Thermostable enzymes in lignocellulose hydrolysis

Liisa Viikari, Marika Alapuranen, Terhi Puranen, Jari Vehmaanperä, Matti Siika-aho

Research output: Chapter in Book/Report/Conference proceedingChapter or book articleScientificpeer-review

239 Citations (Scopus)

Abstract

Thermostable enzymes offer potential benefits in the hydrolysis of lignocellulosic substrates; higher specific activity decreasing the amount of enzymes, enhanced stability allowing improved hydrolysis performance and increased flexibility with respect to process configurations, all leading to improvement of the overall economy of the process. New thermostable cellulase mixtures were composed of cloned fungal enzymes for hydrolysis experiments. Three thermostable cellulases, identified as the most promising enzymes in their categories (cellobiohydrolase, endoglucanase and β-glucosidase), were cloned and produced in Trichoderma reesei and mixed to compose a novel mixture of thermostable cellulases. Thermostable xylanase was added to enzyme preparations used on substrates containing residual hemicellulose. The new optimised thermostable enzyme mixtures were evaluated in high temperature hydrolysis experiments on technical steam pretreated raw materials: spruce and corn stover. The hydrolysis temperature could be increased by about 10–15 °C, as compared with present commercial Trichoderma enzymes. The same degree of hydrolysis, about 90% of theoretical, measured as individual sugars, could be obtained with the thermostable enzymes at 60 °C as with the commercial enzymes at 45 °C. Clearly more efficient hydrolysis per assayed FPU unit or per amount of cellobiohydrolase I protein used was obtained. The maximum FPU activity of the novel enzyme mixture was about 25% higher at the optimum temperature at 65 °C, as compared with the highest activity of the commercial reference enzyme at 60 °C. The results provide a promising basis to produce and formulate improved enzyme products. These products can have high temperature stability in process conditions in the range of 55–60 °C (with present industrial products at 45–50 °C) and clearly improved specific activity, essentially decreasing the protein dosage required for an efficient hydrolysis of lignocellulosic substrates. New types of process configurations based on thermostable enzymes are discussed.
Original languageEnglish
Title of host publicationBiofuels
EditorsLisbeth Olsson
Place of PublicationBerlin - Heidelberg
PublisherSpringer
Pages121-145
ISBN (Electronic)978-3-540-73651-6
ISBN (Print)Print ISBN 978-3-540-73650-9
DOIs
Publication statusPublished - 2007
MoE publication typeA3 Part of a book or another research book

Publication series

SeriesAdvances in Biochemical Engineering/Biotechnology
Volume108
ISSN0724-6145

Fingerprint

lignocellulose
hydrolysis
enzymes
cellulose 1,4-beta-cellobiosidase
cellulases
endo-1,4-beta-glucanase
temperature
Trichoderma reesei
glucosidases
corn stover
Trichoderma
xylanases
hemicellulose
steam
raw materials
Picea

Keywords

  • thermostable
  • cellulases
  • cellobiohydrolase
  • endoglucanase
  • beta-glucosidase
  • lignocellulose
  • hydrolysis

Cite this

Viikari, L., Alapuranen, M., Puranen, T., Vehmaanperä, J., & Siika-aho, M. (2007). Thermostable enzymes in lignocellulose hydrolysis. In L. Olsson (Ed.), Biofuels (pp. 121-145). Berlin - Heidelberg: Springer. Advances in Biochemical Engineering/Biotechnology, Vol.. 108 https://doi.org/10.1007/10_2007_065
Viikari, Liisa ; Alapuranen, Marika ; Puranen, Terhi ; Vehmaanperä, Jari ; Siika-aho, Matti. / Thermostable enzymes in lignocellulose hydrolysis. Biofuels. editor / Lisbeth Olsson. Berlin - Heidelberg : Springer, 2007. pp. 121-145 (Advances in Biochemical Engineering/Biotechnology, Vol. 108).
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Viikari, L, Alapuranen, M, Puranen, T, Vehmaanperä, J & Siika-aho, M 2007, Thermostable enzymes in lignocellulose hydrolysis. in L Olsson (ed.), Biofuels. Springer, Berlin - Heidelberg, Advances in Biochemical Engineering/Biotechnology, vol. 108, pp. 121-145. https://doi.org/10.1007/10_2007_065

Thermostable enzymes in lignocellulose hydrolysis. / Viikari, Liisa; Alapuranen, Marika; Puranen, Terhi; Vehmaanperä, Jari; Siika-aho, Matti.

Biofuels. ed. / Lisbeth Olsson. Berlin - Heidelberg : Springer, 2007. p. 121-145 (Advances in Biochemical Engineering/Biotechnology, Vol. 108).

Research output: Chapter in Book/Report/Conference proceedingChapter or book articleScientificpeer-review

TY - CHAP

T1 - Thermostable enzymes in lignocellulose hydrolysis

AU - Viikari, Liisa

AU - Alapuranen, Marika

AU - Puranen, Terhi

AU - Vehmaanperä, Jari

AU - Siika-aho, Matti

PY - 2007

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N2 - Thermostable enzymes offer potential benefits in the hydrolysis of lignocellulosic substrates; higher specific activity decreasing the amount of enzymes, enhanced stability allowing improved hydrolysis performance and increased flexibility with respect to process configurations, all leading to improvement of the overall economy of the process. New thermostable cellulase mixtures were composed of cloned fungal enzymes for hydrolysis experiments. Three thermostable cellulases, identified as the most promising enzymes in their categories (cellobiohydrolase, endoglucanase and β-glucosidase), were cloned and produced in Trichoderma reesei and mixed to compose a novel mixture of thermostable cellulases. Thermostable xylanase was added to enzyme preparations used on substrates containing residual hemicellulose. The new optimised thermostable enzyme mixtures were evaluated in high temperature hydrolysis experiments on technical steam pretreated raw materials: spruce and corn stover. The hydrolysis temperature could be increased by about 10–15 °C, as compared with present commercial Trichoderma enzymes. The same degree of hydrolysis, about 90% of theoretical, measured as individual sugars, could be obtained with the thermostable enzymes at 60 °C as with the commercial enzymes at 45 °C. Clearly more efficient hydrolysis per assayed FPU unit or per amount of cellobiohydrolase I protein used was obtained. The maximum FPU activity of the novel enzyme mixture was about 25% higher at the optimum temperature at 65 °C, as compared with the highest activity of the commercial reference enzyme at 60 °C. The results provide a promising basis to produce and formulate improved enzyme products. These products can have high temperature stability in process conditions in the range of 55–60 °C (with present industrial products at 45–50 °C) and clearly improved specific activity, essentially decreasing the protein dosage required for an efficient hydrolysis of lignocellulosic substrates. New types of process configurations based on thermostable enzymes are discussed.

AB - Thermostable enzymes offer potential benefits in the hydrolysis of lignocellulosic substrates; higher specific activity decreasing the amount of enzymes, enhanced stability allowing improved hydrolysis performance and increased flexibility with respect to process configurations, all leading to improvement of the overall economy of the process. New thermostable cellulase mixtures were composed of cloned fungal enzymes for hydrolysis experiments. Three thermostable cellulases, identified as the most promising enzymes in their categories (cellobiohydrolase, endoglucanase and β-glucosidase), were cloned and produced in Trichoderma reesei and mixed to compose a novel mixture of thermostable cellulases. Thermostable xylanase was added to enzyme preparations used on substrates containing residual hemicellulose. The new optimised thermostable enzyme mixtures were evaluated in high temperature hydrolysis experiments on technical steam pretreated raw materials: spruce and corn stover. The hydrolysis temperature could be increased by about 10–15 °C, as compared with present commercial Trichoderma enzymes. The same degree of hydrolysis, about 90% of theoretical, measured as individual sugars, could be obtained with the thermostable enzymes at 60 °C as with the commercial enzymes at 45 °C. Clearly more efficient hydrolysis per assayed FPU unit or per amount of cellobiohydrolase I protein used was obtained. The maximum FPU activity of the novel enzyme mixture was about 25% higher at the optimum temperature at 65 °C, as compared with the highest activity of the commercial reference enzyme at 60 °C. The results provide a promising basis to produce and formulate improved enzyme products. These products can have high temperature stability in process conditions in the range of 55–60 °C (with present industrial products at 45–50 °C) and clearly improved specific activity, essentially decreasing the protein dosage required for an efficient hydrolysis of lignocellulosic substrates. New types of process configurations based on thermostable enzymes are discussed.

KW - thermostable

KW - cellulases

KW - cellobiohydrolase

KW - endoglucanase

KW - beta-glucosidase

KW - lignocellulose

KW - hydrolysis

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DO - 10.1007/10_2007_065

M3 - Chapter or book article

SN - Print ISBN 978-3-540-73650-9

T3 - Advances in Biochemical Engineering/Biotechnology

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BT - Biofuels

A2 - Olsson, Lisbeth

PB - Springer

CY - Berlin - Heidelberg

ER -

Viikari L, Alapuranen M, Puranen T, Vehmaanperä J, Siika-aho M. Thermostable enzymes in lignocellulose hydrolysis. In Olsson L, editor, Biofuels. Berlin - Heidelberg: Springer. 2007. p. 121-145. (Advances in Biochemical Engineering/Biotechnology, Vol. 108). https://doi.org/10.1007/10_2007_065