Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome
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 prod...
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ftmdpi:oai:mdpi.com:/2079-7737/2/1/177/ 2023-08-20T04:01:02+02:00 Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome Renaud Berlemont Olivier Jacquin Maud Delsaute Marcello La Salla Jacques Georis Fabienne Verté Moreno Galleni Pablo Power agris 2013-01-25 application/pdf https://doi.org/10.3390/biology2010177 EN eng Multidisciplinary Digital Publishing Institute https://dx.doi.org/10.3390/biology2010177 https://creativecommons.org/licenses/by/3.0/ Biology; Volume 2; Issue 1; Pages: 177-188 α/b hydrolase lipolytic enzymes metagenomics p -nitrophenyl-ester cold-adaptation Text 2013 ftmdpi https://doi.org/10.3390/biology2010177 2023-07-31T20:31:24Z 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 °C, in the pH range of 6–9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 °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 α/b hydrolases. Text Antarc* Antarctic MDPI Open Access Publishing Antarctic Biology 2 1 177 188 |
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Open Polar |
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MDPI Open Access Publishing |
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ftmdpi |
language |
English |
topic |
α/b hydrolase lipolytic enzymes metagenomics p -nitrophenyl-ester cold-adaptation |
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α/b hydrolase lipolytic enzymes metagenomics p -nitrophenyl-ester cold-adaptation Renaud Berlemont Olivier Jacquin Maud Delsaute Marcello La Salla Jacques Georis Fabienne Verté Moreno Galleni Pablo Power Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome |
topic_facet |
α/b hydrolase lipolytic enzymes metagenomics p -nitrophenyl-ester cold-adaptation |
description |
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 °C, in the pH range of 6–9. The MHlip thermal unfolding was investigated by spectrophotometric methods, highlighting a transition (Tm) at 50 °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 α/b hydrolases. |
format |
Text |
author |
Renaud Berlemont Olivier Jacquin Maud Delsaute Marcello La Salla Jacques Georis Fabienne Verté Moreno Galleni Pablo Power |
author_facet |
Renaud Berlemont Olivier Jacquin Maud Delsaute Marcello La Salla Jacques Georis Fabienne Verté Moreno Galleni Pablo Power |
author_sort |
Renaud Berlemont |
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 |
publishDate |
2013 |
url |
https://doi.org/10.3390/biology2010177 |
op_coverage |
agris |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biology; Volume 2; Issue 1; Pages: 177-188 |
op_relation |
https://dx.doi.org/10.3390/biology2010177 |
op_rights |
https://creativecommons.org/licenses/by/3.0/ |
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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1774722176606273536 |