Purification and characterization of an alkaline serine endopeptidase from a feather-degrading Xanthomonas maltophilia strain.
Can J Microbiol
; 48(4): 342-8, 2002 Apr.
Article
en En
| MEDLINE
| ID: mdl-12030707
A keratinolytic Xanthomonas maltophilia strain (POA-1), cultured on feather meal broth, using keratin as its sole source of carbon and nitrogen, secretes several extracellular peptidases. The major serine peptidase was purified to homogeneity by a five-step procedure. Its purity was evaluated by capillary zone electrophoresis. This enzyme has a molecular mass of 36 kDa, an optimum pH of 9.0, and an optimum temperature of 60 degrees C. The inhibitory profile using protease inhibitors shows that this enzyme is a serine endopeptidase. Besides keratin, the enzyme is active upon the substrates azokeratin, azocasein, and the following fluorogenic peptide substrates: Abz-Leu-Gly-Met-Ile-Ser-Leu-Met-Lys-Arg-Pro-Gln-EDDnp, Abz-Lys-Leu-Cys(SBzl)-Gly-Pro-Lys-Gln-EDDnp, and Abz-Lys-Pro-Cys(SBzl)-Phe-Ser-Lys-Gln-EDDnp.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Serina Endopeptidasas
/
Stenotrophomonas maltophilia
/
Plumas
/
Queratinas
Límite:
Animals
Idioma:
En
Revista:
Can J Microbiol
Año:
2002
Tipo del documento:
Article
País de afiliación:
Brasil
Pais de publicación:
Canadá