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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 α/β hydrolase family 6, named MHlip. This enzyme is related to hypothetical genes coding esterases, aryl-esterases and peroxydases, among others. MHlip was prod...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2013
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4009859/ https://www.ncbi.nlm.nih.gov/pubmed/24832657 http://dx.doi.org/10.3390/biology2010177 |
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author | Berlemont, Renaud Jacquin, Olivier Delsaute, Maud Salla, Marcello La Georis, Jacques Verté, Fabienne Galleni, Moreno Power, Pablo |
author_facet | Berlemont, Renaud Jacquin, Olivier Delsaute, Maud Salla, Marcello La Georis, Jacques Verté, Fabienne Galleni, Moreno Power, Pablo |
author_sort | Berlemont, Renaud |
collection | PubMed |
description | An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the α/β 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/β hydrolases. |
format | Online Article Text |
id | pubmed-4009859 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-40098592014-05-07 Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome Berlemont, Renaud Jacquin, Olivier Delsaute, Maud Salla, Marcello La Georis, Jacques Verté, Fabienne Galleni, Moreno Power, Pablo Biology (Basel) Article An Antarctic soil metagenomic library was screened for lipolytic enzymes and allowed for the isolation of a new cytosolic esterase from the α/β 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/β hydrolases. MDPI 2013-01-25 /pmc/articles/PMC4009859/ /pubmed/24832657 http://dx.doi.org/10.3390/biology2010177 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
spellingShingle | Article Berlemont, Renaud Jacquin, Olivier Delsaute, Maud Salla, Marcello La Georis, Jacques Verté, Fabienne Galleni, Moreno Power, Pablo Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome |
title | 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_short | Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome |
title_sort | novel cold-adapted esterase mhlip from an antarctic soil metagenome |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4009859/ https://www.ncbi.nlm.nih.gov/pubmed/24832657 http://dx.doi.org/10.3390/biology2010177 |
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