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Volumn 44, Issue 9, 2009, Pages 949-954

Lowering induction temperature for enhanced production of polygalacturonate lyase in recombinant Pichia pastoris

Author keywords

Adenosine phosphate levels; Cell viability; Pichia pastoris; Polygalacturonate lyase; Proteolytic degradation

Indexed keywords

ADENOSINE PHOSPHATE LEVELS; CELL VIABILITY; PICHIA PASTORIS; POLYGALACTURONATE LYASE; PROTEOLYTIC DEGRADATION;

EID: 67650232980     PISSN: 13595113     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.procbio.2009.04.019     Document Type: Article
Times cited : (49)

References (34)
  • 1
    • 0035069389 scopus 로고    scopus 로고
    • Application of alkaline and thermostable polygalacturonase from Bacillus sp. MG-cp-2 in degumming of ramie (Boehmeria nivea) and sunn hemp (Crotolaria juncia) bast fibers
    • Kapoor M., Beg Q.K., Bhushan B., Singh K., Dadich K.S., and Hoondal G.S. Application of alkaline and thermostable polygalacturonase from Bacillus sp. MG-cp-2 in degumming of ramie (Boehmeria nivea) and sunn hemp (Crotolaria juncia) bast fibers. Process Biochem. 36 (2001) 803-807
    • (2001) Process Biochem. , vol.36 , pp. 803-807
    • Kapoor, M.1    Beg, Q.K.2    Bhushan, B.3    Singh, K.4    Dadich, K.S.5    Hoondal, G.S.6
  • 2
    • 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
  • 3
    • 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
  • 4
    • 0027360579 scopus 로고
    • Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme
    • Nasser W., Awade A.C., Reverchon S., and Robert-Baudouy J. Pectate lyase from Bacillus subtilis: molecular characterization of the gene, and properties of the cloned enzyme. FEBS Lett. 335 (1994) 319-326
    • (1994) FEBS Lett. , vol.335 , pp. 319-326
    • Nasser, W.1    Awade, A.C.2    Reverchon, S.3    Robert-Baudouy, J.4
  • 5
    • 0037047795 scopus 로고    scopus 로고
    • Exopolygalacturonate lyase from Thermotoga maritima: cloning, characterization and organic synthesis application
    • Parisot J., Ghochikyan A., Langlois V., Sakanyan V., and Rabiller C. Exopolygalacturonate lyase from Thermotoga maritima: cloning, characterization and organic synthesis application. Carbohydr. Res. 337 (2002) 1427-1433
    • (2002) Carbohydr. Res. , vol.337 , pp. 1427-1433
    • Parisot, J.1    Ghochikyan, A.2    Langlois, V.3    Sakanyan, V.4    Rabiller, C.5
  • 7
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • Cereghino J.L., and Cregg J.M. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol. Rev. 24 (2000) 45-66
    • (2000) FEMS Microbiol. Rev. , vol.24 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 10
    • 0038355354 scopus 로고    scopus 로고
    • High dissolved oxygen tension enhances heterologous protein expression by recombinant Pichia pastoris
    • Lee C.Y., Lee S.J., Jung K.H., Katoh S., and Lee E.K. High dissolved oxygen tension enhances heterologous protein expression by recombinant Pichia pastoris. Process Biochem. 38 (2003) 1147-1154
    • (2003) Process Biochem. , vol.38 , pp. 1147-1154
    • Lee, C.Y.1    Lee, S.J.2    Jung, K.H.3    Katoh, S.4    Lee, E.K.5
  • 12
    • 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
  • 14
    • 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
  • 15
    • 0037143788 scopus 로고    scopus 로고
    • Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
    • Hong F., Meinander N.Q., and Jönsson L.J. Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris. Biotechnol. Bioeng. 79 (2002) 438-449
    • (2002) Biotechnol. Bioeng. , vol.79 , pp. 438-449
    • Hong, F.1    Meinander, N.Q.2    Jönsson, L.J.3
  • 16
    • 2942584928 scopus 로고    scopus 로고
    • Increasing secretion of a bivalent anti-T-cell immunotoxin by Pichia pastoris
    • Woo J.H., Liu Y.Y., Stavrou S., and Neville Jr. D.M. Increasing secretion of a bivalent anti-T-cell immunotoxin by Pichia pastoris. Appl. Environ. Microbiol. 70 (2004) 3370-3376
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 3370-3376
    • Woo, J.H.1    Liu, Y.Y.2    Stavrou, S.3    Neville Jr., D.M.4
  • 17
    • 0035715001 scopus 로고    scopus 로고
    • Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris
    • Li Z.J., Xiong F., Lin Q.S., d'Anjou M., Daugulis A.J., Yang D.S.C., and Hew C.L. Low-temperature increases the yield of biologically active herring antifreeze protein in Pichia pastoris. Protein Expres. Purif. 21 (2001) 438-445
    • (2001) Protein Expres. Purif. , vol.21 , pp. 438-445
    • Li, Z.J.1    Xiong, F.2    Lin, Q.S.3    d'Anjou, M.4    Daugulis, A.J.5    Yang, D.S.C.6    Hew, C.L.7
  • 18
    • 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
  • 19
    • 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., and Enfors S.O. Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures. Microb. Cell Fact. 2 (2003) 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
  • 20
    • 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
  • 21
    • 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
  • 22
    • 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 (2007) 92-98
    • (2007) Biochem. Eng. J. , vol.40 , pp. 92-98
    • Zhuge, B.1    Du, G.C.2    Shen, W.3    Zhuge, J.4    Chen, J.5
  • 23
    • 55549131481 scopus 로고    scopus 로고
    • Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris
    • Wang Y., Wang Z.H., Du G.C., Hua Z.Z., Liu L.M., Li J., and Chen J. Enhancement of alkaline polygalacturonate lyase production in recombinant Pichia pastoris. Bioresour. Technol. 100 (2009) 1343-1349
    • (2009) Bioresour. Technol. , vol.100 , pp. 1343-1349
    • Wang, Y.1    Wang, Z.H.2    Du, G.C.3    Hua, Z.Z.4    Liu, L.M.5    Li, J.6    Chen, J.7
  • 24
    • 1842400660 scopus 로고
    • Screening and identification of Candida methanosorbosa as alcohol oxidaseproducing methanol using yeast
    • Suye S., Ogawa A., Yokoyama S., and Obayashi A. Screening and identification of Candida methanosorbosa as alcohol oxidaseproducing 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
    • 0023746858 scopus 로고
    • Intracellular accumulation of AMP as a cause for the decline in rate of ethanol production by Saccharomyces cerevisiae during batch fermentation
    • Dombek K.M., and Ingram L.O. Intracellular accumulation of AMP as a cause for the decline in rate of ethanol production by Saccharomyces cerevisiae during batch fermentation. Appl. Environ. Microbiol. 54 (1988) 98-104
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 98-104
    • Dombek, K.M.1    Ingram, L.O.2
  • 26
    • 0030934006 scopus 로고    scopus 로고
    • Determination of ATP related compounds in fresh and canned tuna fish by HPLC
    • Veciana-Nogues M.T., Izquierdo-Pulido M., and Vidal-Carou M.C. Determination of ATP related compounds in fresh and canned tuna fish by HPLC. Food Chem. 59 (1997) 467-472
    • (1997) Food Chem. , vol.59 , pp. 467-472
    • Veciana-Nogues, M.T.1    Izquierdo-Pulido, M.2    Vidal-Carou, M.C.3
  • 27
    • 0038364057 scopus 로고    scopus 로고
    • Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry
    • Hohenblum H., Borth N., and Mattanovich D. Assessing viability and cell-associated product of recombinant protein producing Pichia pastoris with flow cytometry. J. Biotechnol. 102 (2003) 281-290
    • (2003) J. Biotechnol. , vol.102 , pp. 281-290
    • Hohenblum, H.1    Borth, N.2    Mattanovich, D.3
  • 28
    • 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 A.K., Martinelle M., and Enfors S.O. Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J. Biochem. 102 (2003) 45-53
    • (2003) J. Biochem. , vol.102 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.K.3    Martinelle, M.4    Enfors, S.O.5
  • 29
    • 3543069439 scopus 로고    scopus 로고
    • Anoptimized fermentation process for high-level production of a singlechain Fv antibody fragment in Pichia pastoris
    • Damasceno L.M., Pla I., Chang H.J., Cohen L., Ritter G., Old L.J., and Batt C.A. Anoptimized fermentation process for high-level production of a singlechain Fv antibody fragment in Pichia pastoris. Protein Expr. Purif. 37 (2004) 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
  • 31
    • 0014383591 scopus 로고
    • Intracellular transport of secretory proteins in the pancreatic exocrine cell IV: metabolic requirements
    • Jamieson J., and Palade G. Intracellular transport of secretory proteins in the pancreatic exocrine cell IV: metabolic requirements. J. Cell Biol. 39 (1968) 589-603
    • (1968) J. Cell Biol. , vol.39 , pp. 589-603
    • Jamieson, J.1    Palade, G.2
  • 32
    • 11144342006 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A
    • Chuang S.M., Chen L., Lambertson D., Anand M., Kinzy T.G., and Madura K. Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A. Mol. Cell Biol. 25 (2005) 403-413
    • (2005) Mol. Cell Biol. , vol.25 , pp. 403-413
    • Chuang, S.M.1    Chen, L.2    Lambertson, D.3    Anand, M.4    Kinzy, T.G.5    Madura, K.6
  • 33
    • 0018476986 scopus 로고
    • Relationship between protein synthesis and secretion in liver cells and the state of the adenine nucleotide system
    • Edwards K., Urban J., and Schreiber G. Relationship between protein synthesis and secretion in liver cells and the state of the adenine nucleotide system. Aust. J. Biol. Sci. 32 (1979) 299-307
    • (1979) Aust. J. Biol. Sci. , vol.32 , pp. 299-307
    • Edwards, K.1    Urban, J.2    Schreiber, G.3


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