Abstract
| Original language | English |
|---|---|
| Pages (from-to) | 377 - 386 |
| Journal | Applied Microbiology and Biotechnology |
| Volume | 76 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2007 |
| MoE publication type | A1 Journal article-refereed |
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Keywords
- Trichoderma reesei
- xylanases
- Chaetomium thermophilum
- recombinant proteins
- biobleaching
- bleaching
- pulp
- Kraft pulp
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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 journal › Article › Scientific › peer-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 -