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Authordc.contributor.authorAcevedo, J. P. 
Authordc.contributor.authorRodríguez, V. es_CL
Authordc.contributor.authorSaavedra, M. es_CL
Authordc.contributor.authorMuñoz, M. es_CL
Authordc.contributor.authorSalazar, O. es_CL
Authordc.contributor.authorAsenjo de Leuze, Juan es_CL
Authordc.contributor.authorAndrews Farrow, Bárbara es_CL
Cita de ítemdc.identifier.citationJournal of Applied Microbiology 114, 352--363en_US
General notedc.descriptionArtículo de publicación ISIen_US
Abstractdc.description.abstractAims: Cloning, expression and characterization of a new cold-adapted protease with potential biotechnological application, isolated from Antarctic bacteria. Method and Results: A subtilisin-like gene was isolated from several Antarctic bacterial genus using CODPEHOP-designed primers and a genome walking method. This gene encodes a precursor protein, which undergoes an autocatalytic cleavage resulting in a 34 6 kDa active cold-adapted protease with a maximum activity at 25–35°C and optimum pH of 8 0–9 0. It showed a higher catalytic efficiency at lower temperatures compared to its mesophilic counterpart. Heat-induced inactivation resulted in a very low melting point. Local packing analysis using the homology model indicated Ala284 as an important cold-adaptation determinant, which was corroborated by the sitedirected mutagenesis. Conclusions: A new thermolabile subtilisin-like protease has been successfully cloned and analysed, and an important hot spot in the evolution of the cold adaptation and substrate specificity of this enzyme was identified and tested. Significance and Impact of the Study: This work reports a new cold-adapted protease with a vast representation amongst Antarctic genus, suggesting therefore its evolutionary success in this cold environment. Likewise, important sites for genetic potentiation have been identified, which are extrapolated to other enzymes of the same kind.en_US
Type of licensedc.rightsAttribution-NonCommercial-NoDerivs 3.0 Chile*
Link to Licensedc.rights.uri*
Keywordsdc.subjectcold adaptionen_US
Títulodc.titleCloning, expression and decoding of the cold adaptation of a new widely represented thermolabile subtilisin-like proteaseen_US
Document typedc.typeArtículo de revista

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Attribution-NonCommercial-NoDerivs 3.0 Chile
Except where otherwise noted, this item's license is described as Attribution-NonCommercial-NoDerivs 3.0 Chile