Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome

Autores
Berlemont, Renaud; Jacquin, Olivier; Delsaute, Maud; La Salla, Marcello; Georis, Jacques; Verté, Fabienne; Galleni, Moreno; Power, Pablo
Año de publicación
2013
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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
Fil: Berlemont, Renaud. Universite de Liege; Bélgica. University Of California At Irvine; Estados Unidos
Fil: Jacquin, Olivier. Universite de Liege; Bélgica
Fil: Delsaute, Maud. Universite de Liege; Bélgica
Fil: La Salla, Marcello. Universite de Liege; Bélgica
Fil: Georis, Jacques. Puratos Group; Bélgica
Fil: Verté, Fabienne. Puratos Group; Bélgica
Fil: Galleni, Moreno. Universite de Liege; Bélgica
Fil: Power, Pablo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Universite de Liege; Bélgica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
A/B Hydrolase
Lipolytic Enzymes
Metagenomics
Cold-Adaptation
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/12871
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/12871
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novel Cold-Adapted Esterase MHlip from an Antarctic Soil MetagenomeBerlemont, RenaudJacquin, OlivierDelsaute, MaudLa Salla, MarcelloGeoris, JacquesVerté, FabienneGalleni, MorenoPower, PabloA/B HydrolaseLipolytic EnzymesMetagenomicsCold-Adaptationhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1An 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 hydrolasesFil: Berlemont, Renaud. Universite de Liege; Bélgica. University Of California At Irvine; Estados UnidosFil: Jacquin, Olivier. Universite de Liege; BélgicaFil: Delsaute, Maud. Universite de Liege; BélgicaFil: La Salla, Marcello. Universite de Liege; BélgicaFil: Georis, Jacques. Puratos Group; BélgicaFil: Verté, Fabienne. Puratos Group; BélgicaFil: Galleni, Moreno. Universite de Liege; BélgicaFil: Power, Pablo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Universite de Liege; Bélgica. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaMolecular Diversity Preservation International2013-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/12871Berlemont, Renaud; Jacquin, Olivier; Delsaute, Maud; La Salla, Marcello; Georis, Jacques; et al.; Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome; Molecular Diversity Preservation International; Biology; 2; 1; 1-2013; 177-1882079-7737enginfo:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/2079-7737/2/1/177info:eu-repo/semantics/altIdentifier/doi/10.3390/biology2010177info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:41:53Zoai:ri.conicet.gov.ar:11336/12871instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-29 10:41:53.821CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome
title Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome
spellingShingle Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome
Berlemont, Renaud
A/B Hydrolase
Lipolytic Enzymes
Metagenomics
Cold-Adaptation
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
dc.creator.none.fl_str_mv Berlemont, Renaud
Jacquin, Olivier
Delsaute, Maud
La Salla, Marcello
Georis, Jacques
Verté, Fabienne
Galleni, Moreno
Power, Pablo
author Berlemont, Renaud
author_facet Berlemont, Renaud
Jacquin, Olivier
Delsaute, Maud
La Salla, Marcello
Georis, Jacques
Verté, Fabienne
Galleni, Moreno
Power, Pablo
author_role author
author2 Jacquin, Olivier
Delsaute, Maud
La Salla, Marcello
Georis, Jacques
Verté, Fabienne
Galleni, Moreno
Power, Pablo
author2_role author
author
author
author
author
author
author
dc.subject.none.fl_str_mv A/B Hydrolase
Lipolytic Enzymes
Metagenomics
Cold-Adaptation
topic A/B Hydrolase
Lipolytic Enzymes
Metagenomics
Cold-Adaptation
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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
Fil: Berlemont, Renaud. Universite de Liege; Bélgica. University Of California At Irvine; Estados Unidos
Fil: Jacquin, Olivier. Universite de Liege; Bélgica
Fil: Delsaute, Maud. Universite de Liege; Bélgica
Fil: La Salla, Marcello. Universite de Liege; Bélgica
Fil: Georis, Jacques. Puratos Group; Bélgica
Fil: Verté, Fabienne. Puratos Group; Bélgica
Fil: Galleni, Moreno. Universite de Liege; Bélgica
Fil: Power, Pablo. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica; Argentina. Universite de Liege; Bélgica. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
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
publishDate 2013
dc.date.none.fl_str_mv 2013-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/12871
Berlemont, Renaud; Jacquin, Olivier; Delsaute, Maud; La Salla, Marcello; Georis, Jacques; et al.; Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome; Molecular Diversity Preservation International; Biology; 2; 1; 1-2013; 177-188
2079-7737
url http://hdl.handle.net/11336/12871
identifier_str_mv Berlemont, Renaud; Jacquin, Olivier; Delsaute, Maud; La Salla, Marcello; Georis, Jacques; et al.; Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome; Molecular Diversity Preservation International; Biology; 2; 1; 1-2013; 177-188
2079-7737
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/2079-7737/2/1/177
info:eu-repo/semantics/altIdentifier/doi/10.3390/biology2010177
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Molecular Diversity Preservation International
publisher.none.fl_str_mv Molecular Diversity Preservation International
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1844614450780307456
score 13.070432

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