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Volumn 27, Issue 5, 2011, Pages 1257-1263

Effect of codon optimization on the expression of Trichoderma reesei endoglucanase 1 in Pichia pastoris

Author keywords

Cellulose; Codon optimization; Endoglucanase 1; Pichia pastoris; Recombinant expression; Trichoderma reesei

Indexed keywords

CODON OPTIMIZATION; ENDOGLUCANASE 1; PICHIA PASTORIS; RECOMBINANT EXPRESSION; TRICHODERMA REESEI;

EID: 80053897371     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.663     Document Type: Article
Times cited : (39)

References (34)
  • 1
    • 0031295876 scopus 로고    scopus 로고
    • Cellulose degrading enzymes and their potential industrial applications
    • Bhat MK, Bhat S. Cellulose degrading enzymes and their potential industrial applications. Biotechnol Adv 1997; 15: 583-620.
    • (1997) Biotechnol Adv , vol.15 , pp. 583-620
    • Bhat, M.K.1    Bhat, S.2
  • 2
    • 0030669760 scopus 로고    scopus 로고
    • cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast
    • Saloheimo M, Nakari-Setala T, Tenkanen M, Penttila M. cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast. Eur J Biochem. 1997; 249: 584-591.
    • (1997) Eur J Biochem. , vol.249 , pp. 584-591
    • Saloheimo, M.1    Nakari-Setala, T.2    Tenkanen, M.3    Penttila, M.4
  • 3
    • 56749155915 scopus 로고    scopus 로고
    • Gene cloning and heterologous expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38
    • Yao Q, Sun TT, Liu WF, Chen GJ. Gene cloning and heterologous expression of a novel endoglucanase, swollenin, from Trichoderma pseudokoningii S38. Biosci Biotechnol Biochem. 2008; 72: 2799-2805.
    • (2008) Biosci Biotechnol Biochem. , vol.72 , pp. 2799-2805
    • Yao, Q.1    Sun, T.T.2    Liu, W.F.3    Chen, G.J.4
  • 4
    • 38349128431 scopus 로고    scopus 로고
    • Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability
    • Qin Y, Wei X, Liu X, Wang T, Qu Y. Purification and characterization of recombinant endoglucanase of Trichoderma reesei expressed in Saccharomyces cerevisiae with higher glycosylation and stability. Protein Expr Purif. 2008; 58: 162-167.
    • (2008) Protein Expr Purif. , vol.58 , pp. 162-167
    • Qin, Y.1    Wei, X.2    Liu, X.3    Wang, T.4    Qu, Y.5
  • 5
    • 0025815744 scopus 로고
    • Structural and functional analysis of Trichoderma reesei endoglucanase I expressed in yeast Saccharomyces cerevisiae
    • Aho S. Structural and functional analysis of Trichoderma reesei endoglucanase I expressed in yeast Saccharomyces cerevisiae. FEBS Lett. 1991; 291: 45-49.
    • (1991) FEBS Lett. , vol.291 , pp. 45-49
    • Aho, S.1
  • 6
    • 20444378957 scopus 로고    scopus 로고
    • Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes
    • Sandgren M, Stahlberg J, Mitchinson C. Structural and biochemical studies of GH family 12 cellulases: improved thermal stability, and ligand complexes. Prog Biophys Mol Biol. 2005; 89: 246-291.
    • (2005) Prog Biophys Mol Biol. , vol.89 , pp. 246-291
    • Sandgren, M.1    Stahlberg, J.2    Mitchinson, C.3
  • 10
    • 0036122492 scopus 로고    scopus 로고
    • Constitutive expression of the Trichoderma reesei beta-1,4-xylanase gene (xyn2) and the beta-1,4-endoglucanase gene (egl) in Aspergillus niger in molasses and defined glucose media
    • Rose SH, van Zyl WH. Constitutive expression of the Trichoderma reesei beta-1, 4-xylanase gene (xyn2) and the beta-1, 4-endoglucanase gene (egl) in Aspergillus niger in molasses and defined glucose media. Appl Microbiol Biotechnol. 2002; 58: 461-468.
    • (2002) Appl Microbiol Biotechnol. , vol.58 , pp. 461-468
    • Rose, S.H.1    van Zyl, W.H.2
  • 11
    • 0023417565 scopus 로고
    • Expression of two Trichoderma reesei endoglucanases in the yeast Saccharomyces cerevisiae
    • Penttila ME, Andre L, Saloheimo M, Lehtovaara P, Knowles JK. Expression of two Trichoderma reesei endoglucanases in the yeast Saccharomyces cerevisiae. Yeast. 1987; 3: 175-185.
    • (1987) Yeast. , vol.3 , pp. 175-185
    • Penttila, M.E.1    Andre, L.2    Saloheimo, M.3    Lehtovaara, P.4    Knowles, J.K.5
  • 12
    • 0023270359 scopus 로고
    • Cloning, characterization, and expression in Saccharomyces cerevisiae of endoglucanase I from Trichoderma reesei
    • Van Arsdell JN, Kwok S, Schweickart VL, Ladner MB, Gelfand DH, Innis MA. Cloning, characterization, and expression in Saccharomyces cerevisiae of endoglucanase I from Trichoderma reesei. Nat Biotechnol. 1987; 5: 60-64.
    • (1987) Nat Biotechnol. , vol.5 , pp. 60-64
    • Van Arsdell, J.N.1    Kwok, S.2    Schweickart, V.L.3    Ladner, M.B.4    Gelfand, D.H.5    Innis, M.A.6
  • 13
    • 0033203325 scopus 로고    scopus 로고
    • Heterologous expression and characterization of endoglucanase I (EGI) from Trichoderma viride HK-75
    • Kwon I, Ekino K, Goto M, Furukawa K. Heterologous expression and characterization of endoglucanase I (EGI) from Trichoderma viride HK-75. Biosci Biotechnol Biochem. 1999; 63: 1714-1720.
    • (1999) Biosci Biotechnol Biochem. , vol.63 , pp. 1714-1720
    • Kwon, I.1    Ekino, K.2    Goto, M.3    Furukawa, K.4
  • 17
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • Cereghino GP, 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.1    Cereghino, J.L.2    Ilgen, C.3    Cregg, J.M.4
  • 18
    • 33947275929 scopus 로고    scopus 로고
    • Codon optimization of Bacillus licheniformis beta-1,3-1,4-glucanase gene and its expression in Pichia pastoris
    • Teng D, Fan Y, Yang YL, Tian ZG, Luo J, Wang JH. Codon optimization of Bacillus licheniformis beta-1, 3-1, 4-glucanase gene and its expression in Pichia pastoris. Appl Microbiol Biotechnol. 2007; 74: 1074-1083.
    • (2007) Appl Microbiol Biotechnol. , vol.74 , pp. 1074-1083
    • Teng, D.1    Fan, Y.2    Yang, Y.L.3    Tian, Z.G.4    Luo, J.5    Wang, J.H.6
  • 19
    • 77949541645 scopus 로고    scopus 로고
    • Codon optimization through a two-step gene synthesis leads to a high-level expression of Aspergillus niger lip2 gene in Pichia pastoris
    • Yang J, Liu L. Codon optimization through a two-step gene synthesis leads to a high-level expression of Aspergillus niger lip2 gene in Pichia pastoris. J Mol Catal B: Enzym. 2010; 63: 164-169.
    • (2010) J Mol Catal B: Enzym. , vol.63 , pp. 164-169
    • Yang, J.1    Liu, L.2
  • 20
    • 33646089874 scopus 로고    scopus 로고
    • Codon optimization, expression, and characterization of an internalizing anti-ErbB2 single-chain antibody in Pichia pastoris
    • Hu S, Li L, Qiao J, Guo Y, Cheng L, Liu J. Codon optimization, expression, and characterization of an internalizing anti-ErbB2 single-chain antibody in Pichia pastoris. Protein Expr Purif. 2006; 47: 249-257.
    • (2006) Protein Expr Purif. , vol.47 , pp. 249-257
    • Hu, S.1    Li, L.2    Qiao, J.3    Guo, Y.4    Cheng, L.5    Liu, J.6
  • 21
    • 0347915684 scopus 로고    scopus 로고
    • High efficiency transformation by electroporation of P. pastoris pretreated with lithium acetate and dithiothreitol
    • Wu S, Letchworth GJ. High efficiency transformation by electroporation of P. pastoris pretreated with lithium acetate and dithiothreitol. Biotechniques. 2004; 36: 152-154.
    • (2004) Biotechniques. , vol.36 , pp. 152-154
    • Wu, S.1    Letchworth, G.J.2
  • 22
    • 58349096674 scopus 로고    scopus 로고
    • Multiple-layer substrate zymography for detection of several enzymes in a single sodium dodecyl sulfate gel
    • Choi N-S, Kim B-H, Park C-S, Han YJ, Lee HW, Choi JH, Lee S-G, Song JJ. Multiple-layer substrate zymography for detection of several enzymes in a single sodium dodecyl sulfate gel. Anal Biochem. 2009; 386: 121-122.
    • (2009) Anal Biochem. , vol.386 , pp. 121-122
    • Choi, N.-S.1    Kim, B.-H.2    Park, C.-S.3    Han, Y.J.4    Lee, H.W.5    Choi, J.H.6    Lee, S.-G.7    Song, J.J.8
  • 25
    • 80053895608 scopus 로고    scopus 로고
    • Invitrogen Pichia Fermentation Process Guidelines. Available at:
    • Invitrogen Pichia Fermentation Process Guidelines. Available at:
  • 26
    • 45449102836 scopus 로고    scopus 로고
    • Bioseparation of recombinant cellulose-binding module-proteins by affinity adsorption on an ultra-high-capacity cellulosic adsorbent
    • Hong J, Ye X, Wang Y, Zhang YH. Bioseparation of recombinant cellulose-binding module-proteins by affinity adsorption on an ultra-high-capacity cellulosic adsorbent. Anal Chim Acta. 2008; 621: 193-199.
    • (2008) Anal Chim Acta. , vol.621 , pp. 193-199
    • Hong, J.1    Ye, X.2    Wang, Y.3    Zhang, Y.H.4
  • 27
    • 84943470296 scopus 로고
    • Measurement of Cellulase Activities
    • Ghose TK. Measurement of Cellulase Activities. Pure Appl Chem. 1987; 59: 257-268.
    • (1987) Pure Appl Chem. , vol.59 , pp. 257-268
    • Ghose, T.K.1
  • 28
    • 0024970291 scopus 로고
    • Continuous photometric determination of endo-1,4-[beta]-d-glucanase (cellulase) activity using 4-methylumbelliferyl-[beta]-d-cellobioside as a substrate
    • Chernoglazov VM, Jafarova AN, Klyosov AA. Continuous photometric determination of endo-1, 4-[beta]-d-glucanase (cellulase) activity using 4-methylumbelliferyl-[beta]-d-cellobioside as a substrate. Anal Biochem. 1989; 179: 186-189.
    • (1989) Anal Biochem. , vol.179 , pp. 186-189
    • Chernoglazov, V.M.1    Jafarova, A.N.2    Klyosov, A.A.3
  • 29
    • 0023553310 scopus 로고
    • A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei
    • Penttila M, Nevalainen H, Ratto M, Salminen E, Knowles J. A versatile transformation system for the cellulolytic filamentous fungus Trichoderma reesei. Gene. 1987; 61: 155-164.
    • (1987) Gene. , vol.61 , pp. 155-164
    • Penttila, M.1    Nevalainen, H.2    Ratto, M.3    Salminen, E.4    Knowles, J.5
  • 31
  • 32
    • 0036969195 scopus 로고    scopus 로고
    • Identification of glycan structures and glycosylation sites in cellobiohydrolase II and endoglucanase I and II from Trichoderma reesei
    • Hui JPM, White TC, Thibault P. Identification of glycan structures and glycosylation sites in cellobiohydrolase II and endoglucanase I and II from Trichoderma reesei. Glycobiology 2002; 12: 837-849.
    • (2002) Glycobiology , vol.12 , pp. 837-849
    • Hui, J.P.M.1    White, T.C.2    Thibault, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.