Identification and properties of two extracellular proteases from Brevundimonas diminuta
Braz. j. microbiol
; 31(1): 25-29, jan.-mar. 2000. ilus, tab
Article
en En
| LILACS
| ID: lil-306361
Biblioteca responsable:
BR32.1
RESUMO
Extracellular proteases from Brevundimonas diminuta (syn. Pseudomonas diminuta) were studied in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) containing a copolymerized substrate. Two proteases were detected migrating at 67kDa and 50 kDa both of them hydrolysed preferentially gelatin, but casein was also degraded and a slight hydrolysis was observed with hemoglobin. No detectable extracellular proteolytic activity was found in bovine serum albumin-containing gels. The optima temperature and pH for proteolytic activity were between 40ºC and 50ºC in a pH ranging from 7.0 to 11.0, respectively. These enzymes were isolated by analytical high performance liquid chromatography (HPLC). Proteases assays with the synthetic substrate Z-Phe-Arg-MCA and inhibitors EGTA, EDTA and 1, 10 phenanthroline point out that these enzymes are metalloproteases.
Texto completo:
1
Colección:
01-internacional
Base de datos:
LILACS
Asunto principal:
Pseudomonadaceae
/
Pseudomonas
/
Técnicas In Vitro
/
Metaloendopeptidasas
/
Electroforesis en Gel de Poliacrilamida
/
Enzimas
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
Braz. j. microbiol
Asunto de la revista:
MICROBIOLOGIA
Año:
2000
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Brasil