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Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome
Cellulases play a key role in enzymatic routes for degradation of plant cell-wall polysaccharides into simple and economically-relevant sugars. However, their low performance on complex substrates and reduced stability under industrial conditions remain the main obstacle for the large-scale producti...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3866126/ https://www.ncbi.nlm.nih.gov/pubmed/24358302 http://dx.doi.org/10.1371/journal.pone.0083635 |
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author | Alvarez, Thabata M. Paiva, Joice H. Ruiz, Diego M. Cairo, João Paulo L. F. Pereira, Isabela O. Paixão, Douglas A. A. de Almeida, Rodrigo F. Tonoli, Celisa C. C. Ruller, Roberto Santos, Camila R. Squina, Fabio M. Murakami, Mario T. |
author_facet | Alvarez, Thabata M. Paiva, Joice H. Ruiz, Diego M. Cairo, João Paulo L. F. Pereira, Isabela O. Paixão, Douglas A. A. de Almeida, Rodrigo F. Tonoli, Celisa C. C. Ruller, Roberto Santos, Camila R. Squina, Fabio M. Murakami, Mario T. |
author_sort | Alvarez, Thabata M. |
collection | PubMed |
description | Cellulases play a key role in enzymatic routes for degradation of plant cell-wall polysaccharides into simple and economically-relevant sugars. However, their low performance on complex substrates and reduced stability under industrial conditions remain the main obstacle for the large-scale production of cellulose-derived products and biofuels. Thus, in this study a novel cellulase with unusual catalytic properties from sugarcane soil metagenome (CelE1) was isolated and characterized. The polypeptide deduced from the celE1 gene encodes a unique glycoside hydrolase domain belonging to GH5 family. The recombinant enzyme was active on both carboxymethyl cellulose and β-glucan with an endo-acting mode according to capillary electrophoretic analysis of cleavage products. CelE1 showed optimum hydrolytic activity at pH 7.0 and 50 °C with remarkable activity at alkaline conditions that is attractive for industrial applications in which conventional acidic cellulases are not suitable. Moreover, its three-dimensional structure was determined at 1.8 Å resolution that allowed the identification of an insertion of eight residues in the β8-α8 loop of the catalytic domain of CelE1, which is not conserved in its psychrophilic orthologs. This 8-residue-long segment is a prominent and distinguishing feature of thermotolerant cellulases 5 suggesting that it might be involved with thermal stability. Based on its unconventional characteristics, CelE1 could be potentially employed in biotechnological processes that require thermotolerant and alkaline cellulases. |
format | Online Article Text |
id | pubmed-3866126 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Public Library of Science |
record_format | MEDLINE/PubMed |
spelling | pubmed-38661262013-12-19 Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome Alvarez, Thabata M. Paiva, Joice H. Ruiz, Diego M. Cairo, João Paulo L. F. Pereira, Isabela O. Paixão, Douglas A. A. de Almeida, Rodrigo F. Tonoli, Celisa C. C. Ruller, Roberto Santos, Camila R. Squina, Fabio M. Murakami, Mario T. PLoS One Research Article Cellulases play a key role in enzymatic routes for degradation of plant cell-wall polysaccharides into simple and economically-relevant sugars. However, their low performance on complex substrates and reduced stability under industrial conditions remain the main obstacle for the large-scale production of cellulose-derived products and biofuels. Thus, in this study a novel cellulase with unusual catalytic properties from sugarcane soil metagenome (CelE1) was isolated and characterized. The polypeptide deduced from the celE1 gene encodes a unique glycoside hydrolase domain belonging to GH5 family. The recombinant enzyme was active on both carboxymethyl cellulose and β-glucan with an endo-acting mode according to capillary electrophoretic analysis of cleavage products. CelE1 showed optimum hydrolytic activity at pH 7.0 and 50 °C with remarkable activity at alkaline conditions that is attractive for industrial applications in which conventional acidic cellulases are not suitable. Moreover, its three-dimensional structure was determined at 1.8 Å resolution that allowed the identification of an insertion of eight residues in the β8-α8 loop of the catalytic domain of CelE1, which is not conserved in its psychrophilic orthologs. This 8-residue-long segment is a prominent and distinguishing feature of thermotolerant cellulases 5 suggesting that it might be involved with thermal stability. Based on its unconventional characteristics, CelE1 could be potentially employed in biotechnological processes that require thermotolerant and alkaline cellulases. Public Library of Science 2013-12-17 /pmc/articles/PMC3866126/ /pubmed/24358302 http://dx.doi.org/10.1371/journal.pone.0083635 Text en © 2013 Alvarez et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited. |
spellingShingle | Research Article Alvarez, Thabata M. Paiva, Joice H. Ruiz, Diego M. Cairo, João Paulo L. F. Pereira, Isabela O. Paixão, Douglas A. A. de Almeida, Rodrigo F. Tonoli, Celisa C. C. Ruller, Roberto Santos, Camila R. Squina, Fabio M. Murakami, Mario T. Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome |
title | Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome |
title_full | Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome |
title_fullStr | Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome |
title_full_unstemmed | Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome |
title_short | Structure and Function of a Novel Cellulase 5 from Sugarcane Soil Metagenome |
title_sort | structure and function of a novel cellulase 5 from sugarcane soil metagenome |
topic | Research Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3866126/ https://www.ncbi.nlm.nih.gov/pubmed/24358302 http://dx.doi.org/10.1371/journal.pone.0083635 |
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