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Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome
Cellulase catalyzes the hydrolysis of β-1,4-linkages of cellulose to produce industrially relevant monomeric subunits. Cellulases find their applications in pulp and paper, laundry, food and feed, textile, brewing industry and in biofuel production. These industries always have great demand for cell...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5180356/ https://www.ncbi.nlm.nih.gov/pubmed/28008971 http://dx.doi.org/10.1038/srep39634 |
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author | Garg, Roma Srivastava, Ritika Brahma, Vijaya Verma, Lata Karthikeyan, Subramanian Sahni, Girish |
author_facet | Garg, Roma Srivastava, Ritika Brahma, Vijaya Verma, Lata Karthikeyan, Subramanian Sahni, Girish |
author_sort | Garg, Roma |
collection | PubMed |
description | Cellulase catalyzes the hydrolysis of β-1,4-linkages of cellulose to produce industrially relevant monomeric subunits. Cellulases find their applications in pulp and paper, laundry, food and feed, textile, brewing industry and in biofuel production. These industries always have great demand for cellulases that can work efficiently even in harsh conditions such as high salt, heat, and acidic environments. While, cellulases with high thermal and acidic stability are already in use, existence of a high halotolerant cellulase is still elusive. Here, we report a novel cellulase Cel5R, obtained from soil metagenome that shows high halotolerance and thermal stability. The biochemical and functional characterization of Cel5R revealed its endoglucanase activity and high halostability. In addition, the crystal structure of Cel5R determined at 2.2 Å resolution reveals a large number of acidic residues on the surface of the protein that contribute to the halophilic nature of this enzyme. Moreover, we demonstrate that the four free and non-conserved cysteine residues (C65, C90, C231 and C273) contributes to the thermal stability of Cel5R by alanine scanning experiments. Thus, the newly identified endoglucanase Cel5R is a promising candidate for various industrial applications. |
format | Online Article Text |
id | pubmed-5180356 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-51803562016-12-29 Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome Garg, Roma Srivastava, Ritika Brahma, Vijaya Verma, Lata Karthikeyan, Subramanian Sahni, Girish Sci Rep Article Cellulase catalyzes the hydrolysis of β-1,4-linkages of cellulose to produce industrially relevant monomeric subunits. Cellulases find their applications in pulp and paper, laundry, food and feed, textile, brewing industry and in biofuel production. These industries always have great demand for cellulases that can work efficiently even in harsh conditions such as high salt, heat, and acidic environments. While, cellulases with high thermal and acidic stability are already in use, existence of a high halotolerant cellulase is still elusive. Here, we report a novel cellulase Cel5R, obtained from soil metagenome that shows high halotolerance and thermal stability. The biochemical and functional characterization of Cel5R revealed its endoglucanase activity and high halostability. In addition, the crystal structure of Cel5R determined at 2.2 Å resolution reveals a large number of acidic residues on the surface of the protein that contribute to the halophilic nature of this enzyme. Moreover, we demonstrate that the four free and non-conserved cysteine residues (C65, C90, C231 and C273) contributes to the thermal stability of Cel5R by alanine scanning experiments. Thus, the newly identified endoglucanase Cel5R is a promising candidate for various industrial applications. Nature Publishing Group 2016-12-23 /pmc/articles/PMC5180356/ /pubmed/28008971 http://dx.doi.org/10.1038/srep39634 Text en Copyright © 2016, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Garg, Roma Srivastava, Ritika Brahma, Vijaya Verma, Lata Karthikeyan, Subramanian Sahni, Girish Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
title | Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
title_full | Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
title_fullStr | Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
title_full_unstemmed | Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
title_short | Biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
title_sort | biochemical and structural characterization of a novel halotolerant cellulase from soil metagenome |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5180356/ https://www.ncbi.nlm.nih.gov/pubmed/28008971 http://dx.doi.org/10.1038/srep39634 |
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