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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ftdoajarticles:oai:doaj.org/article:33a2437ba5f14182957df1eedbc39327 2023-10-01T03:51:58+02:00 Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome Moreno Galleni Pablo Power Jacques Georis Fabienne Verté Marcello La Salla Maud Delsaute Olivier Jacquin Renaud Berlemont 2013-01-01T00:00:00Z https://doi.org/10.3390/biology2010177 https://doaj.org/article/33a2437ba5f14182957df1eedbc39327 EN eng MDPI AG http://www.mdpi.com/2079-7737/2/1/177 https://doaj.org/toc/2079-7737 doi:10.3390/biology2010177 2079-7737 https://doaj.org/article/33a2437ba5f14182957df1eedbc39327 Biology, Vol 2, Iss 1, Pp 177-188 (2013) α/b hydrolase lipolytic enzymes metagenomics p-nitrophenyl-ester cold-adaptation Biology (General) QH301-705.5 article 2013 ftdoajarticles https://doi.org/10.3390/biology2010177 2023-09-03T00:34:41Z 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. Article in Journal/Newspaper Antarc* Antarctic Directory of Open Access Journals: DOAJ Articles Antarctic Biology 2 1 177 188 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
α/b hydrolase lipolytic enzymes metagenomics p-nitrophenyl-ester cold-adaptation Biology (General) QH301-705.5 |
spellingShingle |
α/b hydrolase lipolytic enzymes metagenomics p-nitrophenyl-ester cold-adaptation Biology (General) QH301-705.5 Moreno Galleni Pablo Power Jacques Georis Fabienne Verté Marcello La Salla Maud Delsaute Olivier Jacquin Renaud Berlemont Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome |
topic_facet |
α/b hydrolase lipolytic enzymes metagenomics p-nitrophenyl-ester cold-adaptation Biology (General) QH301-705.5 |
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 |
Article in Journal/Newspaper |
author |
Moreno Galleni Pablo Power Jacques Georis Fabienne Verté Marcello La Salla Maud Delsaute Olivier Jacquin Renaud Berlemont |
author_facet |
Moreno Galleni Pablo Power Jacques Georis Fabienne Verté Marcello La Salla Maud Delsaute Olivier Jacquin Renaud Berlemont |
author_sort |
Moreno Galleni |
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 |
MDPI AG |
publishDate |
2013 |
url |
https://doi.org/10.3390/biology2010177 https://doaj.org/article/33a2437ba5f14182957df1eedbc39327 |
geographic |
Antarctic |
geographic_facet |
Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Biology, Vol 2, Iss 1, Pp 177-188 (2013) |
op_relation |
http://www.mdpi.com/2079-7737/2/1/177 https://doaj.org/toc/2079-7737 doi:10.3390/biology2010177 2079-7737 https://doaj.org/article/33a2437ba5f14182957df1eedbc39327 |
op_doi |
https://doi.org/10.3390/biology2010177 |
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Biology |
container_volume |
2 |
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1 |
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177 |
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188 |
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1778517367986323456 |