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Thermostability in endoglucanases is fold-specific

BACKGROUND: Endoglucanases are usually considered to be synergistically involved in the initial stages of cellulose breakdown-an essential step in the bioprocessing of lignocellulosic plant materials into bioethanol. Despite their economic importance, we currently lack a basic understanding of how s...

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Detalles Bibliográficos
Autores principales: Yennamalli, Ragothaman M, Rader, Andrew J, Wolt, Jeffrey D, Sen, Taner Z
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3047435/
https://www.ncbi.nlm.nih.gov/pubmed/21291533
http://dx.doi.org/10.1186/1472-6807-11-10
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author Yennamalli, Ragothaman M
Rader, Andrew J
Wolt, Jeffrey D
Sen, Taner Z
author_facet Yennamalli, Ragothaman M
Rader, Andrew J
Wolt, Jeffrey D
Sen, Taner Z
author_sort Yennamalli, Ragothaman M
collection PubMed
description BACKGROUND: Endoglucanases are usually considered to be synergistically involved in the initial stages of cellulose breakdown-an essential step in the bioprocessing of lignocellulosic plant materials into bioethanol. Despite their economic importance, we currently lack a basic understanding of how some endoglucanases can sustain their ability to function at elevated temperatures required for bioprocessing, while others cannot. In this study, we present a detailed comparative analysis of both thermophilic and mesophilic endoglucanases in order to gain insights into origins of thermostability. We analyzed the sequences and structures for sets of endoglucanase proteins drawn from the Carbohydrate-Active enZymes (CAZy) database. RESULTS: Our results demonstrate that thermophilic endoglucanases and their mesophilic counterparts differ significantly in their amino acid compositions. Strikingly, these compositional differences are specific to protein folds and enzyme families, and lead to differences in intramolecular interactions in a fold-dependent fashion. CONCLUSIONS: Here, we provide fold-specific guidelines to control thermostability in endoglucanases that will aid in making production of biofuels from plant biomass more efficient.
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spelling pubmed-30474352011-03-03 Thermostability in endoglucanases is fold-specific Yennamalli, Ragothaman M Rader, Andrew J Wolt, Jeffrey D Sen, Taner Z BMC Struct Biol Research Article BACKGROUND: Endoglucanases are usually considered to be synergistically involved in the initial stages of cellulose breakdown-an essential step in the bioprocessing of lignocellulosic plant materials into bioethanol. Despite their economic importance, we currently lack a basic understanding of how some endoglucanases can sustain their ability to function at elevated temperatures required for bioprocessing, while others cannot. In this study, we present a detailed comparative analysis of both thermophilic and mesophilic endoglucanases in order to gain insights into origins of thermostability. We analyzed the sequences and structures for sets of endoglucanase proteins drawn from the Carbohydrate-Active enZymes (CAZy) database. RESULTS: Our results demonstrate that thermophilic endoglucanases and their mesophilic counterparts differ significantly in their amino acid compositions. Strikingly, these compositional differences are specific to protein folds and enzyme families, and lead to differences in intramolecular interactions in a fold-dependent fashion. CONCLUSIONS: Here, we provide fold-specific guidelines to control thermostability in endoglucanases that will aid in making production of biofuels from plant biomass more efficient. BioMed Central 2011-02-03 /pmc/articles/PMC3047435/ /pubmed/21291533 http://dx.doi.org/10.1186/1472-6807-11-10 Text en Copyright ©2011 Yennamalli 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 Article
Yennamalli, Ragothaman M
Rader, Andrew J
Wolt, Jeffrey D
Sen, Taner Z
Thermostability in endoglucanases is fold-specific
title Thermostability in endoglucanases is fold-specific
title_full Thermostability in endoglucanases is fold-specific
title_fullStr Thermostability in endoglucanases is fold-specific
title_full_unstemmed Thermostability in endoglucanases is fold-specific
title_short Thermostability in endoglucanases is fold-specific
title_sort thermostability in endoglucanases is fold-specific
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3047435/
https://www.ncbi.nlm.nih.gov/pubmed/21291533
http://dx.doi.org/10.1186/1472-6807-11-10
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