High level secretion of cellobiohydrolases by Saccharomyces cerevisiae

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

Standard

High level secretion of cellobiohydrolases by Saccharomyces cerevisiae. / Ilmen, Marja; den Haan, Riaan; Brevnova, Elena; McBride, John; Wiswall, Erin; Froehlich, Allan; Koivula, Anu; Voutilainen, Sanni P.; Siika-Aho, Matti; la Grange, Daniel C.; Thorngren, Naomi; Ahlgren, Simon; Mellon, Mark; Deleault, Kristen; Rajgarhia, Vineet; van Zyl, Willem H.; Penttilä, Merja.

julkaisussa: Biotechnology for Biofuels, Vuosikerta 4, 30, 12.09.2011.

Tutkimustuotos: Lehtiartikkelivertaisarvioitu

Harvard

Ilmen, M, den Haan, R, Brevnova, E, McBride, J, Wiswall, E, Froehlich, A, Koivula, A, Voutilainen, SP, Siika-Aho, M, la Grange, DC, Thorngren, N, Ahlgren, S, Mellon, M, Deleault, K, Rajgarhia, V, van Zyl, WH & Penttilä, M 2011, 'High level secretion of cellobiohydrolases by Saccharomyces cerevisiae', Biotechnology for Biofuels, Vuosikerta. 4, 30. https://doi.org/10.1186/1754-6834-4-30

APA

Vancouver

Ilmen M, den Haan R, Brevnova E, McBride J, Wiswall E, Froehlich A et al. High level secretion of cellobiohydrolases by Saccharomyces cerevisiae. Biotechnology for Biofuels. 2011 syys 12;4. 30. https://doi.org/10.1186/1754-6834-4-30

Author

Ilmen, Marja ; den Haan, Riaan ; Brevnova, Elena ; McBride, John ; Wiswall, Erin ; Froehlich, Allan ; Koivula, Anu ; Voutilainen, Sanni P. ; Siika-Aho, Matti ; la Grange, Daniel C. ; Thorngren, Naomi ; Ahlgren, Simon ; Mellon, Mark ; Deleault, Kristen ; Rajgarhia, Vineet ; van Zyl, Willem H. ; Penttilä, Merja. / High level secretion of cellobiohydrolases by Saccharomyces cerevisiae. Julkaisussa: Biotechnology for Biofuels. 2011 ; Vuosikerta 4.

Bibtex - Lataa

@article{b6f02a688c744b618d7c4aa71f8c3ae3,
title = "High level secretion of cellobiohydrolases by Saccharomyces cerevisiae",
abstract = "Background: The main technological impediment to widespread utilization of lignocellulose for the production of fuels and chemicals is the lack of low-cost technologies to overcome its recalcitrance. Organisms that hydrolyze lignocellulose and produce a valuable product such as ethanol at a high rate and titer could significantly reduce the costs of biomass conversion technologies, and will allow separate conversion steps to be combined in a consolidated bioprocess (CBP). Development of Saccharomyces cerevisiae for CBP requires the high level secretion of cellulases, particularly cellobiohydrolases.Results: We expressed various cellobiohydrolases to identify enzymes that were efficiently secreted by S. cerevisiae. For enhanced cellulose hydrolysis, we engineered bimodular derivatives of a well secreted enzyme that naturally lacks the carbohydrate-binding module, and constructed strains expressing combinations of cbh1 and cbh2 genes. Though there was significant variability in the enzyme levels produced, up to approximately 0.3 g/L CBH1 and approximately 1 g/L CBH2 could be produced in high cell density fermentations. Furthermore, we could show activation of the unfolded protein response as a result of cellobiohydrolase production. Finally, we report fermentation of microcrystalline cellulose (Avicel T) to ethanol by CBH-producing S. cerevisiae strains with the addition of beta-glucosidase.Conclusions: Gene or protein specific features and compatibility with the host are important for efficient cellobiohydrolase secretion in yeast. The present work demonstrated that production of both CBH1 and CBH2 could be improved to levels where the barrier to CBH sufficiency in the hydrolysis of cellulose was overcome.",
keywords = "biofuels, cellulolytic yeast, UPR, UNFOLDED-PROTEIN RESPONSE, TRICHODERMA-REESEI, BETA-GLUCOSIDASE, CELLULOSE HYDROLYSIS, DELTA-INTEGRATION, YEAST STRAINS, EXPRESSION, GENE, STRESS, COORDINATION",
author = "Marja Ilmen and {den Haan}, Riaan and Elena Brevnova and John McBride and Erin Wiswall and Allan Froehlich and Anu Koivula and Voutilainen, {Sanni P.} and Matti Siika-Aho and {la Grange}, {Daniel C.} and Naomi Thorngren and Simon Ahlgren and Mark Mellon and Kristen Deleault and Vineet Rajgarhia and {van Zyl}, {Willem H.} and Merja Penttil{\"a}",
year = "2011",
month = "9",
day = "12",
doi = "10.1186/1754-6834-4-30",
language = "English",
volume = "4",
journal = "Biotechnology for Biofuels",
issn = "1754-6834",
publisher = "BioMed Central",

}

RIS - Lataa

TY - JOUR

T1 - High level secretion of cellobiohydrolases by Saccharomyces cerevisiae

AU - Ilmen, Marja

AU - den Haan, Riaan

AU - Brevnova, Elena

AU - McBride, John

AU - Wiswall, Erin

AU - Froehlich, Allan

AU - Koivula, Anu

AU - Voutilainen, Sanni P.

AU - Siika-Aho, Matti

AU - la Grange, Daniel C.

AU - Thorngren, Naomi

AU - Ahlgren, Simon

AU - Mellon, Mark

AU - Deleault, Kristen

AU - Rajgarhia, Vineet

AU - van Zyl, Willem H.

AU - Penttilä, Merja

PY - 2011/9/12

Y1 - 2011/9/12

N2 - Background: The main technological impediment to widespread utilization of lignocellulose for the production of fuels and chemicals is the lack of low-cost technologies to overcome its recalcitrance. Organisms that hydrolyze lignocellulose and produce a valuable product such as ethanol at a high rate and titer could significantly reduce the costs of biomass conversion technologies, and will allow separate conversion steps to be combined in a consolidated bioprocess (CBP). Development of Saccharomyces cerevisiae for CBP requires the high level secretion of cellulases, particularly cellobiohydrolases.Results: We expressed various cellobiohydrolases to identify enzymes that were efficiently secreted by S. cerevisiae. For enhanced cellulose hydrolysis, we engineered bimodular derivatives of a well secreted enzyme that naturally lacks the carbohydrate-binding module, and constructed strains expressing combinations of cbh1 and cbh2 genes. Though there was significant variability in the enzyme levels produced, up to approximately 0.3 g/L CBH1 and approximately 1 g/L CBH2 could be produced in high cell density fermentations. Furthermore, we could show activation of the unfolded protein response as a result of cellobiohydrolase production. Finally, we report fermentation of microcrystalline cellulose (Avicel T) to ethanol by CBH-producing S. cerevisiae strains with the addition of beta-glucosidase.Conclusions: Gene or protein specific features and compatibility with the host are important for efficient cellobiohydrolase secretion in yeast. The present work demonstrated that production of both CBH1 and CBH2 could be improved to levels where the barrier to CBH sufficiency in the hydrolysis of cellulose was overcome.

AB - Background: The main technological impediment to widespread utilization of lignocellulose for the production of fuels and chemicals is the lack of low-cost technologies to overcome its recalcitrance. Organisms that hydrolyze lignocellulose and produce a valuable product such as ethanol at a high rate and titer could significantly reduce the costs of biomass conversion technologies, and will allow separate conversion steps to be combined in a consolidated bioprocess (CBP). Development of Saccharomyces cerevisiae for CBP requires the high level secretion of cellulases, particularly cellobiohydrolases.Results: We expressed various cellobiohydrolases to identify enzymes that were efficiently secreted by S. cerevisiae. For enhanced cellulose hydrolysis, we engineered bimodular derivatives of a well secreted enzyme that naturally lacks the carbohydrate-binding module, and constructed strains expressing combinations of cbh1 and cbh2 genes. Though there was significant variability in the enzyme levels produced, up to approximately 0.3 g/L CBH1 and approximately 1 g/L CBH2 could be produced in high cell density fermentations. Furthermore, we could show activation of the unfolded protein response as a result of cellobiohydrolase production. Finally, we report fermentation of microcrystalline cellulose (Avicel T) to ethanol by CBH-producing S. cerevisiae strains with the addition of beta-glucosidase.Conclusions: Gene or protein specific features and compatibility with the host are important for efficient cellobiohydrolase secretion in yeast. The present work demonstrated that production of both CBH1 and CBH2 could be improved to levels where the barrier to CBH sufficiency in the hydrolysis of cellulose was overcome.

KW - biofuels

KW - cellulolytic yeast

KW - UPR

KW - UNFOLDED-PROTEIN RESPONSE

KW - TRICHODERMA-REESEI

KW - BETA-GLUCOSIDASE

KW - CELLULOSE HYDROLYSIS

KW - DELTA-INTEGRATION

KW - YEAST STRAINS

KW - EXPRESSION

KW - GENE

KW - STRESS

KW - COORDINATION

U2 - 10.1186/1754-6834-4-30

DO - 10.1186/1754-6834-4-30

M3 - Article

VL - 4

JO - Biotechnology for Biofuels

JF - Biotechnology for Biofuels

SN - 1754-6834

M1 - 30

ER -

ID: 9227861