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Identification and properties of two extracellular proteases from Brevundimonas diminuta BJM
Chaia,André Adriano; Giovanni-De-Simone,Salvatore; Petinate,Simone Dias Gonçalves; Lima,Ana Paula Cabral de Araújo; Branquinha,Marta Helena; Vermelho,Alane Beatriz.
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 67 kDa 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). Protease assays with the synthetic substrate...
Tipo: Info:eu-repo/semantics/article Palavras-chave: Metalloproteases; Brevundimonas diminuta; Pseudomonadaceae; Extracellular proteases.
Ano: 2000 URL: http://www.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007
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