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Volumn 67, Issue 4, 2005, Pages 495-505

Thermostable xylanases, Xyn10A and Xyn11A, from the actinomycete Nonomuraea flexuosa: Isolation of the genes and characterization of recombinant Xyn11A polypeptides produced in Trichoderma reesei

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; ESCHERICHIA COLI; GENES; GENETIC ENGINEERING; GLYCOLS; PLANTS (BOTANY); PURIFICATION; THERMODYNAMIC STABILITY;

EID: 21344465648     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-004-1797-x     Document Type: Article
Times cited : (51)

References (34)
  • 1
    • 0026537453 scopus 로고
    • Interlaboratory testing of methods for assay of xylanase activity
    • Bailey MJ, Biely P, Poutanen K (1992) Interlaboratory testing of methods for assay of xylanase activity. J Biotechnol 23:257-270
    • (1992) J Biotechnol , vol.23 , pp. 257-270
    • Bailey, M.J.1    Biely, P.2    Poutanen, K.3
  • 2
    • 0030002331 scopus 로고    scopus 로고
    • Purification and characterization of two different xylanases from the thermophilic actinomycete Microtetraspora flexuosa SIIX
    • Berens S, Kaspari H, Klemme J-H (1996) Purification and characterization of two different xylanases from the thermophilic actinomycete Microtetraspora flexuosa SIIX. Antonie van Leeuwenhoek. 69:235-241
    • (1996) Antonie Van Leeuwenhoek , vol.69 , pp. 235-241
    • Berens, S.1    Kaspari, H.2    Klemme, J.-H.3
  • 3
    • 0021982304 scopus 로고
    • Soluble chromogenic substrates for the assay of endo-1,4-beta-xylanases and endo1,4-beta-glucanases
    • Biely P, Mislovicova D, Toman R (1985) Soluble chromogenic substrates for the assay of endo-1,4-beta-xylanases and endo1,4-beta-glucanases. Anal Biochem 144:142-146
    • (1985) Anal Biochem , vol.144 , pp. 142-146
    • Biely, P.1    Mislovicova, D.2    Toman, R.3
  • 4
    • 0343036237 scopus 로고    scopus 로고
    • Endo-β-1,4-xylanase families: Differences in catalytic properties
    • Biely P, Vrsanská M, Tenkanen M, Kluepfel D (1997) Endo-β-1,4-xylanase families: differences in catalytic properties. J Biotechnol 57:151-166
    • (1997) J Biotechnol , vol.57 , pp. 151-166
    • Biely, P.1    Vrsanská, M.2    Tenkanen, M.3    Kluepfel, D.4
  • 6
    • 0024312683 scopus 로고
    • Cloning of a Thermomonospora fusca xylanase gene and its expression in Escherichia coli and Streptomyces lividans
    • Changas GS, Hu YJ, Wilson DB (1989) Cloning of a Thermomonospora fusca xylanase gene and its expression in Escherichia coli and Streptomyces lividans. J Bacteriol 171:2963-2969
    • (1989) J Bacteriol , vol.171 , pp. 2963-2969
    • Changas, G.S.1    Hu, Y.J.2    Wilson, D.B.3
  • 7
    • 0030772482 scopus 로고    scopus 로고
    • Family-10 and family-11 xylanases differ in their capacity to enhance the bleachability of hardwood and softwood paper pulps
    • Clarke JH, Rixon JE, Ciruela A, Gilbert HJ, Hazlewood GP (1997) Family-10 and family-11 xylanases differ in their capacity to enhance the bleachability of hardwood and softwood paper pulps. Appl Microbiol Biotechnol 48:177-183
    • (1997) Appl Microbiol Biotechnol , vol.48 , pp. 177-183
    • Clarke, J.H.1    Rixon, J.E.2    Ciruela, A.3    Gilbert, H.J.4    Hazlewood, G.P.5
  • 8
    • 0027503913 scopus 로고
    • Thermostable xylanolytic enzymes from Rhodothermus marinus grown on xylan
    • Dalhberg L, Holst O, Kristjansson JK (1993) Thermostable xylanolytic enzymes from Rhodothermus marinus grown on xylan. Appl Microbiol Biotechnol 40:63-68
    • (1993) Appl Microbiol Biotechnol , vol.40 , pp. 63-68
    • Dalhberg, L.1    Holst, O.2    Kristjansson, J.K.3
  • 9
    • 0032519716 scopus 로고    scopus 로고
    • Substrate-binding domains of glycanases from Streptomyces lividans: Characterization of a new family of xylan-binding domains
    • Dupont C, Roberge M, Shareck F, Morosoli R, Kluepfel D (1998) Substrate-binding domains of glycanases from Streptomyces lividans: characterization of a new family of xylan-binding domains. Biochem J 330:41-45
    • (1998) Biochem J , vol.330 , pp. 41-45
    • Dupont, C.1    Roberge, M.2    Shareck, F.3    Morosoli, R.4    Kluepfel, D.5
  • 10
    • 0028227497 scopus 로고
    • Cloning of two xylanase genes from the newly isolated actinomycete Actinomadura sp.strain FC7 and characterization of the gene products
    • Ethier J-F, Harpin S, Girard C, Beaulieu C, Déry CV, Brzezinski R (1994) Cloning of two xylanase genes from the newly isolated actinomycete Actinomadura sp.strain FC7 and characterization of the gene products. Can J Microbiol 40:362-368
    • (1994) Can J Microbiol , vol.40 , pp. 362-368
    • Ethier, J.-F.1    Harpin, S.2    Girard, C.3    Beaulieu, C.4    Déry, C.V.5    Brzezinski, R.6
  • 11
    • 0028919386 scopus 로고
    • Characterization, subsite mapping and partial amino acid sequence of glucoamylase from the filamentous fungus Trichoderma reesei
    • Fagerström R, Kalkkinen N (1995) Characterization, subsite mapping and partial amino acid sequence of glucoamylase from the filamentous fungus Trichoderma reesei. Biotechnol Appl Biochem 21:223-231
    • (1995) Biotechnol Appl Biochem , vol.21 , pp. 223-231
    • Fagerström, R.1    Kalkkinen, N.2
  • 12
    • 0034647437 scopus 로고    scopus 로고
    • Crystal structure of Streptomyces olivaceoviridis E-86 β-xylanase containing xylan-binding domain
    • Fujimoto Z, Kuno A, Kaneko S, Yoshida S, Kobayashi H, Kusakabe I, Mizuno H (2000) Crystal structure of Streptomyces olivaceoviridis E-86 β-xylanase containing xylan-binding domain. J Mol Biol 300:575-585
    • (2000) J Mol Biol , vol.300 , pp. 575-585
    • Fujimoto, Z.1    Kuno, A.2    Kaneko, S.3    Yoshida, S.4    Kobayashi, H.5    Kusakabe, I.6    Mizuno, H.7
  • 13
    • 0033952763 scopus 로고    scopus 로고
    • Purification and properties of three endo-β-1,4-xylanases produced by Streptomyces sp. strain S38 which differ in their ability to enhance the bleaching of kraft pulps
    • Georis J, Giannotta F, De Buyl E, Granier B, Frère J-M (2000) Purification and properties of three endo-β-1,4-xylanases produced by Streptomyces sp. strain S38 which differ in their ability to enhance the bleaching of kraft pulps. Enzyme Microb Technol 26:178-186
    • (2000) Enzyme Microb Technol , vol.26 , pp. 178-186
    • Georis, J.1    Giannotta, F.2    De Buyl, E.3    Granier, B.4    Frère, J.-M.5
  • 14
    • 0344406096 scopus 로고    scopus 로고
    • Three-dimensional structures of thermophilic β-1,4-xylanases from Chaetomium thermophilum and Nonomurea flexuosa. Comparison of twelve xylanases in relation to their thermal stability
    • Hakulinen NO, Turunen O, Jänis J, Leisola M, Rouvinen J (2003) Three-dimensional structures of thermophilic β-1,4-xylanases from Chaetomium thermophilum and Nonomurea flexuosa. Comparison of twelve xylanases in relation to their thermal stability. Eur J Biochem 270:1399-1412
    • (2003) Eur J Biochem , vol.270 , pp. 1399-1412
    • Hakulinen, N.O.1    Turunen, O.2    Jänis, J.3    Leisola, M.4    Rouvinen, J.5
  • 15
    • 0032571552 scopus 로고    scopus 로고
    • A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants
    • Henrissat B, Teeri TT, Warren RAJ (1998) A scheme for designating enzymes that hydrolyse the polysaccharides in the cell walls of plants. FEBS Lett 425:352-354
    • (1998) FEBS Lett , vol.425 , pp. 352-354
    • Henrissat, B.1    Teeri, T.T.2    Warren, R.A.J.3
  • 16
    • 0032486273 scopus 로고    scopus 로고
    • Novel galactose-binding proteins in Annelida. Characterization of 29 kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris
    • Hirabayashi J, Dutta SK, Kasai K (1998) Novel galactose-binding proteins in Annelida. Characterization of 29 kDa tandem repeat-type lectins from the earthworm Lumbricus terrestris. J Biol Chem 273:14450-14460
    • (1998) J Biol Chem , vol.273 , pp. 14450-14460
    • Hirabayashi, J.1    Dutta, S.K.2    Kasai, K.3
  • 17
    • 0002364468 scopus 로고
    • Production and properties of xylanases from thermophilic actinomycetes
    • Holtz C, Kaspari H, Klemme J-H (1991) Production and properties of xylanases from thermophilic actinomycetes. Antonie van Leeuwenhoek 59:1-7
    • (1991) Antonie Van Leeuwenhoek , vol.59 , pp. 1-7
    • Holtz, C.1    Kaspari, H.2    Klemme, J.-H.3
  • 19
    • 0028294637 scopus 로고
    • Characterization and sequence of a Thermomonospora fusca xylanase
    • Irwin D, Jung ED, Wilson DB (1994) Characterization and sequence of a Thermomonospora fusca xylanase. Appl Environ Microbiol 60:763-770
    • (1994) Appl Environ Microbiol , vol.60 , pp. 763-770
    • Irwin, D.1    Jung, E.D.2    Wilson, D.B.3
  • 20
    • 0000830863 scopus 로고
    • A gas-pulsed liquid-phase sequencer constructed from a Beckman 890D instrument by using Applied Biosystems delivery and cartridge blocks
    • Kalkkinen N, Tilgmann C (1988) A gas-pulsed liquid-phase sequencer constructed from a Beckman 890D instrument by using Applied Biosystems delivery and cartridge blocks. J Protein Chem 7:242-243
    • (1988) J Protein Chem , vol.7 , pp. 242-243
    • Kalkkinen, N.1    Tilgmann, C.2
  • 22
    • 0026460431 scopus 로고
    • Thermophilic and alkalophilic xylanases from several Dictyoglomus isolates
    • Mathrani IM, Ahring BK (1992) Thermophilic and alkalophilic xylanases from several Dictyoglomus isolates. Appl Microbiol Biotechnol 38:23-27
    • (1992) Appl Microbiol Biotechnol , vol.38 , pp. 23-27
    • Mathrani, I.M.1    Ahring, B.K.2
  • 24
    • 2142855140 scopus 로고    scopus 로고
    • High-yield production of a bacterial xylanase in the filamentous fungus Trichoderma reesei requires a carrier polypeptide with an intact domain structure
    • Paloheimo M, Mäntylä A, Kallio J, Suominen P (2003) High-yield production of a bacterial xylanase in the filamentous fungus Trichoderma reesei requires a carrier polypeptide with an intact domain structure. Appl Environ Microbiol 69:7073-7082
    • (2003) Appl Environ Microbiol , vol.69 , pp. 7073-7082
    • Paloheimo, M.1    Mäntylä, A.2    Kallio, J.3    Suominen, P.4
  • 25
    • 0030452145 scopus 로고    scopus 로고
    • Do the non-catalytic polysaccharide-binding domains and linker regions enhance the biobleaching properties of modular xylanases?
    • Rixon JE, Clarke JH, Hazlewood GP, Hoyland RW, McCarthy AJ, Gilbert HJ (1996) Do the non-catalytic polysaccharide-binding domains and linker regions enhance the biobleaching properties of modular xylanases? Appl Microbiol Biotechnol 46:514-520
    • (1996) Appl Microbiol Biotechnol , vol.46 , pp. 514-520
    • Rixon, J.E.1    Clarke, J.H.2    Hazlewood, G.P.3    Hoyland, R.W.4    McCarthy, A.J.5    Gilbert, H.J.6
  • 26
    • 0027134879 scopus 로고
    • Cloning, sequencing and enhanced expression of the Trichoderma reesei endoxylanase II (pI 9) gene xln2
    • Saarelainen R, Paloheimo M, Fagerström R, Suominen PL, Nevalainen KMH (1993) Cloning, sequencing and enhanced expression of the Trichoderma reesei endoxylanase II (pI 9) gene xln2. Mol Gen Genet 241:497-503
    • (1993) Mol Gen Genet , vol.241 , pp. 497-503
    • Saarelainen, R.1    Paloheimo, M.2    Fagerström, R.3    Suominen, P.L.4    Nevalainen, K.M.H.5
  • 28
    • 0026045488 scopus 로고
    • Sequences of three genes specifying xylanases in Streptomyces lividans
    • Shareck F, Roy C, Yaguchi M, Morosoli R, Kluepfel D (1991) Sequences of three genes specifying xylanases in Streptomyces lividans. Gene 107:75-82
    • (1991) Gene , vol.107 , pp. 75-82
    • Shareck, F.1    Roy, C.2    Yaguchi, M.3    Morosoli, R.4    Kluepfel, D.5
  • 29
    • 0000178351 scopus 로고    scopus 로고
    • A family IIb xylan-binding domain has similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity
    • Simpson PJ, Bolam DN, Cooper A, Ciruela A, Hazlewood GP, Gilbert HJ, Williamson MP (1999) A family IIb xylan-binding domain has similar secondary structure to a homologous family IIa cellulose-binding domain but different ligand specificity. Structure 7:853-864
    • (1999) Structure , vol.7 , pp. 853-864
    • Simpson, P.J.1    Bolam, D.N.2    Cooper, A.3    Ciruela, A.4    Hazlewood, G.P.5    Gilbert, H.J.6    Williamson, M.P.7
  • 33
    • 0031799382 scopus 로고    scopus 로고
    • Reclassification of Thermomonospora and Microtetraspora
    • Zhang Z, Wang Y, Ruan J (1998) Reclassification of Thermomonospora and Microtetraspora. Int J Syst Bacteriol 48:411-422
    • (1998) Int J Syst Bacteriol , vol.48 , pp. 411-422
    • Zhang, Z.1    Wang, Y.2    Ruan, J.3
  • 34
    • 0029916417 scopus 로고    scopus 로고
    • The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant
    • Zverlov V, Piotukh K, Dakhova O, Velikodvorskaya G, Borriss R (1996) The multidomain xylanase A of the hyperthermophilic bacterium Thermotoga neapolitana is extremely thermoresistant. Appl Microbiol Biotechnol 45:245-247
    • (1996) Appl Microbiol Biotechnol , vol.45 , pp. 245-247
    • Zverlov, V.1    Piotukh, K.2    Dakhova, O.3    Velikodvorskaya, G.4    Borriss, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.