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Volumn 121, Issue 3, 2006, Pages 381-389

An Aspergillus oryzae acetyl xylan esterase: Molecular cloning and characteristics of recombinant enzyme expressed in Pichia pastoris

Author keywords

Acetyl xylan esterase; Aspergillus oryzae; Heterologous expression; Pichia pastoris

Indexed keywords

ACETIC ACID; AMINO ACIDS; CELL CULTURE; CLONING; ENZYME KINETICS; GENETIC ENGINEERING; PROTEINS;

EID: 30944456517     PISSN: 01681656     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jbiotec.2005.07.015     Document Type: Article
Times cited : (32)

References (30)
  • 1
    • 12244299847 scopus 로고    scopus 로고
    • Subtractive cloning of cDNA from Aspergillus oryzae differentially regulated between solid-state culture and liquid (submerged) culture
    • T. Akao, K. Gomi, K. Goto, N. Okazaki, and O. Akita Subtractive cloning of cDNA from Aspergillus oryzae differentially regulated between solid-state culture and liquid (submerged) culture Curr. Genet. 41 2002 275 281
    • (2002) Curr. Genet. , vol.41 , pp. 275-281
    • Akao, T.1    Gomi, K.2    Goto, K.3    Okazaki, N.4    Akita, O.5
  • 2
    • 0021863774 scopus 로고
    • Acetyl xylan esterases in fungal cellulolytic systems
    • P. Biely, J. Puls, and H. Schneider Acetyl xylan esterases in fungal cellulolytic systems FEBS Lett. 186 1985 80 84
    • (1985) FEBS Lett. , vol.186 , pp. 80-84
    • Biely, P.1    Puls, J.2    Schneider, H.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0037009162 scopus 로고    scopus 로고
    • Cloning the gene encoding acetyl xylan esterase from Aspergillus ficuum and its expression in Pichia pastoris
    • H.J. Chung, S.M. Park, H.R. Kim, M.S. Yang, and D.H. Kim Cloning the gene encoding acetyl xylan esterase from Aspergillus ficuum and its expression in Pichia pastoris Enzyme Microb. Technol. 31 2002 384 391
    • (2002) Enzyme Microb. Technol. , vol.31 , pp. 384-391
    • Chung, H.J.1    Park, S.M.2    Kim, H.R.3    Yang, M.S.4    Kim, D.H.5
  • 5
    • 84981976048 scopus 로고
    • β-1,4-d-Xylan-degrading systems: Biochemistry, molecular biology and applications
    • M.P. Coughlan, and G.P. Hazlewood β-1,4-d-Xylan-degrading systems: biochemistry, molecular biology and applications Biotechnol. Appl. Biochem. 17 1993 259 289
    • (1993) Biotechnol. Appl. Biochem. , vol.17 , pp. 259-289
    • Coughlan, M.P.1    Hazlewood, G.P.2
  • 6
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • H.J. Gilbert G.J. Davies B. Henrissat B. Svensson The Royal Society of Chemistry Cambridge, UK
    • P.M. Coutinho, and B. Henrissat Carbohydrate-active enzymes: an integrated database approach H.J. Gilbert G.J. Davies B. Henrissat B. Svensson Recent Advances in Carbohydrate Bioengineering 1999 The Royal Society of Chemistry Cambridge, UK 3 12
    • (1999) Recent Advances in Carbohydrate Bioengineering , pp. 3-12
    • Coutinho, P.M.1    Henrissat, B.2
  • 7
    • 0242417646 scopus 로고    scopus 로고
    • A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition
    • V.F. Crepin, C.B. Faulds, and I.F. Connerton A non-modular type B feruloyl esterase from Neurospora crassa exhibits concentration-dependent substrate inhibition Biochem. J. 370 2003 417 427
    • (2003) Biochem. J. , vol.370 , pp. 417-427
    • Crepin, V.F.1    Faulds, C.B.2    Connerton, I.F.3
  • 9
    • 0031912439 scopus 로고    scopus 로고
    • Purification and characterization of an acetyl xylan esterase from Bacillus pumilus
    • G. Degrassi, B.C. Okeke, C.V. Bruschi, and V. Venturi Purification and characterization of an acetyl xylan esterase from Bacillus pumilus Appl. Environ. Microbiol. 64 1998 789 792
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 789-792
    • Degrassi, G.1    Okeke, B.C.2    Bruschi, C.V.3    Venturi, V.4
  • 10
    • 0033910674 scopus 로고    scopus 로고
    • The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterase with broad substrate specificity
    • G. Degrassi, M. Kojic, G. Ljubijankic, and V. Venturi The acetyl xylan esterase of Bacillus pumilus belongs to a family of esterase with broad substrate specificity Microbiolgy 146 2000 1585 1591
    • (2000) Microbiolgy , vol.146 , pp. 1585-1591
    • Degrassi, G.1    Kojic, M.2    Ljubijankic, G.3    Venturi, V.4
  • 11
    • 0034618210 scopus 로고    scopus 로고
    • Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides
    • R.P. De Vries, H.C.M. Kester, C.H. Poulsen, J.A.E. Benen, and J. Visser Synergy between enzymes from Aspergillus involved in the degradation of plant cell wall polysaccharides Carbohydr. Res. 327 2000 401 410
    • (2000) Carbohydr. Res. , vol.327 , pp. 401-410
    • De Vries, R.P.1    Kester, H.C.M.2    Poulsen, C.H.3    Benen, J.A.E.4    Visser, J.5
  • 13
    • 0028218853 scopus 로고
    • Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: Specificity for the phenolic moiety and binding to microcrystalline cellulose
    • C.B. Faulds, and G. Williamson Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to microcrystalline cellulose Microbiology 140 1994 779 787
    • (1994) Microbiology , vol.140 , pp. 779-787
    • Faulds, C.B.1    Williamson, G.2
  • 15
    • 0344765499 scopus 로고    scopus 로고
    • Acetylxylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain
    • R. Gutierrez, E. Cederlund, L. Hjelmqvist, A. Peirano, F. Herrera, D. Ghosh, W. Duax, H. Jörnvall, and J. Eyzaguirre Acetylxylan esterase II from Penicillium purpurogenum is similar to an esterase from Trichoderma reesei but lacks a cellulose binding domain FEBS Lett. 423 1998 35 38
    • (1998) FEBS Lett. , vol.423 , pp. 35-38
    • Gutierrez, R.1    Cederlund, E.2    Hjelmqvist, L.3    Peirano, A.4    Herrera, F.5    Ghosh, D.6    Duax, W.7    Jörnvall, H.8    Eyzaguirre, J.9
  • 16
    • 0034465722 scopus 로고    scopus 로고
    • Three-dimensional structure of the catalytic core of acetyl xylan esterase from Trichoderma reesei: Insights into the deacetylation mechanism
    • N. Hakulinen, M. Tenkanen, and J. Rouvinen Three-dimensional structure of the catalytic core of acetyl xylan esterase from Trichoderma reesei: insights into the deacetylation mechanism J. Struct. Biol. 132 2000 180 190
    • (2000) J. Struct. Biol. , vol.132 , pp. 180-190
    • Hakulinen, N.1    Tenkanen, M.2    Rouvinen, J.3
  • 17
    • 0028295908 scopus 로고
    • Purification and some characteristics of the acetylxylan esterase from Schizophyllum commune
    • N. Halgašová, E. Kutejová, and J. Timko Purification and some characteristics of the acetylxylan esterase from Schizophyllum commune Biochem. J. 298 1994 751 755
    • (1994) Biochem. J. , vol.298 , pp. 751-755
    • Halgašová, N.1    Kutejová, E.2    Timko, J.3
  • 18
    • 0035735155 scopus 로고    scopus 로고
    • High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris
    • N. Juge, G. Williamson, A. Puigserver, N.J. Cuimmings, I.F. Connerton, and C.B. Faulds High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris FEMS Yeast Res. 1 2001 127 132
    • (2001) FEMS Yeast Res. , vol.1 , pp. 127-132
    • Juge, N.1    Williamson, G.2    Puigserver, A.3    Cuimmings, N.J.4    Connerton, I.F.5    Faulds, C.B.6
  • 19
    • 0027415218 scopus 로고
    • Purification and characterization of an acetyl xylan esterase from Aspergillus niger
    • F.J.M. Kormelink, B. Lefebvre, F. Strozyk, and A.G.J. Voragen Purification and characterization of an acetyl xylan esterase from Aspergillus niger J. Biotechnol. 27 1993 267 282
    • (1993) J. Biotechnol. , vol.27 , pp. 267-282
    • Kormelink, F.J.M.1    Lefebvre, B.2    Strozyk, F.3    Voragen, A.G.J.4
  • 20
    • 0030765089 scopus 로고    scopus 로고
    • An Aspergillus awamori acetylesterase: Purification of the enzyme, and cloning and sequencing of the gene
    • T. Koseki, S. Furuse, K. Iwano, H. Sakai, and H. Matsuzawa An Aspergillus awamori acetylesterase: purification of the enzyme, and cloning and sequencing of the gene Biochem. J. 326 1997 485 490
    • (1997) Biochem. J. , vol.326 , pp. 485-490
    • Koseki, T.1    Furuse, S.2    Iwano, K.3    Sakai, H.4    Matsuzawa, H.5
  • 21
    • 17444381937 scopus 로고    scopus 로고
    • Biochemical characterization of recombinant acetyl xylan esterase from Aspergillus awamori expressed in Pichia pastoris: Mutational analysis of catalytic residues
    • T. Koseki, Y. Miwa, S. Fushinobu, and K. Hashizume Biochemical characterization of recombinant acetyl xylan esterase from Aspergillus awamori expressed in Pichia pastoris: mutational analysis of catalytic residues Biochim. Biophys. Acta 1749 2005 7 13
    • (2005) Biochim. Biophys. Acta , vol.1749 , pp. 7-13
    • Koseki, T.1    Miwa, Y.2    Fushinobu, S.3    Hashizume, K.4
  • 22
    • 14544295340 scopus 로고    scopus 로고
    • Mutational analysis of a feruloyl esterase from Aspergillus awamori involved in substrate discrimination and pH dependence
    • T. Koseki, K. Takahashi, S. Fushinobu, H. Iefuji, K. Iwano, K. Hashizume, and H. Matsuzawa Mutational analysis of a feruloyl esterase from Aspergillus awamori involved in substrate discrimination and pH dependence Biochim. Biophys. Acta 1722 2005 200 208
    • (2005) Biochim. Biophys. Acta , vol.1722 , pp. 200-208
    • Koseki, T.1    Takahashi, K.2    Fushinobu, S.3    Iefuji, H.4    Iwano, K.5    Hashizume, K.6    Matsuzawa, H.7
  • 23
    • 0033679102 scopus 로고    scopus 로고
    • A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module
    • P.A. Kroon, G. Williamson, N.M. Fish, D.B. Archer, and N.J. Belshaw A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module Eur. J. Biochem. 267 2000 6740 6752
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6740-6752
    • Kroon, P.A.1    Williamson, G.2    Fish, N.M.3    Archer, D.B.4    Belshaw, N.J.5
  • 24
    • 0030886131 scopus 로고    scopus 로고
    • Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: A β-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity
    • W.W. Lorenz, and J. Wiegel Isolation, analysis, and expression of two genes from Thermoanaerobacterium sp. strain JW/SL YS485: a β-xylosidase and a novel acetyl xylan esterase with cephalosporin C deacetylase activity J. Bacteriol. 179 1997 5436 5441
    • (1997) J. Bacteriol. , vol.179 , pp. 5436-5441
    • Lorenz, W.W.1    Wiegel, J.2
  • 25
    • 0029992163 scopus 로고    scopus 로고
    • Acetylxylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain
    • E. Margolles-Clark, M. Tenkanen, H. Söderlund, and M. Penttilä Acetylxylan esterase from Trichoderma reesei contains an active-site serine residue and a cellulose-binding domain Eur. J. Biochem. 237 1996 553 560
    • (1996) Eur. J. Biochem. , vol.237 , pp. 553-560
    • Margolles-Clark, E.1    Tenkanen, M.2    Söderlund, H.3    Penttilä, M.4
  • 27
    • 0028869651 scopus 로고
    • Purification and characterization of two thermostable acetyl xylan esterases from Thermoanaerobacterium sp. strain JW/SL YS485
    • W. Shao, and J. Wiegel Purification and characterization of two thermostable acetyl xylan esterases from Thermoanaerobacterium sp. strain JW/SL YS485 Appl. Environ. Microbiol. 61 1995 729 733
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 729-733
    • Shao, W.1    Wiegel, J.2
  • 28
    • 0025969260 scopus 로고
    • Purification and properties of two acetyl xylan esterases of Trichoderma reesei
    • M. Sundberg, and K. Poutanen Purification and properties of two acetyl xylan esterases of Trichoderma reesei Biotechnol. Appl. Biochem. 13 1991 1 11
    • (1991) Biotechnol. Appl. Biochem. , vol.13 , pp. 1-11
    • Sundberg, M.1    Poutanen, K.2
  • 29
    • 0026031235 scopus 로고
    • Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics
    • M. Tenkanen, J. Schuseil, J. Puls, and K. Poutanen Production, purification and characterization of an esterase liberating phenolic acids from lignocellulosics J. Biotechnol. 18 1991 69 84
    • (1991) J. Biotechnol. , vol.18 , pp. 69-84
    • Tenkanen, M.1    Schuseil, J.2    Puls, J.3    Poutanen, K.4
  • 30
    • 0028862433 scopus 로고
    • An acetylglucomannan esterase of Aspergillus oryzae; Purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan
    • M. Tenkanen, J. Thornton, and L. Viikari An acetylglucomannan esterase of Aspergillus oryzae; purification, characterization and role in the hydrolysis of O-acetyl-galactoglucomannan J. Biotechnol. 42 1995 197 206
    • (1995) J. Biotechnol. , vol.42 , pp. 197-206
    • Tenkanen, M.1    Thornton, J.2    Viikari, L.3


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