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Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential
Thermophilic fungal cellulases are promising enzymes in protein engineering efforts aimed at optimizing industrial processes, such as biomass degradation and biofuel production. The cloning and expression in recent years of new cellulase genes from thermophilic fungi have led to a better understandi...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
SAGE-Hindawi Access to Research
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3226318/ https://www.ncbi.nlm.nih.gov/pubmed/22145076 http://dx.doi.org/10.4061/2011/308730 |
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author | Li, Duo-Chuan Li, An-Na Papageorgiou, Anastassios C. |
author_facet | Li, Duo-Chuan Li, An-Na Papageorgiou, Anastassios C. |
author_sort | Li, Duo-Chuan |
collection | PubMed |
description | Thermophilic fungal cellulases are promising enzymes in protein engineering efforts aimed at optimizing industrial processes, such as biomass degradation and biofuel production. The cloning and expression in recent years of new cellulase genes from thermophilic fungi have led to a better understanding of cellulose degradation in these species. Moreover, crystal structures of thermophilic fungal cellulases are now available, providing insights into their function and stability. The present paper is focused on recent progress in cloning, expression, regulation, and structure of thermophilic fungal cellulases and the current research efforts to improve their properties for better use in biotechnological applications. |
format | Online Article Text |
id | pubmed-3226318 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | SAGE-Hindawi Access to Research |
record_format | MEDLINE/PubMed |
spelling | pubmed-32263182011-12-05 Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential Li, Duo-Chuan Li, An-Na Papageorgiou, Anastassios C. Enzyme Res Review Article Thermophilic fungal cellulases are promising enzymes in protein engineering efforts aimed at optimizing industrial processes, such as biomass degradation and biofuel production. The cloning and expression in recent years of new cellulase genes from thermophilic fungi have led to a better understanding of cellulose degradation in these species. Moreover, crystal structures of thermophilic fungal cellulases are now available, providing insights into their function and stability. The present paper is focused on recent progress in cloning, expression, regulation, and structure of thermophilic fungal cellulases and the current research efforts to improve their properties for better use in biotechnological applications. SAGE-Hindawi Access to Research 2011 2011-11-17 /pmc/articles/PMC3226318/ /pubmed/22145076 http://dx.doi.org/10.4061/2011/308730 Text en Copyright © 2011 Duo-Chuan Li et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Li, Duo-Chuan Li, An-Na Papageorgiou, Anastassios C. Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential |
title | Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential |
title_full | Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential |
title_fullStr | Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential |
title_full_unstemmed | Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential |
title_short | Cellulases from Thermophilic Fungi: Recent Insights and Biotechnological Potential |
title_sort | cellulases from thermophilic fungi: recent insights and biotechnological potential |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3226318/ https://www.ncbi.nlm.nih.gov/pubmed/22145076 http://dx.doi.org/10.4061/2011/308730 |
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