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dc.contributor.author
Berlemont, Renaud  
dc.contributor.author
Jacquin, Olivier  
dc.contributor.author
Delsaute, Maud  
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La Salla, Marcello  
dc.contributor.author
Georis, Jacques  
dc.contributor.author
Verté, Fabienne  
dc.contributor.author
Galleni, Moreno  
dc.contributor.author
Power, Pablo  
dc.date.available
2017-02-10T19:29:34Z  
dc.date.issued
2013-01  
dc.identifier.citation
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  
dc.identifier.issn
2079-7737  
dc.identifier.uri
http://hdl.handle.net/11336/12871  
dc.description.abstract
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  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Molecular Diversity Preservation International  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
A/B Hydrolase  
dc.subject
Lipolytic Enzymes  
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Metagenomics  
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Cold-Adaptation  
dc.subject.classification
Bioquímica y Biología Molecular  
dc.subject.classification
Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Novel Cold-Adapted Esterase MHlip from an Antarctic Soil Metagenome  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2017-02-09T18:22:46Z  
dc.journal.volume
2  
dc.journal.number
1  
dc.journal.pagination
177-188  
dc.journal.pais
Suiza  
dc.journal.ciudad
Basel  
dc.description.fil
Fil: Berlemont, Renaud. Universite de Liege; Bélgica. University Of California At Irvine; Estados Unidos  
dc.description.fil
Fil: Jacquin, Olivier. Universite de Liege; Bélgica  
dc.description.fil
Fil: Delsaute, Maud. Universite de Liege; Bélgica  
dc.description.fil
Fil: La Salla, Marcello. Universite de Liege; Bélgica  
dc.description.fil
Fil: Georis, Jacques. Puratos Group; Bélgica  
dc.description.fil
Fil: Verté, Fabienne. Puratos Group; Bélgica  
dc.description.fil
Fil: Galleni, Moreno. Universite de Liege; Bélgica  
dc.description.fil
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  
dc.journal.title
Biology  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.mdpi.com/2079-7737/2/1/177  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/biology2010177