Identification and properties of two extracellular proteases from Brevundimonas diminuta

Detalhes bibliográficos
Autor(a) principal: Chaia,André Adriano
Data de Publicação: 2000
Outros Autores: Giovanni-De-Simone,Salvatore, Petinate,Simone Dias Gonçalves, Lima,Ana Paula Cabral de Araújo, Branquinha,Marta Helena, Vermelho,Alane Beatriz
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Microbiology
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007
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 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.
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spelling Identification and properties of two extracellular proteases from Brevundimonas diminutametalloproteasesBrevundimonas diminutaPseudomonadaceaeextracellular proteasesExtracellular 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.Sociedade Brasileira de Microbiologia2000-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007Brazilian Journal of Microbiology v.31 n.1 2000reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822000000100007info:eu-repo/semantics/openAccessChaia,André AdrianoGiovanni-De-Simone,SalvatorePetinate,Simone Dias GonçalvesLima,Ana Paula Cabral de AraújoBranquinha,Marta HelenaVermelho,Alane Beatrizeng2000-08-25T00:00:00Zoai:scielo:S1517-83822000000100007Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2000-08-25T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false
dc.title.none.fl_str_mv Identification and properties of two extracellular proteases from Brevundimonas diminuta
title Identification and properties of two extracellular proteases from Brevundimonas diminuta
spellingShingle Identification and properties of two extracellular proteases from Brevundimonas diminuta
Chaia,André Adriano
metalloproteases
Brevundimonas diminuta
Pseudomonadaceae
extracellular proteases
title_short Identification and properties of two extracellular proteases from Brevundimonas diminuta
title_full Identification and properties of two extracellular proteases from Brevundimonas diminuta
title_fullStr Identification and properties of two extracellular proteases from Brevundimonas diminuta
title_full_unstemmed Identification and properties of two extracellular proteases from Brevundimonas diminuta
title_sort Identification and properties of two extracellular proteases from Brevundimonas diminuta
author Chaia,André Adriano
author_facet Chaia,André Adriano
Giovanni-De-Simone,Salvatore
Petinate,Simone Dias Gonçalves
Lima,Ana Paula Cabral de Araújo
Branquinha,Marta Helena
Vermelho,Alane Beatriz
author_role author
author2 Giovanni-De-Simone,Salvatore
Petinate,Simone Dias Gonçalves
Lima,Ana Paula Cabral de Araújo
Branquinha,Marta Helena
Vermelho,Alane Beatriz
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Chaia,André Adriano
Giovanni-De-Simone,Salvatore
Petinate,Simone Dias Gonçalves
Lima,Ana Paula Cabral de Araújo
Branquinha,Marta Helena
Vermelho,Alane Beatriz
dc.subject.por.fl_str_mv metalloproteases
Brevundimonas diminuta
Pseudomonadaceae
extracellular proteases
topic metalloproteases
Brevundimonas diminuta
Pseudomonadaceae
extracellular proteases
description 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.
publishDate 2000
dc.date.none.fl_str_mv 2000-03-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822000000100007
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1517-83822000000100007
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Sociedade Brasileira de Microbiologia
publisher.none.fl_str_mv Sociedade Brasileira de Microbiologia
dc.source.none.fl_str_mv Brazilian Journal of Microbiology v.31 n.1 2000
reponame:Brazilian Journal of Microbiology
instname:Sociedade Brasileira de Microbiologia (SBM)
instacron:SBM
instname_str Sociedade Brasileira de Microbiologia (SBM)
instacron_str SBM
institution SBM
reponame_str Brazilian Journal of Microbiology
collection Brazilian Journal of Microbiology
repository.name.fl_str_mv Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)
repository.mail.fl_str_mv bjm@sbmicrobiologia.org.br||mbmartin@usp.br
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