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Volumn 98, Issue 5, 2004, Pages 338-343

Acidophilic xylanase from Aureobasidium pullulans: Efficient expression and secretion in Pichia pastoris and mutational analysis

Author keywords

Acidophilic enzyme; Aureobasidium pullulans; Heterologous expression; Pichia pastoris; Protein secretion; Signal sequence; Site directed mutagenesis; Xylanase

Indexed keywords

AMINO ACIDS; DNA; PROTEINS; YEAST;

EID: 10944248996     PISSN: 13891723     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1389-1723(04)00292-0     Document Type: Article
Times cited : (45)

References (23)
  • 1
    • 0003151068 scopus 로고
    • Chemistry of hemicelluloses: Relationship between hemicellulose structure and enzymes required for hydrolysis
    • Coughlan, M. P. and Hazlewood, G. P. (ed.). Portland Press, London
    • Puls, J. and Schuseil, J.: Chemistry of hemicelluloses: relationship between hemicellulose structure and enzymes required for hydrolysis, p. 1-27. In Coughlan, M. P. and Hazlewood, G. P. (ed.), Hemicellulose and hemicellulases. Portland Press, London (1993).
    • (1993) Hemicellulose and Hemicellulases , pp. 1-27
    • Puls, J.1    Schuseil, J.2
  • 2
    • 84981976048 scopus 로고
    • β-1,4-D-xylan-degrading enzyme systems: Biochemistry, molecular biology and applications
    • Coughlan, M. P. and Hazlewood, G. P.: β-1,4-D-Xylan-degrading enzyme systems: biochemistry, molecular biology and applications. Biotechnol. Appl. Biochem., 17, 259-289 (1993).
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 3
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B.: A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 280, 309-316 (1991).
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 4
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A.: New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 5
    • 0034770954 scopus 로고    scopus 로고
    • Purification and characterization of an acidophilic xylanase from Aureobasidium pullulans var. melanigenum and sequence analysis of the encoding gene
    • Ohta, K., Moriyama, S., Tanaka, H., Shige, T., and Akimoto, H.: Purification and characterization of an acidophilic xylanase from Aureobasidium pullulans var. melanigenum and sequence analysis of the encoding gene. J. Biosci. Bioeng., 92, 262-270 (2001).
    • (2001) J. Biosci. Bioeng. , vol.92 , pp. 262-270
    • Ohta, K.1    Moriyama, S.2    Tanaka, H.3    Shige, T.4    Akimoto, H.5
  • 6
    • 0030045212 scopus 로고    scopus 로고
    • Expression of Aureobasidium pullulans xynA in, and secretion of the xylanase from, Saccharomyces cerevisiae
    • Li, X.-L. and Ljungdahl, L. G.: Expression of Aureobasidium pullulans xynA in, and secretion of the xylanase from, Saccharomyces cerevisiae. Appl. Environ. Microbiol., 62, 209-213 (1996).
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 209-213
    • Li, X.-L.1    Ljungdahl, L.G.2
  • 7
    • 0002283070 scopus 로고    scopus 로고
    • Expression in the methylotrophic yeast Pichia pastoris
    • Fernandez, J. M. and Hoeffler, J. P. (ed.). Academic Press, New York
    • Cregg, J. M.: Expression in the methylotrophic yeast Pichia pastoris, p. 157-191. In Fernandez, J. M. and Hoeffler, J. P. (ed.), Gene expression systems. Academic Press, New York (1999).
    • (1999) Gene Expression Systems , pp. 157-191
    • Cregg, J.M.1
  • 8
    • 0034084579 scopus 로고    scopus 로고
    • High-level production of recombinant fungal endo-β-1,4-xylanase in the methylotrophic yeast Pichia pastoris
    • Berrin, J.-G., Williamson, G., Puigserver, A., Chaix, J.-C., McLauchlan, W. R., and Juge, N.: High-level production of recombinant fungal endo-β-1,4-xylanase in the methylotrophic yeast Pichia pastoris. Protein Express. Purif., 19, 179-187 (2000).
    • (2000) Protein Express. Purif. , vol.19 , pp. 179-187
    • Berrin, J.-G.1    Williamson, G.2    Puigserver, A.3    Chaix, J.-C.4    McLauchlan, W.R.5    Juge, N.6
  • 10
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R.: Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51-59 (1989).
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 11
    • 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., 31, 426-428 (1959).
    • (1959) Anal. Chem. , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 13
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K.: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680-685 (1970).
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0031459396 scopus 로고    scopus 로고
    • Production, purification and properties of an endoinulinase of Penicillium sp. TN-88 that liberates inulotriose
    • Nakamura, T., Shitara, A., Matsuda, S., Matsuo, T., Suiko, M., and Ohta, K.: Production, purification and properties of an endoinulinase of Penicillium sp. TN-88 that liberates inulotriose. J. Ferment. Bioeng., 84, 313-318 (1997).
    • (1997) J. Ferment. Bioeng. , vol.84 , pp. 313-318
    • Nakamura, T.1    Shitara, A.2    Matsuda, S.3    Matsuo, T.4    Suiko, M.5    Ohta, K.6
  • 15
    • 0030592470 scopus 로고    scopus 로고
    • Three-dimensional structure of endo-1,4-β-xylanase I from Aspergillus niger: Molecular basis for its low pH optimum
    • Krengel, U. and Dijkstra, B. W.: Three-dimensional structure of endo-1,4-β-xylanase I from Aspergillus niger: molecular basis for its low pH optimum. J. Mol. Biol., 263, 70-78 (1996).
    • (1996) J. Mol. Biol. , vol.263 , pp. 70-78
    • Krengel, U.1    Dijkstra, B.W.2
  • 16
    • 0032407988 scopus 로고    scopus 로고
    • Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: Biased distribution of acidic residues and importance of Asp37 for catalysis at low pH
    • Fushinobu, S., Ito, K., Konno, M., Wakagi, T., and Matsuzawa, H.: Crystallographic and mutational analyses of an extremely acidophilic and acid-stable xylanase: biased distribution of acidic residues and importance of Asp37 for catalysis at low pH. Protein Eng., 11, 1121-1128 (1998).
    • (1998) Protein Eng. , vol.11 , pp. 1121-1128
    • Fushinobu, S.1    Ito, K.2    Konno, M.3    Wakagi, T.4    Matsuzawa, H.5
  • 17
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C.: SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res., 31, 3381-3385 (2003).
    • (2003) Nucleic Acids Res. , vol.31 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • Guex, N. and Peitsch, M. C.: SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling. Electrophoresis, 18, 2714-2723 (1997).
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 19
    • 0029004590 scopus 로고
    • Protein modeling by e-mail
    • Peitsch, M. C.: Protein modeling by e-mail. Biotechnology (N.Y.), 13, 658-660 (1995).
    • (1995) Biotechnology (N.Y.) , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 20
    • 0028338985 scopus 로고
    • Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: Two conformational states in the active site
    • Törrönen, A., Harkki, A., and Rouvinen, J.: Three-dimensional structure of endo-1,4-β-xylanase II from Trichoderma reesei: two conformational states in the active site. EMBO J., 13, 2493-2501 (1994).
    • (1994) EMBO J. , vol.13 , pp. 2493-2501
    • Törrönen, A.1    Harkki, A.2    Rouvinen, J.3
  • 21
    • 0028070148 scopus 로고
    • Cloning, sequencing, and regulation of a xylanase gene from the fungus Aureobasidium pullulans Y-2311-1
    • Li, X. L. and Ljungdahl, L. G.: Cloning, sequencing, and regulation of a xylanase gene from the fungus Aureobasidium pullulans Y-2311-1. Appl. Environ. Microbiol., 60, 3160-3166 (1994).
    • (1994) Appl. Environ. Microbiol. , vol.60 , pp. 3160-3166
    • Li, X.L.1    Ljungdahl, L.G.2
  • 22
    • 0027359072 scopus 로고
    • Purification and characterization of a new xylanase (APX-II) from the fungus Aureobasidium pullulans Y-2311-1
    • Li, X. L., Zhang, Z. Q., Dean, J. F., Eriksson, K. E., and Ljungdahl, L. G.: Purification and characterization of a new xylanase (APX-II) from the fungus Aureobasidium pullulans Y-2311-1. Appl. Environ. Microbiol., 59, 3212-3218 (1993).
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 3212-3218
    • Li, X.L.1    Zhang, Z.Q.2    Dean, J.F.3    Eriksson, K.E.4    Ljungdahl, L.G.5
  • 23
    • 0037113937 scopus 로고    scopus 로고
    • Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger
    • Tahir, T. A., Berrin, J.-G., Flatman, R., Roussel, A., Roepstorff, P., Williamson, G., and Juge, N.: Specific characterization of substrate and inhibitor binding sites of a glycosyl hydrolase family 11 xylanase from Aspergillus niger. J. Biol. Chem., 277, 44035-44043 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 44035-44043
    • Tahir, T.A.1    Berrin, J.-G.2    Flatman, R.3    Roussel, A.4    Roepstorff, P.5    Williamson, G.6    Juge, N.7


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