Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1016/j.resmic.2004.12.004 (literal)

Alternative label

• L. Lama; I. Romano; V. Calandrelli; B. Nicolaus; A. Gambacorta (2005)
  Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus
  in Research in microbiology (Paris)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• L. Lama; I. Romano; V. Calandrelli; B. Nicolaus; A. Gambacorta (literal)

Pagina inizio

• 478 (literal)

Pagina fine

• 484 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 156 (literal)

Rivista

• Research in microbiology (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 4 (literal)

Note

• ISI Web of Science (WOS) (literal)
• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Istituto di Chimica Biomolecolare, CNR, via Campi Flegrei 34, 80078 Pozzuoli (NA), Italy (literal)

Titolo

• Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus (literal)

Abstract

• An extracellular protease produced at the end of the exponential growth phase was purified to homogeneity and characterized from the new isolate haloalkaliphilic strain 18AG, phylogenetically related to Salinivibrio costicola subsp. costicola. The protease molecular mass was about 38 kDa. The enzyme was dependent on salt concentration for activity and stability, and it showed optimal activity at 60 oC in the presence of 2.0% NaCl and 2.0 mM CaCl2, while in the absence of CaCl2 the optimum temperature was 50 oC. The enzyme was stable for 24 h at 30oC, whereas at 50 oC in the presence of CaCl2 the half life was about 5 h. The enzyme had an optimum pH of 8.0 with 80% of residual activity at pH 9.0. The protease was strongly inhibited by phenylmethyl sulfonylfluoride (PMSF), slightly activated by denaturing agents such as SDS and urea, and partially inhibited by thiol-containing reducing agents. The synthesis of the enzyme in culture media was influenced by the medium composition: it was specifically dependent upon the NaCl concentration and was induced by the presence of gelatin. (literal)

Prodotto di

• Istituto di chimica biomolecolare (ICB) (Istituto)
• LAMA - Gli Estremofili: extremozimi, esopolisaccaridi e loro applicazioni (PM.P01.008.001) (Modulo)

Autore CNR

• LICIA LAMA (Persona)
• VALERIA CALANDRELLI (Persona)
• AGATA GAMBACORTA (Unità di personale interno)
• BARBARA NICOLAUS (Unità di personale interno)
• IDA ROMANO (Unità di personale interno)

Insieme di parole chiave

• Parole chiave di "Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• LICIA LAMA (Persona)
• VALERIA CALANDRELLI (Persona)
• BARBARA NICOLAUS (Unità di personale interno)
• IDA ROMANO (Unità di personale interno)
• AGATA GAMBACORTA (Unità di personale interno)

Prodotto

• Istituto di chimica biomolecolare (ICB) (Istituto)
• LAMA - Gli Estremofili: extremozimi, esopolisaccaridi e loro applicazioni (PM.P01.008.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Research in microbiology (Rivista)

Insieme di parole chiave di

• Parole chiave di "Purification and characterization of a protease produced by an aerobic haloalkaliphilic species belonging to the Salinivibrio genus" (Insieme di parole chiave)