Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum: A recombinant thermoxylanase for biobleaching of kraft pulp

Arja Mäntylä (Corresponding Author), Marja Paloheimo, Satu Hakola, Emilia: Leskinen, Sanna Lindberg, Jarno Kallio, Jari Vehmaanperä, Raija Lantto, Pirkko Suominen

Research output: Contribution to journalArticleScientificpeer-review

23 Citations (Scopus)

Abstract

Abstract Three endoxylanase genes were cloned from the thermophilic fungus Chaetomium thermophilum CBS 730.95. All genes contained the typical consensus sequence of family 11 glycoside hydrolases. Genomic copies of Ct xyn11A, Ct xyn11B, and Ct xyn11C were expressed in the filamentous fungus T. reesei under the control of the strong T. reesei cel7A (cellobiohydrolase 1, cbh1) promoter. The molecular masses of the Ct Xyn11A, Ct Xyn11B, and Ct Xyn11C proteins on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were 27, 23, and 22 kDa, respectively. Ct Xyn11A was produced almost as efficiently as the homologous xylanase II from a corresponding single-copy transformant strain. Ct Xyn11B production level was approximately half of that of Ct Xyn11A. The amount of Ct Xyn11C was remarkably lower. Ct Xyn11A had the highest temperature optimum and stability of the recombinant xylanases and the highest activity at acid-neutral pH (pH 5–7). It was the most suitable for industrial bleaching of kraft pulp at high temperature.
Original languageEnglish
Pages (from-to)377 - 386
JournalApplied Microbiology and Biotechnology
Volume76
Issue number2
DOIs
Publication statusPublished - 2007
MoE publication typeA1 Journal article-refereed

Fingerprint

Chaetomium
Trichoderma
Fungi
Cellulose 1,4-beta-Cellobiosidase
Endo-1,4-beta Xylanases
Temperature
Glycoside Hydrolases
Consensus Sequence
Sodium Dodecyl Sulfate
Genes
Polyacrylamide Gel Electrophoresis
Acids
Proteins

Keywords

  • Trichoderma reesei
  • xylanases
  • Chaetomium thermophilum
  • recombinant proteins
  • biobleaching
  • bleaching
  • pulp
  • Kraft pulp

Cite this

Mäntylä, Arja ; Paloheimo, Marja ; Hakola, Satu ; Lindberg, Emilia: Leskinen, Sanna ; Kallio, Jarno ; Vehmaanperä, Jari ; Lantto, Raija ; Suominen, Pirkko. / Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum : A recombinant thermoxylanase for biobleaching of kraft pulp. In: Applied Microbiology and Biotechnology. 2007 ; Vol. 76, No. 2. pp. 377 - 386.
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abstract = "Abstract Three endoxylanase genes were cloned from the thermophilic fungus Chaetomium thermophilum CBS 730.95. All genes contained the typical consensus sequence of family 11 glycoside hydrolases. Genomic copies of Ct xyn11A, Ct xyn11B, and Ct xyn11C were expressed in the filamentous fungus T. reesei under the control of the strong T. reesei cel7A (cellobiohydrolase 1, cbh1) promoter. The molecular masses of the Ct Xyn11A, Ct Xyn11B, and Ct Xyn11C proteins on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were 27, 23, and 22 kDa, respectively. Ct Xyn11A was produced almost as efficiently as the homologous xylanase II from a corresponding single-copy transformant strain. Ct Xyn11B production level was approximately half of that of Ct Xyn11A. The amount of Ct Xyn11C was remarkably lower. Ct Xyn11A had the highest temperature optimum and stability of the recombinant xylanases and the highest activity at acid-neutral pH (pH 5–7). It was the most suitable for industrial bleaching of kraft pulp at high temperature.",
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author = "Arja M{\"a}ntyl{\"a} and Marja Paloheimo and Satu Hakola and Lindberg, {Emilia: Leskinen, Sanna} and Jarno Kallio and Jari Vehmaanper{\"a} and Raija Lantto and Pirkko Suominen",
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Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum : A recombinant thermoxylanase for biobleaching of kraft pulp. / Mäntylä, Arja (Corresponding Author); Paloheimo, Marja; Hakola, Satu; Lindberg, Emilia: Leskinen, Sanna; Kallio, Jarno; Vehmaanperä, Jari; Lantto, Raija; Suominen, Pirkko.

In: Applied Microbiology and Biotechnology, Vol. 76, No. 2, 2007, p. 377 - 386.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Production in Trichoderma reesei of three xylanases from Chaetomium thermophilum

T2 - A recombinant thermoxylanase for biobleaching of kraft pulp

AU - Mäntylä, Arja

AU - Paloheimo, Marja

AU - Hakola, Satu

AU - Lindberg, Emilia: Leskinen, Sanna

AU - Kallio, Jarno

AU - Vehmaanperä, Jari

AU - Lantto, Raija

AU - Suominen, Pirkko

PY - 2007

Y1 - 2007

N2 - Abstract Three endoxylanase genes were cloned from the thermophilic fungus Chaetomium thermophilum CBS 730.95. All genes contained the typical consensus sequence of family 11 glycoside hydrolases. Genomic copies of Ct xyn11A, Ct xyn11B, and Ct xyn11C were expressed in the filamentous fungus T. reesei under the control of the strong T. reesei cel7A (cellobiohydrolase 1, cbh1) promoter. The molecular masses of the Ct Xyn11A, Ct Xyn11B, and Ct Xyn11C proteins on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were 27, 23, and 22 kDa, respectively. Ct Xyn11A was produced almost as efficiently as the homologous xylanase II from a corresponding single-copy transformant strain. Ct Xyn11B production level was approximately half of that of Ct Xyn11A. The amount of Ct Xyn11C was remarkably lower. Ct Xyn11A had the highest temperature optimum and stability of the recombinant xylanases and the highest activity at acid-neutral pH (pH 5–7). It was the most suitable for industrial bleaching of kraft pulp at high temperature.

AB - Abstract Three endoxylanase genes were cloned from the thermophilic fungus Chaetomium thermophilum CBS 730.95. All genes contained the typical consensus sequence of family 11 glycoside hydrolases. Genomic copies of Ct xyn11A, Ct xyn11B, and Ct xyn11C were expressed in the filamentous fungus T. reesei under the control of the strong T. reesei cel7A (cellobiohydrolase 1, cbh1) promoter. The molecular masses of the Ct Xyn11A, Ct Xyn11B, and Ct Xyn11C proteins on sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) were 27, 23, and 22 kDa, respectively. Ct Xyn11A was produced almost as efficiently as the homologous xylanase II from a corresponding single-copy transformant strain. Ct Xyn11B production level was approximately half of that of Ct Xyn11A. The amount of Ct Xyn11C was remarkably lower. Ct Xyn11A had the highest temperature optimum and stability of the recombinant xylanases and the highest activity at acid-neutral pH (pH 5–7). It was the most suitable for industrial bleaching of kraft pulp at high temperature.

KW - Trichoderma reesei

KW - xylanases

KW - Chaetomium thermophilum

KW - recombinant proteins

KW - biobleaching

KW - bleaching

KW - pulp

KW - Kraft pulp

U2 - 10.1007/s00253-007-1020-y

DO - 10.1007/s00253-007-1020-y

M3 - Article

VL - 76

SP - 377

EP - 386

JO - Applied Microbiology and Biotechnology

JF - Applied Microbiology and Biotechnology

SN - 0175-7598

IS - 2

ER -