메뉴 건너뛰기




Volumn 116, Issue 2, 2013, Pages 193-198

Improvement of recombinant endoglucanase produced in Pichia pastoris KM71 through the use of synthetic medium for inoculum and pH control of proteolysis

Author keywords

Endoglucanase; Inoculum development; Lag time; Pichia pastoris; Proteolysis

Indexed keywords

ECONOMICAL PRODUCTION; ENDOGLUCANASES; FED-BATCH CULTIVATION; INOCULUM DEVELOPMENT; LAG-TIME; OPTIMAL CONDITIONS; PICHIA PASTORIS; RECOMBINANT PROTEIN PRODUCTIONS;

EID: 84879100878     PISSN: 13891723     EISSN: 13474421     Source Type: Journal    
DOI: 10.1016/j.jbiosc.2013.02.020     Document Type: Article
Times cited : (30)

References (30)
  • 2
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • Daly R., Hearn M.T.W. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J.Mol. Recognit. 2005, 18:119-138.
    • (2005) J.Mol. Recognit. , vol.18 , pp. 119-138
    • Daly, R.1    Hearn, M.T.W.2
  • 3
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S., Fazenda M.L., McNeil B., Harvey L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 2005, 22:249-270.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 4
    • 33748915125 scopus 로고    scopus 로고
    • Operational strategies, monitoring and control of heterologous protein production in the methylotrophic yeast Pichia pastoris under different promoter: a review
    • Cos O., Ramón R., Montesinos L.J., Valero F. Operational strategies, monitoring and control of heterologous protein production in the methylotrophic yeast Pichia pastoris under different promoter: a review. Microb. Cell Fact. 2006, 5:17.
    • (2006) Microb. Cell Fact. , vol.5 , pp. 17
    • Cos, O.1    Ramón, R.2    Montesinos, L.J.3    Valero, F.4
  • 5
    • 33845497166 scopus 로고    scopus 로고
    • Process technology for production and recovery of heterologous proteins with Pichia pastoris
    • Jahic M., Veide A., Charoenrat T., Teeri T., Enfors S.-O. Process technology for production and recovery of heterologous proteins with Pichia pastoris. Biotechnol. Prog. 2006, 22:1465-1473.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 1465-1473
    • Jahic, M.1    Veide, A.2    Charoenrat, T.3    Teeri, T.4    Enfors, S.-O.5
  • 6
    • 0002414346 scopus 로고    scopus 로고
    • Fermentation technology, bioprocessing, scale-up and manufacture
    • Harwood Academic Publishers, Amsterdam, D.G. Springham (Ed.)
    • Chisti Y., Moo-Young M. Fermentation technology, bioprocessing, scale-up and manufacture. Biotechnology - The science and the business 1999, 177-222. Harwood Academic Publishers, Amsterdam. 2nd ed. D.G. Springham (Ed.).
    • (1999) Biotechnology - The science and the business , pp. 177-222
    • Chisti, Y.1    Moo-Young, M.2
  • 10
    • 38849181132 scopus 로고    scopus 로고
    • The proteolytic systems and heterologous proteins degradation in the methylotrophic yeast Pichia pastoris
    • Zhang Y., Liu R., Wu X. The proteolytic systems and heterologous proteins degradation in the methylotrophic yeast Pichia pastoris. Ann. Microbiol. 2007, 57:553-560.
    • (2007) Ann. Microbiol. , vol.57 , pp. 553-560
    • Zhang, Y.1    Liu, R.2    Wu, X.3
  • 11
    • 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., Enfors S.-O. 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
  • 12
    • 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 S.-O. 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
  • 13
    • 44649083784 scopus 로고    scopus 로고
    • Comparison of pretreatment strategies of sugarcane bagasse: experimental design for citric acid production
    • Khosravi-Darani K., Zoghi A. Comparison of pretreatment strategies of sugarcane bagasse: experimental design for citric acid production. Bioresour. Technol. 2008, 99:6986-6993.
    • (2008) Bioresour. Technol. , vol.99 , pp. 6986-6993
    • Khosravi-Darani, K.1    Zoghi, A.2
  • 14
    • 80855139035 scopus 로고    scopus 로고
    • Strategies to enhance enzymatic hydrolysis of cellulose in lignocellulosic biomass MMG 445
    • MacLellan J. Strategies to enhance enzymatic hydrolysis of cellulose in lignocellulosic biomass MMG 445. Basic Biotechnol. 2010, 6:31-35.
    • (2010) Basic Biotechnol. , vol.6 , pp. 31-35
    • MacLellan, J.1
  • 15
    • 38549088955 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum BCC18080 in Pichia pastoris
    • Wonganu B., Pootanakit K., Boonyapakron K., Champreda V., Tanapongpipat S., Eurwilaichitr L. Cloning, expression and characterization of a thermotolerant endoglucanase from Syncephalastrum racemosum BCC18080 in Pichia pastoris. Protein Expr. Purif. 2008, 58:78-86.
    • (2008) Protein Expr. Purif. , vol.58 , pp. 78-86
    • Wonganu, B.1    Pootanakit, K.2    Boonyapakron, K.3    Champreda, V.4    Tanapongpipat, S.5    Eurwilaichitr, L.6
  • 17
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller G.L. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem. 1959, 31:426-428.
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 18
    • 0017184389 scopus 로고
    • Arapid and sensitivity method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding
    • Bradford M.M. Arapid and sensitivity method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of head of bacteriophage T4. Nature 1970, 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0035167888 scopus 로고    scopus 로고
    • The effect of ethanol and acetate on protein expression in Pichia pastoris
    • Inan M., Meagher M.M. The effect of ethanol and acetate on protein expression in Pichia pastoris. J.Biosci. Bioeng. 2001, 92:337-341.
    • (2001) J.Biosci. Bioeng. , vol.92 , pp. 337-341
    • Inan, M.1    Meagher, M.M.2
  • 23
    • 84856790732 scopus 로고    scopus 로고
    • Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway
    • Krainer F.W., Dietzsch C., Hajek T., Herwig C., Spadiut O., Glieder A. Recombinant protein expression in Pichia pastoris strains with an engineered methanol utilization pathway. Microb. Cell Fact. 2012, 11:22.
    • (2012) Microb. Cell Fact. , vol.11 , pp. 22
    • Krainer, F.W.1    Dietzsch, C.2    Hajek, T.3    Herwig, C.4    Spadiut, O.5    Glieder, A.6
  • 24
    • 84879071536 scopus 로고
    • Control of stock culture preservation and inoculum build-up in bacterial fermentations
    • Pergamon Press, Oxford
    • Lincoln R.E. Control of stock culture preservation and inoculum build-up in bacterial fermentations. Principle of fermentation technology 1960, 147-166. Pergamon Press, Oxford.
    • (1960) Principle of fermentation technology , pp. 147-166
    • Lincoln, R.E.1
  • 25
    • 23944500291 scopus 로고    scopus 로고
    • Elevated expression temperature in a mesophilic host results in increased secretion of a hyperthermophilic enzyme and decreased cell stress
    • Smith J.D., Richardson N.E., Robinson A.S. Elevated expression temperature in a mesophilic host results in increased secretion of a hyperthermophilic enzyme and decreased cell stress. Biochim. Biophys. Acta 2005, 1752:18-25.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 18-25
    • Smith, J.D.1    Richardson, N.E.2    Robinson, A.S.3
  • 26
    • 0037143788 scopus 로고    scopus 로고
    • Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
    • Hong F., Meinander N.Q., Jonaaon L.J. 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    Jonaaon, L.J.3
  • 27
    • 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 A.J., Yang D.S., Hew C.L. 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
  • 28
    • 0031604266 scopus 로고    scopus 로고
    • Secretion of recombinant human insulin-like growth factor I (IGF-I)
    • Brierley R.A. Secretion of recombinant human insulin-like growth factor I (IGF-I). Methods Mol. Biol. 1998, 103:149-177.
    • (1998) Methods Mol. Biol. , vol.103 , pp. 149-177
    • Brierley, R.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.