Identification and properties of two extracellular proteases from Brevundimonas diminuta

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 Z-Phe-Arg-MCA and the inhibitors EGTA, EDTA and 1, 10 phenanthroline point out that these enzymes are metalloproteases.

Bibliographic Details

Main Authors:	Chaia,André Adriano, Giovanni-De-Simone,Salvatore, Petinate,Simone Dias Gonçalves, Lima,Ana Paula Cabral de Araújo, Branquinha,Marta Helena, Vermelho,Alane Beatriz
Format:	Digital revista
Language:	English
Published:	Sociedade Brasileira de Microbiologia 2000
Online Access:	http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007
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