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Characterization of a thermostable endoglucanase produced by Isoptericola variabilis sp. IDAH9
This study aimed to isolate and evaluate the cellulase activity of cellulolytic bacteria in hot springs of Dehloran, Ilam province, Iran. Water and sludge samples were collected from the hot springs and the bacterial enrichment was performed in a medium containing rice barn and carboxymethyl cellulo...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Sociedade Brasileira de Microbiologia
2015
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4704623/ https://www.ncbi.nlm.nih.gov/pubmed/26691485 http://dx.doi.org/10.1590/S1517-838246420140846 |
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author | Azizi, Maryam Hemmat, Jafar Seifati, Seyed Morteza Torktaz, Ibrahim Karimi, Soodabeh |
author_facet | Azizi, Maryam Hemmat, Jafar Seifati, Seyed Morteza Torktaz, Ibrahim Karimi, Soodabeh |
author_sort | Azizi, Maryam |
collection | PubMed |
description | This study aimed to isolate and evaluate the cellulase activity of cellulolytic bacteria in hot springs of Dehloran, Ilam province, Iran. Water and sludge samples were collected from the hot springs and the bacterial enrichment was performed in a medium containing rice barn and carboxymethyl cellulose (CMC). The cultures were incubated at 50 °C in aerobic conditions. The bacteria were isolated on CMC agar (1%) medium. Cellulase assay of the isolates was measured by the evaluation of endoglucanase enzyme activity, which is also called as carboxymethyl cellulase (CMCase). The isolated thermotolerant bacteria were then identified and optimized for the production of CMCase. Moreover, stabilizing elements of the enzyme were identified with in silico approach. The chosen isolate was identified as Isoptericola variabilis sp. IDAH9. The identified strain produced the most thermostable CMCase at a concentration of 5.6 g/L of ammonium sulfate, 9 g/L CMCase or 12 g/L rice bran, 0/6% Tween-80, and 0.2% sucrose. The produced enzyme showed 80% of the residual activity after 1 h of incubation at 65 °C. In silico data indicated that the remaining residual activity was due to the redundant stabilizing elements in the protein structure. Consequently, I. variabilis can be isolated from the extreme environment and has a thermostable endoglucanase which may be used for various applications after studying them. |
format | Online Article Text |
id | pubmed-4704623 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2015 |
publisher | Sociedade Brasileira de Microbiologia |
record_format | MEDLINE/PubMed |
spelling | pubmed-47046232016-01-14 Characterization of a thermostable endoglucanase produced by Isoptericola variabilis sp. IDAH9 Azizi, Maryam Hemmat, Jafar Seifati, Seyed Morteza Torktaz, Ibrahim Karimi, Soodabeh Braz J Microbiol Industrial Microbiology This study aimed to isolate and evaluate the cellulase activity of cellulolytic bacteria in hot springs of Dehloran, Ilam province, Iran. Water and sludge samples were collected from the hot springs and the bacterial enrichment was performed in a medium containing rice barn and carboxymethyl cellulose (CMC). The cultures were incubated at 50 °C in aerobic conditions. The bacteria were isolated on CMC agar (1%) medium. Cellulase assay of the isolates was measured by the evaluation of endoglucanase enzyme activity, which is also called as carboxymethyl cellulase (CMCase). The isolated thermotolerant bacteria were then identified and optimized for the production of CMCase. Moreover, stabilizing elements of the enzyme were identified with in silico approach. The chosen isolate was identified as Isoptericola variabilis sp. IDAH9. The identified strain produced the most thermostable CMCase at a concentration of 5.6 g/L of ammonium sulfate, 9 g/L CMCase or 12 g/L rice bran, 0/6% Tween-80, and 0.2% sucrose. The produced enzyme showed 80% of the residual activity after 1 h of incubation at 65 °C. In silico data indicated that the remaining residual activity was due to the redundant stabilizing elements in the protein structure. Consequently, I. variabilis can be isolated from the extreme environment and has a thermostable endoglucanase which may be used for various applications after studying them. Sociedade Brasileira de Microbiologia 2015-12-01 /pmc/articles/PMC4704623/ /pubmed/26691485 http://dx.doi.org/10.1590/S1517-838246420140846 Text en Copyright © 2015, Sociedade Brasileira de Microbiologia http://creativecommons.org/licenses/by-nc/4.0/ All the content of the journal, except where otherwise noted, is licensed under a Creative Commons License CC BY-NC. |
spellingShingle | Industrial Microbiology Azizi, Maryam Hemmat, Jafar Seifati, Seyed Morteza Torktaz, Ibrahim Karimi, Soodabeh Characterization of a thermostable endoglucanase produced by Isoptericola variabilis sp. IDAH9 |
title | Characterization of a thermostable endoglucanase produced by
Isoptericola variabilis sp. IDAH9 |
title_full | Characterization of a thermostable endoglucanase produced by
Isoptericola variabilis sp. IDAH9 |
title_fullStr | Characterization of a thermostable endoglucanase produced by
Isoptericola variabilis sp. IDAH9 |
title_full_unstemmed | Characterization of a thermostable endoglucanase produced by
Isoptericola variabilis sp. IDAH9 |
title_short | Characterization of a thermostable endoglucanase produced by
Isoptericola variabilis sp. IDAH9 |
title_sort | characterization of a thermostable endoglucanase produced by
isoptericola variabilis sp. idah9 |
topic | Industrial Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4704623/ https://www.ncbi.nlm.nih.gov/pubmed/26691485 http://dx.doi.org/10.1590/S1517-838246420140846 |
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