PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization
Abstract Cold-adapted proteases have been found to be the dominant activity throughout the cold marine environment, indicating their importance in bacterial acquisition of nitrogen-rich complex organic compounds. However, few extracellular proteases from marine organisms have been characterized so f...
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ftopenaccessrep:oai:zenodo.org:87191 2023-10-25T01:32:07+02:00 PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization Andrea Carpentieri C. De Santi N. Bergamasco Maria Giuliani Angela Amoresano Ermenegilda Parrilli Donatella de Pascale Maria Luisa Tutino 2010-08-01 https://www.openaccessrepository.it/record/87191 https://doi.org/10.1016/j.polar.2010.03.009 eng eng url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/87191 doi:10.1016/j.polar.2010.03.009 info:eu-repo/semantics/openAccess Aurora Universities Network General Earth and Planetary Sciences Ecology Aquatic Science Evolution Behavior and Systematics info:eu-repo/semantics/article publication-article 2010 ftopenaccessrep https://doi.org/10.1016/j.polar.2010.03.009 2023-09-26T22:18:08Z Abstract Cold-adapted proteases have been found to be the dominant activity throughout the cold marine environment, indicating their importance in bacterial acquisition of nitrogen-rich complex organic compounds. However, few extracellular proteases from marine organisms have been characterized so far, and the mechanisms that enable their activity in situ are still largely unknown. Aside from their ecological importance and use as model enzyme for structure/function investigations, cold-active proteolytic enzymes offer great potential for biotechnological applications. Our studies on cold adapted proteases were performed on exo-enzyme produced by the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. By applying a proteomic approach, we identified several proteolytic activities from its culture supernatant. PhAP protease was selected for further investigations. The encoding gene was cloned and the protein was recombinantly produced in E. coli cells. The homogeneous product was biochemically characterised and it turned out that the enzyme is a Zn-dependent aminopeptidase, with an activity dependence from assay temperature typical of psychrophilic enzymes. Article in Journal/Newspaper Antarc* Antarctic Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository Antarctic The Antarctic Polar Science 4 2 285 294 |
institution |
Open Polar |
collection |
Istituto Nazionale di Fisica Nucleare (INFN): Open Access Repository |
op_collection_id |
ftopenaccessrep |
language |
English |
topic |
Aurora Universities Network General Earth and Planetary Sciences Ecology Aquatic Science Evolution Behavior and Systematics |
spellingShingle |
Aurora Universities Network General Earth and Planetary Sciences Ecology Aquatic Science Evolution Behavior and Systematics Andrea Carpentieri C. De Santi N. Bergamasco Maria Giuliani Angela Amoresano Ermenegilda Parrilli Donatella de Pascale Maria Luisa Tutino PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization |
topic_facet |
Aurora Universities Network General Earth and Planetary Sciences Ecology Aquatic Science Evolution Behavior and Systematics |
description |
Abstract Cold-adapted proteases have been found to be the dominant activity throughout the cold marine environment, indicating their importance in bacterial acquisition of nitrogen-rich complex organic compounds. However, few extracellular proteases from marine organisms have been characterized so far, and the mechanisms that enable their activity in situ are still largely unknown. Aside from their ecological importance and use as model enzyme for structure/function investigations, cold-active proteolytic enzymes offer great potential for biotechnological applications. Our studies on cold adapted proteases were performed on exo-enzyme produced by the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125. By applying a proteomic approach, we identified several proteolytic activities from its culture supernatant. PhAP protease was selected for further investigations. The encoding gene was cloned and the protein was recombinantly produced in E. coli cells. The homogeneous product was biochemically characterised and it turned out that the enzyme is a Zn-dependent aminopeptidase, with an activity dependence from assay temperature typical of psychrophilic enzymes. |
format |
Article in Journal/Newspaper |
author |
Andrea Carpentieri C. De Santi N. Bergamasco Maria Giuliani Angela Amoresano Ermenegilda Parrilli Donatella de Pascale Maria Luisa Tutino |
author_facet |
Andrea Carpentieri C. De Santi N. Bergamasco Maria Giuliani Angela Amoresano Ermenegilda Parrilli Donatella de Pascale Maria Luisa Tutino |
author_sort |
Andrea Carpentieri |
title |
PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization |
title_short |
PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization |
title_full |
PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization |
title_fullStr |
PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization |
title_full_unstemmed |
PhAP protease from Pseudoalteromonas haloplanktis TAC125: Gene cloning, recombinant production in E. coli and enzyme characterization |
title_sort |
phap protease from pseudoalteromonas haloplanktis tac125: gene cloning, recombinant production in e. coli and enzyme characterization |
publishDate |
2010 |
url |
https://www.openaccessrepository.it/record/87191 https://doi.org/10.1016/j.polar.2010.03.009 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_relation |
url:https://www.openaccessrepository.it/communities/itmirror https://www.openaccessrepository.it/record/87191 doi:10.1016/j.polar.2010.03.009 |
op_rights |
info:eu-repo/semantics/openAccess |
op_doi |
https://doi.org/10.1016/j.polar.2010.03.009 |
container_title |
Polar Science |
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4 |
container_issue |
2 |
container_start_page |
285 |
op_container_end_page |
294 |
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1780727690152640512 |