Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples
Abstract In this study, the mining of an Antarctic soil sample by functional metagenomics allowed the isolation of a cold-adapted protein (RBcel1) that hydrolyzes only carboxymethyl cellulose. The new enzyme is related to family 5 of the glycosyl hydrolase (GH5) protein from Pseudomonas stutzeri (Ps...
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Oxford University Press (OUP)
2009
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croxfordunivpr:10.1038/ismej.2009.48 2024-06-23T07:47:07+00:00 Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples Berlemont, Renaud Delsaute, Maud Pipers, Delphine D'Amico, Salvino Feller, Georges Galleni, Moreno Power, Pablo 2009 http://dx.doi.org/10.1038/ismej.2009.48 http://www.nature.com/articles/ismej200948.pdf http://www.nature.com/articles/ismej200948 https://academic.oup.com/ismej/article-pdf/3/9/1070/56532716/41396_2009_article_bfismej200948.pdf en eng Oxford University Press (OUP) https://academic.oup.com/pages/standard-publication-reuse-rights The ISME Journal volume 3, issue 9, page 1070-1081 ISSN 1751-7362 1751-7370 journal-article 2009 croxfordunivpr https://doi.org/10.1038/ismej.2009.48 2024-06-04T06:09:35Z Abstract In this study, the mining of an Antarctic soil sample by functional metagenomics allowed the isolation of a cold-adapted protein (RBcel1) that hydrolyzes only carboxymethyl cellulose. The new enzyme is related to family 5 of the glycosyl hydrolase (GH5) protein from Pseudomonas stutzeri (Pst_2494) and does not possess a carbohydrate-binding domain. The protein was produced and purified to homogeneity. RBcel1 displayed an endoglucanase activity, producing cellobiose and cellotriose, using carboxymethyl cellulose as a substrate. Moreover, the study of pH and the thermal dependence of the hydrolytic activity shows that RBcel1 was active from pH 6 to pH 9 and remained significantly active when temperature decreased (18% of activity at 10 °C). It is interesting that RBcel1 was able to synthetize non-reticulated cellulose using cellobiose as a substrate. Moreover, by a combination of bioinformatics and enzyme analysis, the physiological relevance of the RBcel1 protein and its mesophilic homologous Pst_2494 protein from P. stutzeri, A1501, was established as the key enzymes involved in the production of cellulose by bacteria. In addition, RBcel1 and Pst_2494 are the two primary enzymes belonging to the GH5 family involved in this process. Article in Journal/Newspaper Antarc* Antarctic Oxford University Press Antarctic The ISME Journal 3 9 1070 1081 |
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Open Polar |
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Oxford University Press |
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croxfordunivpr |
language |
English |
description |
Abstract In this study, the mining of an Antarctic soil sample by functional metagenomics allowed the isolation of a cold-adapted protein (RBcel1) that hydrolyzes only carboxymethyl cellulose. The new enzyme is related to family 5 of the glycosyl hydrolase (GH5) protein from Pseudomonas stutzeri (Pst_2494) and does not possess a carbohydrate-binding domain. The protein was produced and purified to homogeneity. RBcel1 displayed an endoglucanase activity, producing cellobiose and cellotriose, using carboxymethyl cellulose as a substrate. Moreover, the study of pH and the thermal dependence of the hydrolytic activity shows that RBcel1 was active from pH 6 to pH 9 and remained significantly active when temperature decreased (18% of activity at 10 °C). It is interesting that RBcel1 was able to synthetize non-reticulated cellulose using cellobiose as a substrate. Moreover, by a combination of bioinformatics and enzyme analysis, the physiological relevance of the RBcel1 protein and its mesophilic homologous Pst_2494 protein from P. stutzeri, A1501, was established as the key enzymes involved in the production of cellulose by bacteria. In addition, RBcel1 and Pst_2494 are the two primary enzymes belonging to the GH5 family involved in this process. |
format |
Article in Journal/Newspaper |
author |
Berlemont, Renaud Delsaute, Maud Pipers, Delphine D'Amico, Salvino Feller, Georges Galleni, Moreno Power, Pablo |
spellingShingle |
Berlemont, Renaud Delsaute, Maud Pipers, Delphine D'Amico, Salvino Feller, Georges Galleni, Moreno Power, Pablo Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples |
author_facet |
Berlemont, Renaud Delsaute, Maud Pipers, Delphine D'Amico, Salvino Feller, Georges Galleni, Moreno Power, Pablo |
author_sort |
Berlemont, Renaud |
title |
Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples |
title_short |
Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples |
title_full |
Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples |
title_fullStr |
Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples |
title_full_unstemmed |
Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples |
title_sort |
insights into bacterial cellulose biosynthesis by functional metagenomics on antarctic soil samples |
publisher |
Oxford University Press (OUP) |
publishDate |
2009 |
url |
http://dx.doi.org/10.1038/ismej.2009.48 http://www.nature.com/articles/ismej200948.pdf http://www.nature.com/articles/ismej200948 https://academic.oup.com/ismej/article-pdf/3/9/1070/56532716/41396_2009_article_bfismej200948.pdf |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
The ISME Journal volume 3, issue 9, page 1070-1081 ISSN 1751-7362 1751-7370 |
op_rights |
https://academic.oup.com/pages/standard-publication-reuse-rights |
op_doi |
https://doi.org/10.1038/ismej.2009.48 |
container_title |
The ISME Journal |
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3 |
container_issue |
9 |
container_start_page |
1070 |
op_container_end_page |
1081 |
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1802651080975187968 |