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Volumn 29, Issue 6, 2013, Pages 1377-1385

Optimization of five environmental factors to increase beta-propeller phytase production in Pichia pastoris and impact on the physiological response of the host

Author keywords

Beta propeller phytase; Physiological response; Pichia pastoris; Simplex optimization method

Indexed keywords

BETA-PROPELLER PHYTASE; EXTRACELLULAR PHYTASE; EXTRACELLULAR PROTEASE; OPTIMIZED CULTURE CONDITIONS; PHYSIOLOGICAL RESPONSE; PICHIA PASTORIS; RECOMBINANT PROTEIN SECRETION; SIMPLEX OPTIMIZATION;

EID: 84890145307     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.1822     Document Type: Article
Times cited : (21)

References (54)
  • 1
    • 0034767777 scopus 로고    scopus 로고
    • Biotechnological development of effective phytases for mineral nutrition and environmental protection
    • Lei XG, Stahl CH. Biotechnological development of effective phytases for mineral nutrition and environmental protection, Appl Microbiol Biotechnol. 2001;57:474-481.
    • (2001) Appl Microbiol Biotechnol. , vol.57 , pp. 474-481
    • Lei, X.G.1    Stahl, C.H.2
  • 3
    • 84890669450 scopus 로고    scopus 로고
    • Phytases: Attributes, catalytic mechanisms: applications
    • Turner L, Richardson AE, Mullaney EJ, editors, Oxfordshire: CAB International
    • Mullaney EJ, Ullah AHJ. Phytases: Attributes, catalytic mechanisms: applications. In: Turner L, Richardson AE, Mullaney EJ, editors. Inositol phosphates: linking agriculture and the environment. Oxfordshire: CAB International; 2007:97-110.
    • (2007) Inositol phosphates: linking agriculture and the environment , pp. 97-110
    • Mullaney, E.J.1    Ullah, A.H.J.2
  • 5
    • 0031747416 scopus 로고    scopus 로고
    • Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis
    • Kerovuo J, Lauraeus M, Nurminen P, Kalkkinen N, Apajalahti J. Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis. Appl Environ Microbiol. 1998;64:2079-2085.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2079-2085
    • Kerovuo, J.1    Lauraeus, M.2    Nurminen, P.3    Kalkkinen, N.4    Apajalahti, J.5
  • 6
    • 0031982859 scopus 로고    scopus 로고
    • Purification and properties of a thermostable phytase from Bacillus sp. DS11
    • Kim YO, Kim HK, Bae KS, Yu JH, Oh TK. Purification and properties of a thermostable phytase from Bacillus sp. DS11. Enzyme Microb Technol. 1998;22:2-7.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 2-7
    • Kim, Y.O.1    Kim, H.K.2    Bae, K.S.3    Yu, J.H.4    Oh, T.K.5
  • 7
    • 0033950597 scopus 로고    scopus 로고
    • Crystal structures of a novel thermostable phytase in partially and fully calcium-loaded states
    • Ha NC, Oh BC, Shin S, Kim HJ, Oh TK, Kim YO, Choi KY, Oh BH. Crystal structures of a novel thermostable phytase in partially and fully calcium-loaded states, Nat Struct Biol. 2000;7:147-153.
    • (2000) Nat Struct Biol. , vol.7 , pp. 147-153
    • Ha, N.C.1    Oh, B.C.2    Shin, S.3    Kim, H.J.4    Oh, T.K.5    Kim, Y.O.6    Choi, K.Y.7    Oh, B.H.8
  • 8
    • 0034802540 scopus 로고    scopus 로고
    • Enzyme mechanism and catalytic property of beta propeller phytase
    • Shin S, Ha NC, Oh BC, Oh TK, Oh BH. Enzyme mechanism and catalytic property of beta propeller phytase, Structure. 2001;9:851-858.
    • (2001) Structure. , vol.9 , pp. 851-858
    • Shin, S.1    Ha, N.C.2    Oh, B.C.3    Oh, T.K.4    Oh, B.H.5
  • 9
    • 34547768136 scopus 로고    scopus 로고
    • Distribution and diversity of phytate-mineralizing bacteria
    • Lim BL, Yeung P, Cheng C, Hill JE. Distribution and diversity of phytate-mineralizing bacteria, ISME J. 2007;1:321-330.
    • (2007) ISME J. , vol.1 , pp. 321-330
    • Lim, B.L.1    Yeung, P.2    Cheng, C.3    Hill, J.E.4
  • 13
    • 0031608474 scopus 로고    scopus 로고
    • High cell-density fermentation
    • Higgins DR, Cregg JM, editors, Totowa: Humana Press Inc
    • Stratton J, Chiruvolu V, Meagher M. High cell-density fermentation. In: Higgins DR, Cregg JM, editors. Pichia Protocols. Methods in Molecular Biology. Totowa: Humana Press Inc.; 1998, Vol. 103:107-120.
    • (1998) Pichia Protocols. Methods in Molecular Biology , vol.103 , pp. 107-120
    • Stratton, J.1    Chiruvolu, V.2    Meagher, M.3
  • 14
    • 33748915125 scopus 로고    scopus 로고
    • Operational strategies, monitoring and control of heterologous protein production in the methylotrophic yeast Pichia pastoris under different promoters: A review
    • Cos O, Ramón R, Montesinos JL, Valero F. Operational strategies, monitoring and control of heterologous protein production in the methylotrophic yeast Pichia pastoris under different promoters: A review, Microb Cell Fact. 2006;5:17.
    • (2006) Microb Cell Fact. , vol.5 , pp. 17
    • Cos, O.1    Ramón, R.2    Montesinos, J.L.3    Valero, F.4
  • 15
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li Z, Xiong F, Lin Q, d'Anjou M, Daugulis AJ, Yang DS, Hew CL. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris, Protein Expr Purif. 2001;21:438-445.
    • (2001) Protein Expr Purif. , vol.21 , pp. 438-445
    • Li, Z.1    Xiong, F.2    Lin, Q.3    d'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.6    Hew, C.L.7
  • 16
    • 0037143788 scopus 로고    scopus 로고
    • Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
    • Hong F, Meinander NQ, Jönsson LJ. Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris, Biotechnol Bioeng. 2002;79:438-449.
    • (2002) Biotechnol Bioeng. , vol.79 , pp. 438-449
    • Hong, F.1    Meinander, N.Q.2    Jönsson, L.J.3
  • 17
    • 2942627936 scopus 로고    scopus 로고
    • Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
    • Jahic M, Wallberg F, Bollok M, Garcia P, Enfors SO. Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures, Microb Cell Fact. 2003;2:6.
    • (2003) Microb Cell Fact. , vol.2 , pp. 6
    • Jahic, M.1    Wallberg, F.2    Bollok, M.3    Garcia, P.4    Enfors, S.O.5
  • 18
    • 67650232980 scopus 로고    scopus 로고
    • Lowering induction temperature for enhanced production of polygalacturonate lyase in recombinant Pichia pastoris
    • Wang Y, Wang Z, Xu Q, Du G, Hua Z, Liu L, Li J, Chen J. Lowering induction temperature for enhanced production of polygalacturonate lyase in recombinant Pichia pastoris, Process Biochem. 2009;44:949-954.
    • (2009) Process Biochem. , vol.44 , pp. 949-954
    • Wang, Y.1    Wang, Z.2    Xu, Q.3    Du, G.4    Hua, Z.5    Liu, L.6    Li, J.7    Chen, J.8
  • 20
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • Jahic M, Gustavsson M, Jansen AK, Martinelle M, Enfors SO. Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes, J Biotechnol. 2003;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
  • 21
    • 0033975293 scopus 로고    scopus 로고
    • High-level expression of recombinant human serum albumin from the methylotrophic yeast Pichia pastoris with minimal protease production and activation
    • Kobayashi K, Kuwae S, Ohya T, Ohda T, Ohyama M, Ohi H, Tomomitsu K, Ohmura T. High-level expression of recombinant human serum albumin from the methylotrophic yeast Pichia pastoris with minimal protease production and activation, J Biosci Bioeng. 2000;89:55-61.
    • (2000) J Biosci Bioeng. , vol.89 , pp. 55-61
    • Kobayashi, K.1    Kuwae, S.2    Ohya, T.3    Ohda, T.4    Ohyama, M.5    Ohi, H.6    Tomomitsu, K.7    Ohmura, T.8
  • 22
    • 34247347868 scopus 로고    scopus 로고
    • Sorbitol co-feeding reduces metabolic burden caused by the overexpression of a Rhizopus oryzae lipase in Pichia pastoris
    • Ramón R, Ferrer P, Valero F. Sorbitol co-feeding reduces metabolic burden caused by the overexpression of a Rhizopus oryzae lipase in Pichia pastoris, J Biotechnol. 2007;130:39-46.
    • (2007) J Biotechnol. , vol.130 , pp. 39-46
    • Ramón, R.1    Ferrer, P.2    Valero, F.3
  • 24
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino JL, Cregg JM. Heterologous protein expression in the methylotrophic yeast Pichia pastoris, FEMS Microbiol Rev. 2000;24:45-66.
    • (2000) FEMS Microbiol Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 26
    • 84890206246 scopus 로고    scopus 로고
    • Anonymous. Pichia fermentation process guidelines. Invitrogen. 2002. Available at: URL: Last accessed date March, 2013.
    • Anonymous. Pichia fermentation process guidelines. Invitrogen. 2002. Available at: URL: http://tools.invitrogen.com/content/sfs/manuals/pichiaferm_prot.pdf. Last accessed date March, 2013.
  • 29
    • 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
    • 2-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. 1998;86:482-487.
    • (1998) J Ferment Bioeng. , vol.86 , 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
  • 30
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzene sulfonic acid
    • Habeeb AF. Determination of free amino groups in proteins by trinitrobenzene sulfonic acid, Anal Biochem. 1966;14:328-336.
    • (1966) Anal Biochem. , vol.14 , pp. 328-336
    • Habeeb, A.F.1
  • 31
    • 84890194193 scopus 로고    scopus 로고
    • Modified methylotrophic Pichia pastoris yeast which secretes human growth hormone. U.S. Patent 6,342,375 B1
    • Guerrero-Olazarán M, Barrera-Saldaña HA, Viader-Salvadó JM. Modified methylotrophic Pichia pastoris yeast which secretes human growth hormone. U.S. Patent 6, 342, 375 B1, 2002.
    • (2002)
    • Guerrero-Olazarán, M.1    Barrera-Saldaña, H.A.2    Viader-Salvadó, J.M.3
  • 32
    • 84890221209 scopus 로고    scopus 로고
    • Levaduras metilotróficas modificadas genéticamente para la producción y secreción de hormona del crecimiento humano. MX Patent 203,194
    • Guerrero-Olazarán M, Barrera-Saldaña HA, Viader-Salvadó JM. Levaduras metilotróficas modificadas genéticamente para la producción y secreción de hormona del crecimiento humano. MX Patent 203, 194, 2001.
    • (2001)
    • Guerrero-Olazarán, M.1    Barrera-Saldaña, H.A.2    Viader-Salvadó, J.M.3
  • 36
    • 54249109629 scopus 로고    scopus 로고
    • Bioprocess optimization using design of experiments methodology
    • Mandenius CF, Brundin A. Bioprocess optimization using design of experiments methodology, Biotechnol Prog. 2008;24:1191-1203.
    • (2008) Biotechnol Prog. , vol.24 , pp. 1191-1203
    • Mandenius, C.F.1    Brundin, A.2
  • 38
    • 68449104172 scopus 로고    scopus 로고
    • Developing a scalable model of recombinant protein yield from Pichia pastoris: The influence of culture conditions, biomass and induction regime
    • Holmes WJ, Darby RA, Wilks MD, Smith R, Bill RM. Developing a scalable model of recombinant protein yield from Pichia pastoris: The influence of culture conditions, biomass and induction regime, Microb Cell Fact. 2009;8:35.
    • (2009) Microb Cell Fact. , vol.8 , pp. 35
    • Holmes, W.J.1    Darby, R.A.2    Wilks, M.D.3    Smith, R.4    Bill, R.M.5
  • 39
    • 84859853677 scopus 로고    scopus 로고
    • The implementation of a design of experiments strategy to increase recombinant protein yields in yeast (Review)
    • Bill RM, editor, Totowa: Humana Press Inc
    • Bora N, Bawa Z, Bill RM, Wilks MDB. The implementation of a design of experiments strategy to increase recombinant protein yields in yeast (Review). In: Bill RM, editor. Recombinant Protein Production in Yeast, Methods in Molecular Biology. Totowa: Humana Press Inc.;2012, Vol.866:115-127.
    • (2012) Recombinant Protein Production in Yeast, Methods in Molecular Biology , vol.866 , pp. 115-127
    • Bora, N.1    Bawa, Z.2    Bill, R.M.3    Wilks, M.D.B.4
  • 40
    • 12944323169 scopus 로고    scopus 로고
    • The effect of nitrogen source on yield and glycosylation of a human cystatin C mutant expressed in Pichia pastoris
    • Pritchett J, Baldwin SA. The effect of nitrogen source on yield and glycosylation of a human cystatin C mutant expressed in Pichia pastoris, J Ind Microbiol Biotechnol. 2004;31:553-558.
    • (2004) J Ind Microbiol Biotechnol. , vol.31 , pp. 553-558
    • Pritchett, J.1    Baldwin, S.A.2
  • 41
    • 3543069439 scopus 로고    scopus 로고
    • An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris
    • Damasceno LM, Pla I, Chang HJ, Cohen L, Ritter G, Old LJ, Batt CA. An optimized fermentation process for high-level production of a single-chain Fv antibody fragment in Pichia pastoris, Protein Expr Purif. 2004;37:18-26.
    • (2004) Protein Expr Purif. , vol.37 , pp. 18-26
    • Damasceno, L.M.1    Pla, I.2    Chang, H.J.3    Cohen, L.4    Ritter, G.5    Old, L.J.6    Batt, C.A.7
  • 42
    • 84876461126 scopus 로고    scopus 로고
    • + phenotype: Methanol limited or methanol non-limited fed-batch cultures?
    • + phenotype: Methanol limited or methanol non-limited fed-batch cultures? Biochem Eng J. 2013;75:47-54.
    • (2013) Biochem Eng J , vol.75 , pp. 47-54
    • Barrigón, J.M.1    Montesinos, J.L.2    Valero, F.3
  • 43
    • 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, Bevins MA, Plantz BA, Smith LA, Meagher MM. 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. 2000;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
  • 44
    • 0037457707 scopus 로고    scopus 로고
    • Effect of methanol feeding strategies on production and yield of recombinant mouse endostatin from Pichia pastoris
    • Trinh LB, Phue JN, Shiloach J. Effect of methanol feeding strategies on production and yield of recombinant mouse endostatin from Pichia pastoris, Biotechnol Bioeng. 2003;82:438-444.
    • (2003) Biotechnol Bioeng. , vol.82 , pp. 438-444
    • Trinh, L.B.1    Phue, J.N.2    Shiloach, J.3
  • 46
    • 0031472701 scopus 로고    scopus 로고
    • A model-based feeding strategy for fed-batch fermentation of recombinant Pichia pastoris
    • d'Anjou MC, Daugulis AJ. A model-based feeding strategy for fed-batch fermentation of recombinant Pichia pastoris, Biotechnol Tech. 1997;11:865-868.
    • (1997) Biotechnol Tech. , vol.11 , pp. 865-868
    • d'Anjou, M.C.1    Daugulis, A.J.2
  • 47
    • 0035808160 scopus 로고    scopus 로고
    • A rational approach to improving productivity in recombinant Pichia pastoris fermentation
    • d'Anjou MC, Daugulis AJ. A rational approach to improving productivity in recombinant Pichia pastoris fermentation, Biotechnol Bioeng. 2001;72:1-11.
    • (2001) Biotechnol Bioeng. , vol.72 , pp. 1-11
    • d'Anjou, M.C.1    Daugulis, A.J.2
  • 49
    • 79952100002 scopus 로고    scopus 로고
    • A dynamic method based on the specific substrate uptake rate to set up a feeding strategy for Pichia pastoris
    • Dietzsch C, Spadiut O, Herwig C. A dynamic method based on the specific substrate uptake rate to set up a feeding strategy for Pichia pastoris, Microb Cell Fact. 2011;10:14.
    • (2011) Microb Cell Fact. , vol.10 , pp. 14
    • Dietzsch, C.1    Spadiut, O.2    Herwig, C.3
  • 50
    • 3242882045 scopus 로고    scopus 로고
    • A Pichia pastoris fermentation strategy for enhancing the heterologous expression of an Escherichia coli phytase
    • Chen CC, Wu PH, Huang CT, Cheng KJ. A Pichia pastoris fermentation strategy for enhancing the heterologous expression of an Escherichia coli phytase, Enzyme Microb Technol. 2004;35:315-320.
    • (2004) Enzyme Microb Technol. , vol.35 , pp. 315-320
    • Chen, C.C.1    Wu, P.H.2    Huang, C.T.3    Cheng, K.J.4
  • 51
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • Cereghino GPL, Cereghino JL, Ilgen C, Cregg JM. Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris, Curr Opin Biotechnol. 2002;13;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
  • 52
    • 33748425718 scopus 로고    scopus 로고
    • A simple model-based control for Pichia pastoris allows a more efficient heterologous protein production bioprocess
    • Cos O, Ramon R, Montesinos JL, Valero F. A simple model-based control for Pichia pastoris allows a more efficient heterologous protein production bioprocess, Biotechnol Bioeng. 2006;95:145-154.
    • (2006) Biotechnol Bioeng. , vol.95 , pp. 145-154
    • Cos, O.1    Ramon, R.2    Montesinos, J.L.3    Valero, F.4
  • 53
    • 0025168284 scopus 로고
    • Fermentation development of recombinant Pichia pastoris expressing the heterologous gene: Bovine lysozyme
    • Brierley RA, Bussineau C, Kosson R, Melton A, Siegel RS. Fermentation development of recombinant Pichia pastoris expressing the heterologous gene: Bovine lysozyme, Ann NY Acad Sci. 1990;589:350-362.
    • (1990) Ann NY Acad Sci. , vol.589 , pp. 350-362
    • Brierley, R.A.1    Bussineau, C.2    Kosson, R.3    Melton, A.4    Siegel, R.S.5


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