Identification and properties of two extracellular proteases from Brevundimonas diminuta

Brazilian Journal of Microbiology

André Adriano Chaia²  Salvatore Giovanni-de-simone¹  Simone Dias Gonçalves Petinate²  Ana Paula Cabral De Araújo Lima¹  Marta Helena Branquinha²  Alane Beatriz Vermelho² 

[1] ,Universidade Federal do Rio de Janeiro Instituto de Microbiologia Professor Paulo de Góes Departamento de Microbiologia GeralRio de Janeiro RJ ,Brasil

关键词: metalloproteases;    Brevundimonas diminuta;    Pseudomonadaceae;    extracellular proteases;    metaloproteases;    Brevundimonas diminuta;    Pseudomonadaceae;    proteases extracelulares;   

DOI  :  10.1590/S1517-83822000000100007

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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