Characterization of novel thermostable fungal cellobiohydrolases

T. Puranen, Sanni Voutilainen, Matti Siika-aho, J. Kallio, Satu Hooman, Liisa Viikari, Anu Koivula, J. Vehmaanperä

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

Abstract

Cellulose degradation requires sequential or simultaneous synergic action of three types of hydrolytic enzymes: cellobiohydrolases, endoglucanases and beta-glucosidases. Various filamentous fungi produce these enzymes in order to hydrolyze insoluble cellulose into glucose. Cellulases are currently extensively studied in enzyme industry for cellulosic biomass conversion to ethanol. Here, molecular cloning of three different cellobiohydrolase genes from thermophilic ascomycetes is presented together with their heterologous expression in Trichoderma reesei. The recombinant cellobiohydrolases that belong to the glycosyl hydrolase (GH) family 7 were purified and characterized in terms of pH optimum, thermal stability and kinetic parameters. Thermostable cellulases such as described here have been proposed to improve the overall process economy of the biomass conversion with favourable impact on enzyme need, hydrolysis performance and flexibility of the process.
Original languageEnglish
Title of host publication3rd European Federation of Biotechnology Conference
Subtitle of host publicationPhysiology of Yeasts and Filamentous Fungi PYFF3. Kuokka-Ihalainen
Place of PublicationEspoo
PublisherVTT Technical Research Centre of Finland
Pages145
ISBN (Electronic)978-951-38-6314-2
ISBN (Print)978-951-38-6313-5
Publication statusPublished - 2007
Event3rd European Federation of Biotechnology Conference : Physiology of Yeasts and Filamentous Fungi - Helsinki, Finland
Duration: 13 Jun 200716 Jun 2007

Publication series

SeriesVTT Symposium
Number245
ISSN0357-9387

Conference

Conference3rd European Federation of Biotechnology Conference
Abbreviated titlePYFF3
CountryFinland
CityHelsinki
Period13/06/0716/06/07

Fingerprint

cellulose 1,4-beta-cellobiosidase
cellulases
enzymes
cellulose
Trichoderma reesei
glycosidases
biomass
beta-glucosidase
thermal stability
endo-1,4-beta-glucanase
Ascomycota
molecular cloning
hydrolysis
ethanol
industry
kinetics
glucose
fungi
degradation
genes

Cite this

Puranen, T., Voutilainen, S., Siika-aho, M., Kallio, J., Hooman, S., Viikari, L., ... Vehmaanperä, J. (2007). Characterization of novel thermostable fungal cellobiohydrolases. In 3rd European Federation of Biotechnology Conference: Physiology of Yeasts and Filamentous Fungi PYFF3. Kuokka-Ihalainen (pp. 145). [P89] Espoo: VTT Technical Research Centre of Finland. VTT Symposium, No. 245
Puranen, T. ; Voutilainen, Sanni ; Siika-aho, Matti ; Kallio, J. ; Hooman, Satu ; Viikari, Liisa ; Koivula, Anu ; Vehmaanperä, J. / Characterization of novel thermostable fungal cellobiohydrolases. 3rd European Federation of Biotechnology Conference: Physiology of Yeasts and Filamentous Fungi PYFF3. Kuokka-Ihalainen. Espoo : VTT Technical Research Centre of Finland, 2007. pp. 145 (VTT Symposium; No. 245).
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abstract = "Cellulose degradation requires sequential or simultaneous synergic action of three types of hydrolytic enzymes: cellobiohydrolases, endoglucanases and beta-glucosidases. Various filamentous fungi produce these enzymes in order to hydrolyze insoluble cellulose into glucose. Cellulases are currently extensively studied in enzyme industry for cellulosic biomass conversion to ethanol. Here, molecular cloning of three different cellobiohydrolase genes from thermophilic ascomycetes is presented together with their heterologous expression in Trichoderma reesei. The recombinant cellobiohydrolases that belong to the glycosyl hydrolase (GH) family 7 were purified and characterized in terms of pH optimum, thermal stability and kinetic parameters. Thermostable cellulases such as described here have been proposed to improve the overall process economy of the biomass conversion with favourable impact on enzyme need, hydrolysis performance and flexibility of the process.",
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Puranen, T, Voutilainen, S, Siika-aho, M, Kallio, J, Hooman, S, Viikari, L, Koivula, A & Vehmaanperä, J 2007, Characterization of novel thermostable fungal cellobiohydrolases. in 3rd European Federation of Biotechnology Conference: Physiology of Yeasts and Filamentous Fungi PYFF3. Kuokka-Ihalainen., P89, VTT Technical Research Centre of Finland, Espoo, VTT Symposium, no. 245, pp. 145, 3rd European Federation of Biotechnology Conference , Helsinki, Finland, 13/06/07.

Characterization of novel thermostable fungal cellobiohydrolases. / Puranen, T.; Voutilainen, Sanni; Siika-aho, Matti; Kallio, J.; Hooman, Satu; Viikari, Liisa; Koivula, Anu; Vehmaanperä, J.

3rd European Federation of Biotechnology Conference: Physiology of Yeasts and Filamentous Fungi PYFF3. Kuokka-Ihalainen. Espoo : VTT Technical Research Centre of Finland, 2007. p. 145 P89 (VTT Symposium; No. 245).

Research output: Chapter in Book/Report/Conference proceedingConference abstract in proceedingsScientific

TY - CHAP

T1 - Characterization of novel thermostable fungal cellobiohydrolases

AU - Puranen, T.

AU - Voutilainen, Sanni

AU - Siika-aho, Matti

AU - Kallio, J.

AU - Hooman, Satu

AU - Viikari, Liisa

AU - Koivula, Anu

AU - Vehmaanperä, J.

PY - 2007

Y1 - 2007

N2 - Cellulose degradation requires sequential or simultaneous synergic action of three types of hydrolytic enzymes: cellobiohydrolases, endoglucanases and beta-glucosidases. Various filamentous fungi produce these enzymes in order to hydrolyze insoluble cellulose into glucose. Cellulases are currently extensively studied in enzyme industry for cellulosic biomass conversion to ethanol. Here, molecular cloning of three different cellobiohydrolase genes from thermophilic ascomycetes is presented together with their heterologous expression in Trichoderma reesei. The recombinant cellobiohydrolases that belong to the glycosyl hydrolase (GH) family 7 were purified and characterized in terms of pH optimum, thermal stability and kinetic parameters. Thermostable cellulases such as described here have been proposed to improve the overall process economy of the biomass conversion with favourable impact on enzyme need, hydrolysis performance and flexibility of the process.

AB - Cellulose degradation requires sequential or simultaneous synergic action of three types of hydrolytic enzymes: cellobiohydrolases, endoglucanases and beta-glucosidases. Various filamentous fungi produce these enzymes in order to hydrolyze insoluble cellulose into glucose. Cellulases are currently extensively studied in enzyme industry for cellulosic biomass conversion to ethanol. Here, molecular cloning of three different cellobiohydrolase genes from thermophilic ascomycetes is presented together with their heterologous expression in Trichoderma reesei. The recombinant cellobiohydrolases that belong to the glycosyl hydrolase (GH) family 7 were purified and characterized in terms of pH optimum, thermal stability and kinetic parameters. Thermostable cellulases such as described here have been proposed to improve the overall process economy of the biomass conversion with favourable impact on enzyme need, hydrolysis performance and flexibility of the process.

M3 - Conference abstract in proceedings

SN - 978-951-38-6313-5

T3 - VTT Symposium

SP - 145

BT - 3rd European Federation of Biotechnology Conference

PB - VTT Technical Research Centre of Finland

CY - Espoo

ER -

Puranen T, Voutilainen S, Siika-aho M, Kallio J, Hooman S, Viikari L et al. Characterization of novel thermostable fungal cellobiohydrolases. In 3rd European Federation of Biotechnology Conference: Physiology of Yeasts and Filamentous Fungi PYFF3. Kuokka-Ihalainen. Espoo: VTT Technical Research Centre of Finland. 2007. p. 145. P89. (VTT Symposium; No. 245).