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Hyperthermophilic endoglucanase for in planta lignocellulose conversion

BACKGROUND: The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the sustainable and environmentally friendly production of biofuels. However, a major drawback of enzymes from mesophilic sources is their suboptimal activity under established pretreat...

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Autores principales: Klose, Holger, Röder, Juliane, Girfoglio, Michele, Fischer, Rainer, Commandeur, Ulrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3497586/
https://www.ncbi.nlm.nih.gov/pubmed/22928996
http://dx.doi.org/10.1186/1754-6834-5-63
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author Klose, Holger
Röder, Juliane
Girfoglio, Michele
Fischer, Rainer
Commandeur, Ulrich
author_facet Klose, Holger
Röder, Juliane
Girfoglio, Michele
Fischer, Rainer
Commandeur, Ulrich
author_sort Klose, Holger
collection PubMed
description BACKGROUND: The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the sustainable and environmentally friendly production of biofuels. However, a major drawback of enzymes from mesophilic sources is their suboptimal activity under established pretreatment conditions, e.g. high temperatures, extreme pH values and high salt concentrations. Enzymes from extremophiles are better adapted to these conditions and could be produced by heterologous expression in microbes, or even directly in the plant biomass. RESULTS: Here we show that a cellulase gene (sso1354) isolated from the hyperthermophilic archaeon Sulfolobus solfataricus can be expressed in plants, and that the recombinant enzyme is biologically active and exhibits the same properties as the wild type form. Since the enzyme is inactive under normal plant growth conditions, this potentially allows its expression in plants without negative effects on growth and development, and subsequent heat-inducible activation. Furthermore we demonstrate that the recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade α-cellulose or even complex cell wall preparations under those pretreatment conditions. CONCLUSION: The hyperthermophilic endoglucanase SSO1354 with its unique features is an excellent tool for advanced biomass conversion. Here we demonstrate its expression in planta and the possibility for post harvest activation. Moreover the enzyme is suitable for combined pretreatment and hydrolysis applications.
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spelling pubmed-34975862012-11-15 Hyperthermophilic endoglucanase for in planta lignocellulose conversion Klose, Holger Röder, Juliane Girfoglio, Michele Fischer, Rainer Commandeur, Ulrich Biotechnol Biofuels Research BACKGROUND: The enzymatic conversion of lignocellulosic plant biomass into fermentable sugars is a crucial step in the sustainable and environmentally friendly production of biofuels. However, a major drawback of enzymes from mesophilic sources is their suboptimal activity under established pretreatment conditions, e.g. high temperatures, extreme pH values and high salt concentrations. Enzymes from extremophiles are better adapted to these conditions and could be produced by heterologous expression in microbes, or even directly in the plant biomass. RESULTS: Here we show that a cellulase gene (sso1354) isolated from the hyperthermophilic archaeon Sulfolobus solfataricus can be expressed in plants, and that the recombinant enzyme is biologically active and exhibits the same properties as the wild type form. Since the enzyme is inactive under normal plant growth conditions, this potentially allows its expression in plants without negative effects on growth and development, and subsequent heat-inducible activation. Furthermore we demonstrate that the recombinant enzyme acts in high concentrations of ionic liquids and can therefore degrade α-cellulose or even complex cell wall preparations under those pretreatment conditions. CONCLUSION: The hyperthermophilic endoglucanase SSO1354 with its unique features is an excellent tool for advanced biomass conversion. Here we demonstrate its expression in planta and the possibility for post harvest activation. Moreover the enzyme is suitable for combined pretreatment and hydrolysis applications. BioMed Central 2012-08-28 /pmc/articles/PMC3497586/ /pubmed/22928996 http://dx.doi.org/10.1186/1754-6834-5-63 Text en Copyright ©2012 Klose et al.; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
Klose, Holger
Röder, Juliane
Girfoglio, Michele
Fischer, Rainer
Commandeur, Ulrich
Hyperthermophilic endoglucanase for in planta lignocellulose conversion
title Hyperthermophilic endoglucanase for in planta lignocellulose conversion
title_full Hyperthermophilic endoglucanase for in planta lignocellulose conversion
title_fullStr Hyperthermophilic endoglucanase for in planta lignocellulose conversion
title_full_unstemmed Hyperthermophilic endoglucanase for in planta lignocellulose conversion
title_short Hyperthermophilic endoglucanase for in planta lignocellulose conversion
title_sort hyperthermophilic endoglucanase for in planta lignocellulose conversion
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3497586/
https://www.ncbi.nlm.nih.gov/pubmed/22928996
http://dx.doi.org/10.1186/1754-6834-5-63
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