Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome.
peer reviewed An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the a/b hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others....
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2013
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Online Access: | https://orbi.uliege.be/handle/2268/188993 https://doi.org/10.3390/biology2010177 |
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ftorbi:oai:orbi.ulg.ac.be:2268/188993 2024-04-21T07:52:29+00:00 Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. Berlemont, Renaud Jacquin, Olivier Delsaute, Maud La Salla, Marcello Georis, Jacques Verte, Fabienne Galleni, Moreno Power, Pablo 2013 https://orbi.uliege.be/handle/2268/188993 https://doi.org/10.3390/biology2010177 en eng Multidisciplinary Digital Publishing Institute (MDPI) urn:issn:2079-7737 https://orbi.uliege.be/handle/2268/188993 info:hdl:2268/188993 doi:10.3390/biology2010177 scopus-id:2-s2.0-84893084992 info:pmid:24832657 restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess Biology, 2 (1), 177-88 (2013) 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 2013 ftorbi https://doi.org/10.3390/biology2010177 2024-03-27T14:53:38Z peer reviewed An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the a/b hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others. MHlip was produced, purified and its activity was determined. The substrate profile of MHlip reveals a high specificity for short p-nitrophenyl-esters. The apparent optimal activity of MHlip was measured for p-nitrophenyl-acetate, at 33 degrees C, in the pH range of 6-9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 degrees C. The biochemical characterization of this enzyme showed its adaptation to cold temperatures, even when it did not present evident signatures associated with cold-adapted proteins. Thus, MHlip adaptation to cold probably results from many discrete structural modifications, allowing the protein to remain active at low temperatures. Functional metagenomics is a powerful approach to isolate new enzymes with tailored biophysical properties (e.g., cold adaptation). In addition, beside the ever growing amount of sequenced DNA, the functional characterization of new catalysts derived from environment is still required, especially for poorly characterized protein families like alpha/b hydrolases. Article in Journal/Newspaper Antarc* Antarctic University of Liège: ORBi (Open Repository and Bibliography) Biology 2 1 177 188 |
institution |
Open Polar |
collection |
University of Liège: ORBi (Open Repository and Bibliography) |
op_collection_id |
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 Jacquin, Olivier Delsaute, Maud La Salla, Marcello Georis, Jacques Verte, Fabienne Galleni, Moreno Power, Pablo Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. |
topic_facet |
Life sciences Biochemistry biophysics & molecular biology Sciences du vivant Biochimie biophysique & biologie moléculaire |
description |
peer reviewed An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the a/b hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others. MHlip was produced, purified and its activity was determined. The substrate profile of MHlip reveals a high specificity for short p-nitrophenyl-esters. The apparent optimal activity of MHlip was measured for p-nitrophenyl-acetate, at 33 degrees C, in the pH range of 6-9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 degrees C. The biochemical characterization of this enzyme showed its adaptation to cold temperatures, even when it did not present evident signatures associated with cold-adapted proteins. Thus, MHlip adaptation to cold probably results from many discrete structural modifications, allowing the protein to remain active at low temperatures. Functional metagenomics is a powerful approach to isolate new enzymes with tailored biophysical properties (e.g., cold adaptation). In addition, beside the ever growing amount of sequenced DNA, the functional characterization of new catalysts derived from environment is still required, especially for poorly characterized protein families like alpha/b hydrolases. |
format |
Article in Journal/Newspaper |
author |
Berlemont, Renaud Jacquin, Olivier Delsaute, Maud La Salla, Marcello Georis, Jacques Verte, Fabienne Galleni, Moreno Power, Pablo |
author_facet |
Berlemont, Renaud Jacquin, Olivier Delsaute, Maud La Salla, Marcello Georis, Jacques Verte, Fabienne Galleni, Moreno Power, Pablo |
author_sort |
Berlemont, Renaud |
title |
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. |
title_short |
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. |
title_full |
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. |
title_fullStr |
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. |
title_full_unstemmed |
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome. |
title_sort |
novel cold-adapted esterase mhlip from an antarctic soil metagenome. |
publisher |
Multidisciplinary Digital Publishing Institute (MDPI) |
publishDate |
2013 |
url |
https://orbi.uliege.be/handle/2268/188993 https://doi.org/10.3390/biology2010177 |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biology, 2 (1), 177-88 (2013) |
op_relation |
urn:issn:2079-7737 https://orbi.uliege.be/handle/2268/188993 info:hdl:2268/188993 doi:10.3390/biology2010177 scopus-id:2-s2.0-84893084992 info:pmid:24832657 |
op_rights |
restricted access http://purl.org/coar/access_right/c_16ec info:eu-repo/semantics/restrictedAccess |
op_doi |
https://doi.org/10.3390/biology2010177 |
container_title |
Biology |
container_volume |
2 |
container_issue |
1 |
container_start_page |
177 |
op_container_end_page |
188 |
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1796935712023511040 |