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Volumn 21, Issue 10, 2011, Pages 1012-1020

Cloning, expression, purification, and properties of an endoglucanase gene (glycosyl hydrolase family 12) from Aspergillus niger VTCC-F021 in Pichia pastoris

Author keywords

Aspergillus niger VTCC F021; Cloning; Endoglucanase gene; Expression; Properties

Indexed keywords

BETA GLUCAN; GLYCOSIDASE; GLYCOSYLHYDROLASE 12; UNCLASSIFIED DRUG;

EID: 80055041446     PISSN: 10177825     EISSN: 17388872     Source Type: Journal    
DOI: 10.4014/jmb.1104.04030     Document Type: Article
Times cited : (23)

References (35)
  • 1
    • 0032590072 scopus 로고    scopus 로고
    • An endoglucanase, EglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed-linkage (1-3),(1-4)-β-D-glucans and cellulose
    • Bauer, M. W., L. E. Driskill, W. Callen, M. A. Snead, E. J. Mathur, and R. M. Kelly. 1999. An endoglucanase, EglA, from the hyperthermophilic archaeon Pyrococcus furiosus hydrolyzes β-1,4 bonds in mixed-linkage (1-3),(1-4)-β-D-glucans and cellulose. J. Bacteriol. 181: 284-290.
    • (1999) J. Bacteriol , vol.181 , pp. 284-290
    • Bauer, M.W.1    Driskill, L.E.2    Callen, W.3    Snead, M.A.4    Mathur, E.J.5    Kelly, R.M.6
  • 2
    • 0028088841 scopus 로고
    • The biological degradation of cellulose
    • Beguin, P. and J. P. Aubert. 1994. The biological degradation of cellulose. FEMS Microbiol. Rev. 13: 25-58.
    • (1994) FEMS Microbiol. Rev , vol.13 , pp. 25-58
    • Beguin, P.1    Aubert, J.P.2
  • 3
    • 0034253208 scopus 로고    scopus 로고
    • Cellulases and related enzymes in biotechnology
    • Bhat, M. K. 2004. Cellulases and related enzymes in biotechnology. Biotechnol. Adv. 18: 355-383.
    • (2004) Biotechnol. Adv , vol.18 , pp. 355-383
    • Bhat, M.K.1
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0025118121 scopus 로고
    • Studies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I
    • Claeyssens, M., H. V. Tilbeurgh, J. P. Kamerling, J. Berg, M. Vrsanska, and P. Biely. 1990. Studies of the cellulolytic system of the filamentous fungus Trichoderma reesei QM 9414. Substrate specificity and transfer activity of endoglucanase I. Biochem. J. 270: 251-256.
    • (1990) Biochem. J , vol.270 , pp. 251-256
    • Claeyssens, M.1    Tilbeurgh, H.V.2    Kamerling, J.P.3    Berg, J.4    Vrsanska, M.5    Biely, P.6
  • 6
    • 3042625351 scopus 로고    scopus 로고
    • Treatment of recycled fiber with Trichoderma cellulases
    • Dienes, D., A. Egyhazi, and K. Reczey. 2004. Treatment of recycled fiber with Trichoderma cellulases. Ind. Crop Prod. 20: 11-21.
    • (2004) Ind. Crop Prod , vol.20 , pp. 11-21
    • Dienes, D.1    Egyhazi, A.2    Reczey, K.3
  • 7
    • 1842506029 scopus 로고    scopus 로고
    • Volumetric productivity improvement for endoglucanase of Trichoderma pseudokoingii S-38
    • Duan, X. Y., S. Y. Liu, W. Zhang, C. Q. X. Zhang, and P. J. Gao. 2004. Volumetric productivity improvement for endoglucanase of Trichoderma pseudokoingii S-38. J. Appl. Microbiol. 96: 772-776.
    • (2004) J. Appl. Microbiol , vol.96 , pp. 772-776
    • Duan, X.Y.1    Liu, S.Y.2    Zhang, W.3    Zhang, C.Q.X.4    Gao, P.J.5
  • 9
    • 34249864393 scopus 로고    scopus 로고
    • Cloning and identification of novel cellulase genes from uncultured microorganisms in rabbit cecum and characterization of the expressed cellulases
    • Feng, Y., C. J. Duan, H. Pang, X. C. Mo, C. F. Wu, and Y. Yu. 2007. Cloning and identification of novel cellulase genes from uncultured microorganisms in rabbit cecum and characterization of the expressed cellulases. Appl. Microbiol. Biotechnol. 75: 319-328.
    • (2007) Appl. Microbiol. Biotechnol , vol.75 , pp. 319-328
    • Feng, Y.1    Duan, C.J.2    Pang, H.3    Mo, X.C.4    Wu, C.F.5    Yu, Y.6
  • 10
    • 0035663545 scopus 로고    scopus 로고
    • Cloning of a gene encoding a highly stable endo-beta-1,4- glucanase from Aspergillus niger and its expression in yeast
    • Hong, J., H. Tamaki, S. Akiba, K. Yamamoto, and H. Kumagai. 2001. Cloning of a gene encoding a highly stable endo-beta-1,4- glucanase from Aspergillus niger and its expression in yeast. J. Biosci. Bioeng. 92: 434-441.
    • (2001) J. Biosci. Bioeng , vol.92 , pp. 434-441
    • Hong, J.1    Tamaki, H.2    Akiba, S.3    Yamamoto, K.4    Kumagai, H.5
  • 11
    • 12944280876 scopus 로고    scopus 로고
    • A highly acid-stable and thermostable endo-β-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus
    • Huang, Y., G. Krauss, S. Cottaz, H. Driguez, and G. Lipps. 2005. A highly acid-stable and thermostable endo-β-glucanase from the thermoacidophilic archaeon Sulfolobus solfataricus. Biochem. J. 385: 581-588.
    • (2005) Biochem. J , vol.385 , pp. 581-588
    • Huang, Y.1    Krauss, G.2    Cottaz, S.3    Driguez, H.4    Lipps, G.5
  • 12
    • 0017397397 scopus 로고
    • Purification and properties of a cellulase from Aspergillus niger
    • Hurst, P. L., J. Nielsen, P. A. Sullivan, and M. G. Shepherd. 1977. Purification and properties of a cellulase from Aspergillus niger. Biochem. J. 165: 33-41.
    • (1977) Biochem. J , vol.165 , pp. 33-41
    • Hurst, P.L.1    Nielsen, J.2    Sullivan, P.A.3    Shepherd, M.G.4
  • 13
    • 43749115333 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of a novel endoglucanase (CMCase) from Gymnoascella citrina produced under solid-state condition
    • Jabbar, A., M. H. Rashid, and M. R. Javed. 2008. Kinetics and thermodynamics of a novel endoglucanase (CMCase) from Gymnoascella citrina produced under solid-state condition. J. Ind. Microbiol. Biotechnol. 35: 515-524.
    • (2008) J. Ind. Microbiol. Biotechnol , vol.35 , pp. 515-524
    • Jabbar, A.1    Rashid, M.H.2    Javed, M.R.3
  • 14
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius, K., A. Mølgaard, R. Gupta, and S. Brunak. 2005. Prediction, conservation analysis and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 15: 153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Mølgaard, A.2    Gupta, R.3    Brunak, S.4
  • 16
    • 0030462509 scopus 로고    scopus 로고
    • Molecular cloning, purification and characterization of two endo-1,4-beta-glucanases from Aspergillus oryzae KBN616
    • Kitamoto, N., M. Go, T. Shibayama, T. Kimura, Y. Kito, K. Ohmiya, and N. Tsukagoshi. 1996. Molecular cloning, purification and characterization of two endo-1,4-beta-glucanases from Aspergillus oryzae KBN616. Appl. Microbiol. Biotechnol. 46: 538-544.
    • (1996) Appl. Microbiol. Biotechnol , vol.46 , pp. 538-544
    • Kitamoto, N.1    Go, M.2    Shibayama, T.3    Kimura, T.4    Kito, Y.5    Ohmiya, K.6    Tsukagoshi, N.7
  • 17
    • 0027414938 scopus 로고
    • Role of sugar chains in the in vitro activity of recombinant human interleukin 5
    • Kodama, S., M. Tsujimoto, N. Tsuruoka, T. Sugo, T. Endo, and A. Kobata. 1993. Role of sugar chains in the in vitro activity of recombinant human interleukin 5. Eur. J. Biochem. 211: 903-908.
    • (1993) Eur. J. Biochem , vol.211 , pp. 903-908
    • Kodama, S.1    Tsujimoto, M.2    Tsuruoka, N.3    Sugo, T.4    Endo, T.5    Kobata, A.6
  • 18
    • 0014949207 scopus 로고
    • Clevage of structure proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Clevage of structure proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick, S., M. L. Fazenda, B. McNeil, and L. M. Harvey. 2005. Heterologous protein production using the Pichia pastoris expression system. Yeast 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
  • 21
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • Miller, G. L. 1959. Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Biochem. 31: 426-428.
    • (1959) Anal. Biochem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 22
    • 67649231785 scopus 로고    scopus 로고
    • Purification and characterization of an endoglucanase from Aspergillus terreus highly active against barley b-glucan and xyloglucan
    • Nazir, A., R. Soni, H. S. Saini, R. K. Manhas, and B. S. Chadha. 2009. Purification and characterization of an endoglucanase from Aspergillus terreus highly active against barley b-glucan and xyloglucan. World J. Microbiol. Biotechnol. 25: 1189-1197.
    • (2009) World J. Microbiol. Biotechnol , vol.25 , pp. 1189-1197
    • Nazir, A.1    Soni, R.2    Saini, H.S.3    Manhas, R.K.4    Chadha, B.S.5
  • 23
    • 0031890507 scopus 로고    scopus 로고
    • Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414
    • Okada, H., K. Tada, T. Sekiya, K. Yokoyama, A. Takahashi, A. Tohda, H. Kumagai, and Y. Morikawa. 1998. Molecular characterization and heterologous expression of the gene encoding a low-molecular-mass endoglucanase from Trichoderma reesei QM9414. Appl. Environ. Microbiol. 62: 555-563.
    • (1998) Appl. Environ. Microbiol , vol.62 , pp. 555-563
    • Okada, H.1    Tada, K.2    Sekiya, T.3    Yokoyama, K.4    Takahashi, A.5    Tohda, A.6    Kumagai, H.7    Morikawa, Y.8
  • 24
  • 25
    • 0025107894 scopus 로고
    • Complete nucleotide sequence of a gene coding for Aspergillus aculeatus cellulase (F1-CMCase)
    • Ooi, T., A. Shinmyo, H. Okada, S. Murao, T. Kawaguchi, and M. Arai. 1990. Complete nucleotide sequence of a gene coding for Aspergillus aculeatus cellulase (F1-CMCase). Nucleic Acids Res. 18: 5884.
    • (1990) Nucleic Acids Res , vol.18 , pp. 5884
    • Ooi, T.1    Shinmyo, A.2    Okada, H.3    Murao, S.4    Kawaguchi, T.5    Arai, M.6
  • 26
    • 3142724822 scopus 로고    scopus 로고
    • Study of the strawberry Cel1 endo-(1,4)-glucanase protein accumulation and characterization of its in vitro activity by heterologous expression in Pichia pastoris
    • Palomer, X., E. Dominguez-Puigjaner, M. Vendrell, and I. Llop- Tous. 2004. Study of the strawberry Cel1 endo-(1,4)-glucanase protein accumulation and characterization of its in vitro activity by heterologous expression in Pichia pastoris. Plant Sci. 167: 509-518.
    • (2004) Plant Sci , vol.167 , pp. 509-518
    • Palomer, X.1    Dominguez-Puigjaner, E.2    Vendrell, M.3    Llop-Tous, I.4
  • 27
    • 0032942942 scopus 로고    scopus 로고
    • A xyloglucanspecific endo-beta-1,4-glucanase from Aspergillus aculeatus: Expression cloning in yeast, purification and characterization of the recombinant enzyme
    • Pauly, M., L. N. Andersen, S. Kauppinen, L. V. Kofod, W. S. York, P. Albersheim, and A. Darvill. 1999. A xyloglucanspecific endo-beta-1,4-glucanase from Aspergillus aculeatus: Expression cloning in yeast, purification and characterization of the recombinant enzyme. Glycobiology 9: 93-100.
    • (1999) Glycobiology , vol.9 , pp. 93-100
    • Pauly, M.1    Andersen, L.N.2    Kauppinen, S.3    Kofod, L.V.4    York, W.S.5    Albersheim, P.6    Darvill, A.7
  • 28
    • 33751542136 scopus 로고    scopus 로고
    • A novel esterase from Ralstonia sp. M1: Gene cloning, sequencing, high-level expression and characterization
    • Quyen, D. T., S. L. T. Nguyen, and T. T. Dao. 2007. A novel esterase from Ralstonia sp. M1: Gene cloning, sequencing, high-level expression and characterization. Prot. Expr. Purif. 51: 133-140.
    • (2007) Prot. Expr. Purif , vol.51 , pp. 133-140
    • Quyen, D.T.1    Nguyen, S.L.T.2    Dao, T.T.3
  • 29
    • 54849426626 scopus 로고    scopus 로고
    • Improvement of Aspergillus oryzae for hyperproductionof endoglucanase: Expression cloning of cmc-1 gene of Aspergillus aculeatus
    • Rashid, M. H., M. R. Javed, T. Kawaguchi, J. Sumitani, and M. Arai. 2008. Improvement of Aspergillus oryzae for hyperproductionof endoglucanase: Expression cloning of cmc-1 gene of Aspergillus aculeatus. Biotechnol. Lett. 30: 2165-2172.
    • (2008) Biotechnol. Lett , vol.30 , pp. 2165-2172
    • Rashid, M.H.1    Javed, M.R.2    Kawaguchi, T.3    Sumitani, J.4    Arai, M.5
  • 30
    • 0036122492 scopus 로고    scopus 로고
    • Constitutive expression of the Trichoderma reesei β-1,4-xylanase gene (xyn2) and the β-1,4- endoglucanase gene (egI) in Aspergillus niger in molasses and defined glucose media
    • Rose, S. H. and W. H. Zyl. 2002. Constitutive expression of the Trichoderma reesei β-1,4-xylanase gene (xyn2) and the β-1,4- endoglucanase gene (egI) in Aspergillus niger in molasses and defined glucose media. Appl. Microbiol. Biotechnol. 58: 461-468.
    • (2002) Appl. Microbiol. Biotechnol , vol.58 , pp. 461-468
    • Rose, S.H.1    Zyl, W.H.2
  • 31
    • 0028915489 scopus 로고
    • Cloning and sequencing of cellulase cDNA from Aspergillus kawachii and its expression in Saccharomyces cerevisiae
    • Sakamoto, S., G. Tamura, K. Ito, T. Ishikawa, K. Iwano, and N. Nishiya. 1995. Cloning and sequencing of cellulase cDNA from Aspergillus kawachii and its expression in Saccharomyces cerevisiae. Curr. Genet. 27: 435-439.
    • (1995) Curr. Genet , vol.27 , pp. 435-439
    • Sakamoto, S.1    Tamura, G.2    Ito, K.3    Ishikawa, T.4    Iwano, K.5    Nishiya, N.6
  • 32
    • 0028080142 scopus 로고
    • The role of the N-linked carbohydrate chain of rice aamylase in thermostability and enzyme kinetics
    • Terashima, M., A. Kubo, M. Suzawa, Y. Itoh, and S. Katoh. 1994. The role of the N-linked carbohydrate chain of rice aamylase in thermostability and enzyme kinetics. Eur. J. Biochem. 226: 249-254.
    • (1994) Eur. J. Biochem , vol.226 , pp. 249-254
    • Terashima, M.1    Kubo, A.2    Suzawa, M.3    Itoh, Y.4    Katoh, S.5
  • 33
    • 77951228328 scopus 로고    scopus 로고
    • Substrate specificity of family 5, 6, 7, 9, 12, and 45 endoglucanases
    • Vlasenko, E., M. Schülein, J. Cherry, and F. Xu. 2010. Substrate specificity of family 5, 6, 7, 9, 12, and 45 endoglucanases. Bioresour. Technol. 101: 2405-2411.
    • (2010) Bioresour. Technol , vol.101 , pp. 2405-2411
    • Vlasenko, E.1    Schülein, M.2    Cherry, J.3    Xu, F.4
  • 34
    • 0026011237 scopus 로고
    • Purification and characterization of two endo-1-4- beta-D-glucanases from Sclerotinia sclerotium
    • Waksman, G. 1991. Purification and characterization of two endo-1-4- beta-D-glucanases from Sclerotinia sclerotium. Biochem. Biophys. Acta 1073: 49-55.
    • (1991) Biochem. Biophys. Acta , vol.1073 , pp. 49-55
    • Waksman, G.1
  • 35
    • 77954281012 scopus 로고    scopus 로고
    • High-level expression of an Aspergillus niger endo-β-1,4- glucanase in Pichia pastoris through gene codon optimization and synthesis
    • Zhao, S., J. Huang, C. Zhang, L. Deng, N. Hu, and Y. Liang. 2010. High-level expression of an Aspergillus niger endo-β-1,4- glucanase in Pichia pastoris through gene codon optimization and synthesis. J. Microbiol. Biotechnol. 20: 467-473.
    • (2010) J. Microbiol. Biotechnol , vol.20 , pp. 467-473
    • Zhao, S.1    Huang, J.2    Zhang, C.3    Deng, L.4    Hu, N.5    Liang, Y.6


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