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Volumn 100, Issue 3, 2009, Pages 1343-1349

Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris according to the ratio of methanol to cell concentration

Author keywords

Alkaline polygalacturonate lyase (PGL); Feeding strategy; Pichia pastoris; Ratio of methanol to cell concentration

Indexed keywords

BIOMASS; CELLS; CONCENTRATION (PROCESS); CYTOLOGY; FEEDING; GLYCEROL; GROWTH KINETICS; METHANOL; RENEWABLE ENERGY RESOURCES;

EID: 55549131481     PISSN: 09608524     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biortech.2008.07.049     Document Type: Article
Times cited : (46)

References (37)
  • 1
    • 0005338574 scopus 로고    scopus 로고
    • Bleach-boosting of eucalyptus kraft pulp using combination of xylanase and pectinase from Streptomyces sp. QG-11-3
    • Beg Q.K., Kapoor M., Tiwari R.P., and Hoondal G.S. Bleach-boosting of eucalyptus kraft pulp using combination of xylanase and pectinase from Streptomyces sp. QG-11-3. Res. Bull. Panjab. Univ. Sci. 51 (2001) 71-78
    • (2001) Res. Bull. Panjab. Univ. Sci. , vol.51 , pp. 71-78
    • Beg, Q.K.1    Kapoor, M.2    Tiwari, R.P.3    Hoondal, G.S.4
  • 3
    • 0028319223 scopus 로고
    • Pectinolytic enzymes from actinomycetes for the degumming of ramie bast fibers
    • Bruhlmann F., Kim K.S., Zimmerman W., and Fiechter A. Pectinolytic enzymes from actinomycetes for the degumming of ramie bast fibers. Appl. Environ. Microbiol. 60 (1994) 2107-2112
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 2107-2112
    • Bruhlmann, F.1    Kim, K.S.2    Zimmerman, W.3    Fiechter, A.4
  • 4
    • 0034056247 scopus 로고    scopus 로고
    • Fermentation, purification, and efficacy of a recombinant vaccine candidate against botulinum neurotoxin type F from Pichia pastoris
    • Byrne M.P., Titball R.W., Holley J., and Smith L.A. Fermentation, purification, and efficacy of a recombinant vaccine candidate against botulinum neurotoxin type F from Pichia pastoris. Prot. Expr. Puri. 18 (2000) 327-337
    • (2000) Prot. Expr. Puri. , vol.18 , pp. 327-337
    • Byrne, M.P.1    Titball, R.W.2    Holley, J.3    Smith, L.A.4
  • 5
    • 38649128790 scopus 로고    scopus 로고
    • Improving intracellular production of recombinant protein in Pichia pastoris using an optimized preinduction glycerol-feeding scheme
    • Chu W., Zhou X.S., and Zhang Y.X. Improving intracellular production of recombinant protein in Pichia pastoris using an optimized preinduction glycerol-feeding scheme. Appl. Microbiol. Biotechnol. 78 (2007) 257-264
    • (2007) Appl. Microbiol. Biotechnol. , vol.78 , pp. 257-264
    • Chu, W.1    Zhou, X.S.2    Zhang, Y.X.3
  • 6
    • 0034607792 scopus 로고    scopus 로고
    • Design of metabolic feed controllers: Application to high density fermentation of Pichia pastoris: Mathematical model for fedbatch high cell density culture
    • Chung J.D. Design of metabolic feed controllers: Application to high density fermentation of Pichia pastoris: Mathematical model for fedbatch high cell density culture. Biotechnol. Bioeng. 68 (2000) 298-307
    • (2000) Biotechnol. Bioeng. , vol.68 , pp. 298-307
    • Chung, J.D.1
  • 8
    • 0034537455 scopus 로고    scopus 로고
    • Heterologous protein production in methylotrophic yeasts
    • Gellissen G. Heterologous protein production in methylotrophic yeasts. Appl. Microbiol. Biotechnol. 54 (2000) 741-750
    • (2000) Appl. Microbiol. Biotechnol. , vol.54 , pp. 741-750
    • Gellissen, G.1
  • 9
    • 45449089448 scopus 로고    scopus 로고
    • Optimization of chemically defined medium for recombinant Pichia pastoris for biomass production
    • Ghosalkar A., Sahai V., and Srivastava A. Optimization of chemically defined medium for recombinant Pichia pastoris for biomass production. Bioresour. Technol. 99 (2008) 7906-7910
    • (2008) Bioresour. Technol. , vol.99 , pp. 7906-7910
    • Ghosalkar, A.1    Sahai, V.2    Srivastava, A.3
  • 10
    • 0035922031 scopus 로고    scopus 로고
    • High-level expression and stabilization of recombinant human chitinase produced in a continuous constitutive Pichia pastoris expression system
    • Goodrick J.C., Xu M., Finnegan R., Schilling B.M., Schiavi S., Hoppe H., and Wan N.C. High-level expression and stabilization of recombinant human chitinase produced in a continuous constitutive Pichia pastoris expression system. Biotechnol. Bioeng. 74 (2001) 492-497
    • (2001) Biotechnol. Bioeng. , vol.74 , pp. 492-497
    • Goodrick, J.C.1    Xu, M.2    Finnegan, R.3    Schilling, B.M.4    Schiavi, S.5    Hoppe, H.6    Wan, N.C.7
  • 11
    • 0028894866 scopus 로고
    • Cloning of a novel constitutively expressed pectate lyase gene pelB from Fusarium solani f. Sp. pisi and characterization of the gene product expressed in Pichia pastoris.
    • Guo W., González-Candelas L., and Kolattukudy P.E. Cloning of a novel constitutively expressed pectate lyase gene pelB from Fusarium solani f. Sp. pisi and characterization of the gene product expressed in Pichia pastoris. J. Bacteriol. 177 (1995) 7070-7077
    • (1995) J. Bacteriol. , vol.177 , pp. 7070-7077
    • Guo, W.1    González-Candelas, L.2    Kolattukudy, P.E.3
  • 12
    • 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 fermentation
    • Hellwig S., Emde F., Raven N.P.G., Henke M., Van der Logt P., and Fischer R. Analysis of single chain antibody production in Pichia pastoris using on-line methanol control in fed-batch and mixed-feed fermentation. Biotechnol. Bioeng. 74 (2000) 344-352
    • (2000) 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
  • 15
    • 0035167888 scopus 로고    scopus 로고
    • The effect of ethanol and acetate on protein expression
    • Inan M., and Meagher M.M. The effect of ethanol and acetate on protein expression. J. Biosci. Bioeng. 92 (2001) 337-341
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 337-341
    • Inan, M.1    Meagher, M.M.2
  • 16
    • 22544467018 scopus 로고    scopus 로고
    • Microbial pectinolytic enzymes: A review
    • Jayani R.S., Saxena S., and Gupta R. Microbial pectinolytic enzymes: A review. Process Biochem. 40 (2005) 2931-2944
    • (2005) Process Biochem. , vol.40 , pp. 2931-2944
    • Jayani, R.S.1    Saxena, S.2    Gupta, R.3
  • 18
    • 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 Hoffmann F. Impact of methanol concentration on secreted protein production in oxygen-limited cultures of recombinant Pichia pastoris. Biotechnol. Bioeng. 93 (2006) 871-879
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 871-879
    • Khatri, N.K.1    Hoffmann, F.2
  • 19
    • 0034281883 scopus 로고    scopus 로고
    • High level secretion of recombinant human serum albumin by fed-batch fermentation of the methylotrophic yeast, Pichia pastoris, based on optimal methanol feeding strategy
    • Kobayashi K., Kuwae S., Ohya T., Ohda T., Ohyama M., and Tomomitsu K. High level secretion of recombinant human serum albumin by fed-batch fermentation of the methylotrophic yeast, Pichia pastoris, based on optimal methanol feeding strategy. J. Biosci. Bioeng. 90 (2000) 280-288
    • (2000) J. Biosci. Bioeng. , vol.90 , pp. 280-288
    • Kobayashi, K.1    Kuwae, S.2    Ohya, T.3    Ohda, T.4    Ohyama, M.5    Tomomitsu, K.6
  • 20
    • 0001669429 scopus 로고
    • Molecular genetics of pathogenesis by soft-rot Erwinia
    • Kotoujansky A. Molecular genetics of pathogenesis by soft-rot Erwinia. Annu. Rev. Phytopathol. 25 (1987) 405-430
    • (1987) Annu. Rev. Phytopathol. , vol.25 , pp. 405-430
    • Kotoujansky, A.1
  • 21
    • 0034115482 scopus 로고    scopus 로고
    • Production of pectate lyases and cellulases by Chryseomonas luteola strain MFCL0 depends on the growth temperature and the nature of the culture medium: evidence for two critical temperatures
    • Laurent P., Buchon L., Guespin-Michel J.F., and Orange N. Production of pectate lyases and cellulases by Chryseomonas luteola strain MFCL0 depends on the growth temperature and the nature of the culture medium: evidence for two critical temperatures. Appl. Environ. Microbiol. 66 (2000) 1538-1543
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1538-1543
    • Laurent, P.1    Buchon, L.2    Guespin-Michel, J.F.3    Orange, N.4
  • 22
    • 0042932499 scopus 로고    scopus 로고
    • Effects of substrate feed rates on heterologous protein expression by Pichia pastoris in DO-stat fed-batch fermentation
    • Lee C.Y., Nakana A., Shiomi N., Lee E.K., and Katoh S. Effects of substrate feed rates on heterologous protein expression by Pichia pastoris in DO-stat fed-batch fermentation. Enzyme Microb. Technol. 33 (2003) 358-365
    • (2003) Enzyme Microb. Technol. , vol.33 , pp. 358-365
    • Lee, C.Y.1    Nakana, A.2    Shiomi, N.3    Lee, E.K.4    Katoh, S.5
  • 23
    • 0036883453 scopus 로고    scopus 로고
    • Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification
    • Matsumoto T., Katsura D., Kondo A., and Fukuda H. Efficient secretory overexpression of Bacillus subtilis pectate lyase in Escherichia coli and single-step purification. Biochem. Eng. J. 12 (2002) 175-179
    • (2002) Biochem. Eng. J. , vol.12 , pp. 175-179
    • Matsumoto, T.1    Katsura, D.2    Kondo, A.3    Fukuda, H.4
  • 24
    • 33845569361 scopus 로고    scopus 로고
    • Effects of post-induction feed strategies on secretory production of recombinant streptokinase in Escherichia coli
    • Ramalingam S., Gautam P., Mukherjee K.J., and Jayaraman G. Effects of post-induction feed strategies on secretory production of recombinant streptokinase in Escherichia coli. Biochem. Eng. J. 33 (2007) 34-41
    • (2007) Biochem. Eng. J. , vol.33 , pp. 34-41
    • Ramalingam, S.1    Gautam, P.2    Mukherjee, K.J.3    Jayaraman, G.4
  • 25
    • 33646056991 scopus 로고    scopus 로고
    • High yield production of a mutant Nippostrongylus brasiliensis acetylcholinesterase in Pichia pastoris and its purification
    • Richter S., Nieveler J., Schulze H., Bachmann T.T., and Schmid R.D. High yield production of a mutant Nippostrongylus brasiliensis acetylcholinesterase in Pichia pastoris and its purification. Biotechnol. Bioeng. 93 (2006) 1017-1022
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 1017-1022
    • Richter, S.1    Nieveler, J.2    Schulze, H.3    Bachmann, T.T.4    Schmid, R.D.5
  • 27
    • 12144251696 scopus 로고    scopus 로고
    • Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: case study with recombinant ovine interferon-τ
    • Sinha J., Plantz B.A., Inan M., and Meagher M.M. Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: case study with recombinant ovine interferon-τ. Biotechnol. Bioeng. 89 (2005) 102-112
    • (2005) Biotechnol. Bioeng. , vol.89 , pp. 102-112
    • Sinha, J.1    Plantz, B.A.2    Inan, M.3    Meagher, M.M.4
  • 29
    • 0026702554 scopus 로고
    • Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungus Fusarium solani f. sp. pisi (Nectria haematococca, mating population VI)
    • Suga H., Ikeda S., Taga M., Kageyama K., and Hyakumachi M. Isolation and analysis of a novel inducible pectate lyase gene from the phytopathogenic fungus Fusarium solani f. sp. pisi (Nectria haematococca, mating population VI). J. Bacteriol 174 (1992) 6343-6349
    • (1992) J. Bacteriol , vol.174 , pp. 6343-6349
    • Suga, H.1    Ikeda, S.2    Taga, M.3    Kageyama, K.4    Hyakumachi, M.5
  • 30
    • 34250333764 scopus 로고    scopus 로고
    • Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastoris
    • Surribas A., Stahn R., Montesinos J.L., Enfors S.O., Valero F., and Jahic M. Optimization of the high-level production of Rhizopus oryzae lipase in Pichia pastoris. J. Biotechnol. 130 (2007) 291-299
    • (2007) J. Biotechnol. , vol.130 , pp. 291-299
    • Surribas, A.1    Stahn, R.2    Montesinos, J.L.3    Enfors, S.O.4    Valero, F.5    Jahic, M.6
  • 31
    • 0037457707 scopus 로고    scopus 로고
    • Effect of methanol feeding strategies on production and yield of recombinant mouse endostatin from Pichia pastoris
    • Trinh L.B., Phue J.N., and Shiloach J. Effect of methanol feeding strategies on production and yield of recombinant mouse endostatin from Pichia pastoris. Biotechnol. Bioeng. 82 (2003) 438-844
    • (2003) Biotechnol. Bioeng. , vol.82 , pp. 438-844
    • Trinh, L.B.1    Phue, J.N.2    Shiloach, J.3
  • 32
    • 0026417070 scopus 로고
    • Effect of chemically-induced, cloned-gene expression on protein synthesis in E. Coli
    • Wood T.K., and Peretti S.W. Effect of chemically-induced, cloned-gene expression on protein synthesis in E. Coli. Biotechnol. Bioeng. 38 (1991) 397-412
    • (1991) Biotechnol. Bioeng. , vol.38 , pp. 397-412
    • Wood, T.K.1    Peretti, S.W.2
  • 33
    • 0034725943 scopus 로고    scopus 로고
    • Polygalacturonase is the key component in enzymatic retting of flax
    • Zhang J., Henriksson G., and Johansson G. Polygalacturonase is the key component in enzymatic retting of flax. J. Biotechnol. 81 (2000) 85-89
    • (2000) J. Biotechnol. , vol.81 , pp. 85-89
    • Zhang, J.1    Henriksson, G.2    Johansson, G.3
  • 34
    • 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 M.A., Plantz B.A., Smith L.A., and Meagher M.M. 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.1    Bevins, M.A.2    Plantz, B.A.3    Smith, L.A.4    Meagher, M.M.5
  • 35
    • 22144467705 scopus 로고    scopus 로고
    • Isolation, phylogenetic analysis of a bacterium with high yield of alkaline pectate lyase and optimization of its culture conditions
    • Zhang J.H., Li Y., Liu H., Liu D.R., and Chen J. Isolation, phylogenetic analysis of a bacterium with high yield of alkaline pectate lyase and optimization of its culture conditions. Chin. J. Appl. Environ. Biol. 11 (2005) 354-358
    • (2005) Chin. J. Appl. Environ. Biol. , vol.11 , pp. 354-358
    • Zhang, J.H.1    Li, Y.2    Liu, H.3    Liu, D.R.4    Chen, J.5
  • 36
    • 0035145669 scopus 로고    scopus 로고
    • Degumming of ramie fibers by alkalophilic bacteria and their polysaccharide-degrading enzymes
    • Zheng L.S., Du Y.M., and Zhang J.Y. Degumming of ramie fibers by alkalophilic bacteria and their polysaccharide-degrading enzymes. Bioresour. Technol. 78 (2001) 89-94
    • (2001) Bioresour. Technol. , vol.78 , pp. 89-94
    • Zheng, L.S.1    Du, Y.M.2    Zhang, J.Y.3
  • 37
    • 42949179630 scopus 로고    scopus 로고
    • Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris
    • Zhuge B., Du G.C., Shen W., Zhuge J., and Chen J. Expression of a Bacillus subtilis pectate lyase gene in Pichia pastoris. Biochem. Eng. J. 40 (2008) 92-98
    • (2008) Biochem. Eng. J. , vol.40 , pp. 92-98
    • Zhuge, B.1    Du, G.C.2    Shen, W.3    Zhuge, J.4    Chen, J.5


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