, T.2    Omura, T.3
  • 32
    • 0037143788 scopus 로고    scopus 로고
    • Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
    • DOI 10.1002/bit.10297
    • F. Hong, N.Q. Meinander, and L.J. Jonsson Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris Biotechnol Bioeng 79 4 2002 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
  • 33
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • M. Jahic, M. Gustavsson, A.K. Jansen, M. Martinelle, and S.O. Enfors Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes J Biotechnol 102 2003 42 53
    • (2003) J Biotechnol , vol.102 , pp. 42-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.K.3    Martinelle, M.4    Enfors, S.O.5
  • 34
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • DOI 10.1006/prep.2001.1395
    • Z. Li, F. Xiong, Q.S. Lin, M. d'Anjou, A.J. Daugulis, and D.S.C. Yang Low temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris Protein Expr Purif 21 3 2001 438 445 (Pubitemid 34179417)
    • (2001) Protein Expression and Purification , vol.21 , Issue.3 , pp. 438-445
    • Li, Z.1    Xiong, F.2    Lin, Q.3    D'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.C.6    Hew, C.L.7
  • 35
    • 0033809942 scopus 로고    scopus 로고
    • Expression of recombinant galactose oxidase by Pichia pastoris
    • M.M. Whittaker, and J.W. Whittaker Expression of recombinant galactose oxidase by Pichia pastoris Protein Expr Purif 20 2000 105 111
    • (2000) Protein Expr Purif , vol.20 , pp. 105-111
    • Whittaker, M.M.1    Whittaker, J.W.2
  • 36
    • 0036411891 scopus 로고    scopus 로고
    • Expression and purification of a small cytokine growth-blocking peptide from armyworm Pseudaletia separata by an optimized fermentation method using the methylotrophic yeast Pichia pastoris
    • DOI 10.1016/S1046-5928(02)00036-0, PII S1046592802000360
    • N. Koganesawa, T. Aizava, H. Shimojo, K. Miura, A. Ohnishi, and M. Demura Expression and purification of a small cytokine growth-blocking peptide from armyworm Pseudaletia separata by an optimized fermentation method using the methylotrophic yeast Pichia pastoris Protein Expr Purif 25 3 2002 416 425 (Pubitemid 35293969)
    • (2002) Protein Expression and Purification , vol.25 , Issue.3 , pp. 416-425
    • Koganesawa, N.1    Aizawa, T.2    Shimojo, H.3    Miura, K.4    Ohnishi, A.5    Demura, M.6    Hayakawa, Y.7    Nitta, K.8    Kawano, K.9
  • 37
    • 0037617683 scopus 로고    scopus 로고
    • Cyclic fed-batch culture for production of human serum albumin in Pichia pastoris
    • DOI 10.1002/bit.10616
    • M.E. Bushell, M. Rowe, C.A. Avignone-Rossa, and J.N. Wardell Cyclic fed-batch culture for production of human serum albumin in Pichia pastoris Biotechnol Bioeng 82 2003 678 683 (Pubitemid 36576231)
    • (2003) Biotechnology and Bioengineering , vol.82 , Issue.6 , pp. 678-683
    • Bushell, M.E.1    Rowe, M.2    Avignone-Rossa, C.A.3    Wardell, J.N.4
  • 38
    • 10044227272 scopus 로고    scopus 로고
    • Reduced oxygen supply increases process stability and product yield with recombinant Pichia pastoris
    • DOI 10.1021/bp049711h
    • O. Trentmann, N.K. Khatri, and F. Hoffmann Reduced oxygen supply increases process stability and product yield with recombinant Pichia pastoris Biotechnol Prog 20 2004 1766 1775 (Pubitemid 39606460)
    • (2004) Biotechnology Progress , vol.20 , Issue.6 , pp. 1766-1775
    • Trentmann, O.1    Khatri, N.K.2    Hoffmann, F.3
  • 39
    • 0032806179 scopus 로고    scopus 로고
    • Use of Pichia pastoris for expression of recombinant proteins
    • DOI 10.1016/S0076-6879(99)06011-5
    • S.A. Rosenfeld Use of Pichia pastoris for expression of recombinant proteins Methods Enzymol 306 1999 154 169 (Pubitemid 29356830)
    • (1999) Methods in Enzymology , vol.306 , pp. 154-169
    • Rosenfeld, S.A.1
  • 40
    • 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
    • H. Hohenblum, B. Gasser, M. Maurer, N. Borth, and D. Mattanovich Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris Biotechnol Bioeng 85 2004 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
  • 41
    • 0031104672 scopus 로고    scopus 로고
    • Expression level tuning for optimal heterologous protein secretion in Saccharomyces cerevisiae
    • DOI 10.1021/bp970009d
    • R.N. Parekh, and K.D. Wittrup Expression level tuning for optimal heterologous protein secretion in Saccharomyces cerevisiae Biotechnol Prog 13 1997 117 122 (Pubitemid 27169864)
    • (1997) Biotechnology Progress , vol.13 , Issue.2 , pp. 117-122
    • Parekh, R.N.1    Wittrup, K.D.2
  • 42
    • 0029257263 scopus 로고
    • Constitutive overexpression of secreted heterologous proteins reduces BiP and PDI in yeast
    • A.S. Robinson, and K.D. Wittrup Constitutive overexpression of secreted heterologous proteins reduces BiP and PDI in yeast Biotechnol Prog 11 1995 171 177
    • (1995) Biotechnol Prog , vol.11 , pp. 171-177
    • Robinson, A.S.1    Wittrup, K.D.2
  • 43
    • 0029944822 scopus 로고    scopus 로고
    • Reduction of BiP levels decreases heterologous protein secretion in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.17.10017
    • A.S. Robinson, J.A. Bockhaus, A.C. Voegler, and K.D. Wittrup Reduction of BiP level decreases heterologous protein secretion in Saccharomyces cerevisiae J Biol Chem 271 1996 10017 10022 (Pubitemid 26131557)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.17 , pp. 10017-10022
    • Robinson, A.S.1    Bockhaus, J.A.2    Voegler, A.C.3    Wittrup, K.D.4
  • 44
    • 0031879861 scopus 로고    scopus 로고
    • Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments
    • DOI 10.1038/nbt0898-773
    • E.V. Shusta, R.T. Raines, A. Pluckthun, and K.D. Wittrup Increasing the secretory capacity of Saccharomyces cerevisiae for production of single-chain antibody fragments Nat Biotechnol 16 1998 773 777 (Pubitemid 28363761)
    • (1998) Nature Biotechnology , vol.16 , Issue.8 , pp. 773-777
    • Shusta, E.V.1    Raines, R.T.2    Pluckthun, A.3    Wittrup, K.D.4
  • 45
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • DOI 10.1016/S0955-0674(00)00219-2
    • C. Patil, and P. Walter Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals Curr Opin Cell Biol 13 2001 349 356 (Pubitemid 32429501)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.3 , pp. 349-356
    • Patil, C.1    Walter, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.