Insights into bacterial cellulose biosynthesis by functional metagenomics on Antarctic soil samples.
peer reviewed 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 stutzer...
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ftorbi:oai:orbi.ulg.ac.be:2268/15202 2024-10-13T14:02:43+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 https://orbi.uliege.be/handle/2268/15202 https://orbi.uliege.be/bitstream/2268/15202/1/ISMEJ_2009_Berlemont.pdf https://doi.org/10.1038/ismej.2009.48 en eng Nature Publishing Group urn:issn:1751-7362 urn:issn:1751-7370 https://orbi.uliege.be/handle/2268/15202 info:hdl:2268/15202 https://orbi.uliege.be/bitstream/2268/15202/1/ISMEJ_2009_Berlemont.pdf doi:10.1038/ismej.2009.48 info:pmid:19458657 open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess ISME Journal, 3 (9), 1070-1081 (2009) Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire journal article http://purl.org/coar/resource_type/c_6501 info:eu-repo/semantics/article peer reviewed 2009 ftorbi https://doi.org/10.1038/ismej.2009.48 2024-09-27T07:02:04Z peer reviewed 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 degrees 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.The ISME Journal advance online publication, 21 May 2009; doi:10.1038/ismej.2009.48. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Antarctic The ISME Journal 3 9 1070 1081 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
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ftorbi |
language |
English |
topic |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
spellingShingle |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire 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. |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed 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 degrees 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.The ISME Journal advance online publication, 21 May 2009; doi:10.1038/ismej.2009.48. |
format |
Article in Journal/Newspaper |
author |
Berlemont, Renaud Delsaute, Maud Pipers, Delphine D'Amico, Salvino Feller, Georges Galleni, Moreno Power, Pablo |
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 |
Nature Publishing Group |
publishDate |
2009 |
url |
https://orbi.uliege.be/handle/2268/15202 https://orbi.uliege.be/bitstream/2268/15202/1/ISMEJ_2009_Berlemont.pdf https://doi.org/10.1038/ismej.2009.48 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
ISME Journal, 3 (9), 1070-1081 (2009) |
op_relation |
urn:issn:1751-7362 urn:issn:1751-7370 https://orbi.uliege.be/handle/2268/15202 info:hdl:2268/15202 https://orbi.uliege.be/bitstream/2268/15202/1/ISMEJ_2009_Berlemont.pdf doi:10.1038/ismej.2009.48 info:pmid:19458657 |
op_rights |
open access http://purl.org/coar/access_right/c_abf2 info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1038/ismej.2009.48 |
container_title |
The ISME Journal |
container_volume |
3 |
container_issue |
9 |
container_start_page |
1070 |
op_container_end_page |
1081 |
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1812819194053394432 |