Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate

Cold-adapted enzymes are generally derived from psychrophilic microorganisms and have features that make them very attractive for industrial and biotechnological purposes. In this work, we identified a 50 kDa extracellular protease (MP10) from the Antarctic isolate Pseudomonas sp. AU10. The enzyme w...

Full description

Saved in:
Bibliographic Details
Main Author: Fullana, Natalia (author)
Other Authors: Braña, Victoria (author), Marizcurrena, Juan José (author), Morales, Danilo (author), Betton, Jean-Michel (author), Marín Gutiérrez, Mónica (author), Castro-Sowinski, Susana (author)
Format: article
Language:English
Published: 2017
Subjects:
Online Access:https://hdl.handle.net/20.500.12008/22016
Tags: Add Tag
No Tags, Be the first to tag this record!
_version_ 1868890242386231296
author Fullana, Natalia
author2 Braña, Victoria
Marizcurrena, Juan José
Morales, Danilo
Betton, Jean-Michel
Marín Gutiérrez, Mónica
Castro-Sowinski, Susana
author2_role author
author
author
author
author
author
author_browse Betton, Jean-Michel
Braña, Victoria
Castro-Sowinski, Susana
Fullana, Natalia
Marizcurrena, Juan José
Marín Gutiérrez, Mónica
Morales, Danilo
author_facet Fullana, Natalia
Braña, Victoria
Marizcurrena, Juan José
Morales, Danilo
Betton, Jean-Michel
Marín Gutiérrez, Mónica
Castro-Sowinski, Susana
author_role author
collection COLIBRI
dc.contributor.none.fl_str_mv Fullana , Natalia. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología
Braña, Victoria. IIBCE
Marizcurrena, Juan José. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología
Morales, Danilo. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología
Marín Gutierrez, Mónica. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología
Castro-Sowinski, Susana. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología
dc.creator.none.fl_str_mv Fullana, Natalia
Braña, Victoria
Marizcurrena, Juan José
Morales, Danilo
Betton, Jean-Michel
Marín Gutiérrez, Mónica
Castro-Sowinski, Susana
dc.date.none.fl_str_mv 2017
2019-10-02T22:08:28Z
2019-10-02T22:08:28Z
20190930
dc.format.none.fl_str_mv application/pdf
dc.identifier.none.fl_str_mv Fullana, N., et al.Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate. AIMS Bioengineering, 2017, 4 (3): 386-401. doi: 10.3934/bioeng.2017.3.386
2375-1495
https://hdl.handle.net/20.500.12008/22016
10.3934/bioeng.2017.3.386
dc.language.none.fl_str_mv en
eng
dc.publisher.none.fl_str_mv AIMS Press
dc.relation.none.fl_str_mv AIMS Bioengineering, 2017, 4 (3): 386-401
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
Licencia Creative Commons Atribución (CC –BY 4.0)
dc.source.none.fl_str_mv reponame:COLIBRI
instname:Universidad de la República
instacron:Universidad de la República
dc.subject.none.fl_str_mv Protease
Pseudomonas
Cold-adaptation
Surfactant
Antarctica
dc.title.none.fl_str_mv Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
dc.type.none.fl_str_mv Artículo
info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
description Cold-adapted enzymes are generally derived from psychrophilic microorganisms and have features that make them very attractive for industrial and biotechnological purposes. In this work, we identified a 50 kDa extracellular protease (MP10) from the Antarctic isolate Pseudomonas sp. AU10. The enzyme was produced by recombinant DNA technology, purified using immobilized metal affinity chromatography and partially characterized. MP10 is an alkaline thermosensitive serine-metallo protease with optimal activity at pH 8.0 and 40 ℃, in the presence of 1.5 mM Ca2+. MP10 showed 100% residual activity and stability (up to 60 min) when incubated with 7% of non-ionic surfactants (Triton X-100, Tween-80 and Tween-20) and 1.5% of the oxidizing agent hydrogen peroxide. The 3D MP10 structure was predicted and compared with the crystal structure of mesophilic homologous protease produced by Pseudomonas aeruginosa PA01 (reference strain) and other proteases, showing similarity in surface area and volume of proteins, but a significantly higher surface pocket area and volume of MP10. The observed differences presumably may explain the enhanced activity of MP10 for substrate binding at low temperatures. These results give insight to the potential use of MP10 in developing new biotechnologically processes active at low to moderate temperatures, probably with focus in the detergent industry.
eu_rights_str_mv openAccess
format article
id anni_f9fd757efde99cae75a0ca2a98b2b76f
identifier_str_mv Fullana, N., et al.Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate. AIMS Bioengineering, 2017, 4 (3): 386-401. doi: 10.3934/bioeng.2017.3.386
2375-1495
10.3934/bioeng.2017.3.386
instacron_str Universidad de la República
institution Universidad de la República
instname_str Universidad de la República
language eng
language_invalid_str_mv en
network_acronym_str anni
network_name_str oai-lr-anni
oai_identifier_str oai:colibri.udelar.edu.uy:20.500.12008/22016
publishDate 2017
publishDateSort 2017
publisher.none.fl_str_mv AIMS Press
reponame_str COLIBRI
repository.mail.fl_str_mv
repository.name.fl_str_mv
repository_id_str
rights_invalid_str_mv Licencia Creative Commons Atribución (CC –BY 4.0)
spelling Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolateFullana, NataliaBraña, VictoriaMarizcurrena, Juan JoséMorales, DaniloBetton, Jean-MichelMarín Gutiérrez, MónicaCastro-Sowinski, SusanaProteasePseudomonasCold-adaptationSurfactantAntarcticaCold-adapted enzymes are generally derived from psychrophilic microorganisms and have features that make them very attractive for industrial and biotechnological purposes. In this work, we identified a 50 kDa extracellular protease (MP10) from the Antarctic isolate Pseudomonas sp. AU10. The enzyme was produced by recombinant DNA technology, purified using immobilized metal affinity chromatography and partially characterized. MP10 is an alkaline thermosensitive serine-metallo protease with optimal activity at pH 8.0 and 40 ℃, in the presence of 1.5 mM Ca2+. MP10 showed 100% residual activity and stability (up to 60 min) when incubated with 7% of non-ionic surfactants (Triton X-100, Tween-80 and Tween-20) and 1.5% of the oxidizing agent hydrogen peroxide. The 3D MP10 structure was predicted and compared with the crystal structure of mesophilic homologous protease produced by Pseudomonas aeruginosa PA01 (reference strain) and other proteases, showing similarity in surface area and volume of proteins, but a significantly higher surface pocket area and volume of MP10. The observed differences presumably may explain the enhanced activity of MP10 for substrate binding at low temperatures. These results give insight to the potential use of MP10 in developing new biotechnologically processes active at low to moderate temperatures, probably with focus in the detergent industry.AIMS PressFullana , Natalia. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de BiologíaBraña, Victoria. IIBCEMarizcurrena, Juan José. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de BiologíaMorales, Danilo. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de BiologíaMarín Gutierrez, Mónica. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de BiologíaCastro-Sowinski, Susana. Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología2019-10-02T22:08:28Z2019-10-02T22:08:28Z201720190930Artículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfFullana, N., et al.Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate. AIMS Bioengineering, 2017, 4 (3): 386-401. doi: 10.3934/bioeng.2017.3.3862375-1495https://hdl.handle.net/20.500.12008/2201610.3934/bioeng.2017.3.386reponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaenengAIMS Bioengineering, 2017, 4 (3): 386-401Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad De La República. (Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución (CC –BY 4.0)oai:colibri.udelar.edu.uy:20.500.12008/220162026-04-14T10:09:15Z
spellingShingle Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
Fullana, Natalia
Protease
Pseudomonas
Cold-adaptation
Surfactant
Antarctica
status_str publishedVersion
title Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
title_full Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
title_fullStr Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
title_full_unstemmed Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
title_short Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
title_sort Identification, recombinant production and partial biochemical characterization of an extracellular cold-active serine-metalloprotease from an Antarctic Pseudomonas isolate
topic Protease
Pseudomonas
Cold-adaptation
Surfactant
Antarctica
url https://hdl.handle.net/20.500.12008/22016