Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Anais da Academia Brasileira de Ciências (Online) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000100109 |
Resumo: | Two psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus(99%), with query coverage of 99% and 98%, respectively.The spent culture media from both isolates displayed proteolytic activities detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis containing gelatin as protein substrate. Under the employed conditions, S. aquimarina showed a 55 kDa protease with the best activity detected at pH 7.0 and at 27°C. A. antarcticusalso showed a single extracellular protease, however its molecular mass was around 90kDa and its best activity was detected at pH 9.0 and at 37°C. The proteases from both isolates were inhibited by 1,10-phenanthroline and EDTA, two metalloprotease inhibitors. This is the first record of protease detection in both species, and our results may contribute to broaden the basic knowledge of proteases from the Antarctica environment and may help prospecting future biotechnological applications of these enzymes. |
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Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soilAlgoriphagus antarcticusAntarcticaSporosarcina aquimarinaProteaseTwo psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus(99%), with query coverage of 99% and 98%, respectively.The spent culture media from both isolates displayed proteolytic activities detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis containing gelatin as protein substrate. Under the employed conditions, S. aquimarina showed a 55 kDa protease with the best activity detected at pH 7.0 and at 27°C. A. antarcticusalso showed a single extracellular protease, however its molecular mass was around 90kDa and its best activity was detected at pH 9.0 and at 37°C. The proteases from both isolates were inhibited by 1,10-phenanthroline and EDTA, two metalloprotease inhibitors. This is the first record of protease detection in both species, and our results may contribute to broaden the basic knowledge of proteases from the Antarctica environment and may help prospecting future biotechnological applications of these enzymes.Academia Brasileira de Ciências2015-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000100109Anais da Academia Brasileira de Ciências v.87 n.1 2015reponame:Anais da Academia Brasileira de Ciências (Online)instname:Academia Brasileira de Ciências (ABC)instacron:ABC10.1590/0001-3765201520130519info:eu-repo/semantics/openAccessSantos,Anderson F.Pires,FabianoJesus,Hugo E.Santos,André L.S.Peixoto,RaquelRosado,Alexandre S.D'Avila-Levy,Claudia M.Branquinha,Marta H.eng2015-11-16T00:00:00Zoai:scielo:S0001-37652015000100109Revistahttp://www.scielo.br/aabchttps://old.scielo.br/oai/scielo-oai.php||aabc@abc.org.br1678-26900001-3765opendoar:2015-11-16T00:00Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC)false |
dc.title.none.fl_str_mv |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
title |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
spellingShingle |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil Santos,Anderson F. Algoriphagus antarcticus Antarctica Sporosarcina aquimarina Protease |
title_short |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
title_full |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
title_fullStr |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
title_full_unstemmed |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
title_sort |
Detection of proteases from Sporosarcina aquimarina and Algoriphagus antarcticus isolated from Antarctic soil |
author |
Santos,Anderson F. |
author_facet |
Santos,Anderson F. Pires,Fabiano Jesus,Hugo E. Santos,André L.S. Peixoto,Raquel Rosado,Alexandre S. D'Avila-Levy,Claudia M. Branquinha,Marta H. |
author_role |
author |
author2 |
Pires,Fabiano Jesus,Hugo E. Santos,André L.S. Peixoto,Raquel Rosado,Alexandre S. D'Avila-Levy,Claudia M. Branquinha,Marta H. |
author2_role |
author author author author author author author |
dc.contributor.author.fl_str_mv |
Santos,Anderson F. Pires,Fabiano Jesus,Hugo E. Santos,André L.S. Peixoto,Raquel Rosado,Alexandre S. D'Avila-Levy,Claudia M. Branquinha,Marta H. |
dc.subject.por.fl_str_mv |
Algoriphagus antarcticus Antarctica Sporosarcina aquimarina Protease |
topic |
Algoriphagus antarcticus Antarctica Sporosarcina aquimarina Protease |
description |
Two psychrophilic bacterial samples were isolated from King George Island soil, in Antarctica. The phylogenetic analysis based on the 16S rRNA (rrs) gene led to the correlation with the closest related isolates as Sporosarcina aquimarina (99%) and Algoriphagus antarcticus(99%), with query coverage of 99% and 98%, respectively.The spent culture media from both isolates displayed proteolytic activities detected by sodium dodecyl sulfate polyacrylamide gel electrophoresis containing gelatin as protein substrate. Under the employed conditions, S. aquimarina showed a 55 kDa protease with the best activity detected at pH 7.0 and at 27°C. A. antarcticusalso showed a single extracellular protease, however its molecular mass was around 90kDa and its best activity was detected at pH 9.0 and at 37°C. The proteases from both isolates were inhibited by 1,10-phenanthroline and EDTA, two metalloprotease inhibitors. This is the first record of protease detection in both species, and our results may contribute to broaden the basic knowledge of proteases from the Antarctica environment and may help prospecting future biotechnological applications of these enzymes. |
publishDate |
2015 |
dc.date.none.fl_str_mv |
2015-03-01 |
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=S0001-37652015000100109 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0001-37652015000100109 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/0001-3765201520130519 |
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 |
Academia Brasileira de Ciências |
publisher.none.fl_str_mv |
Academia Brasileira de Ciências |
dc.source.none.fl_str_mv |
Anais da Academia Brasileira de Ciências v.87 n.1 2015 reponame:Anais da Academia Brasileira de Ciências (Online) instname:Academia Brasileira de Ciências (ABC) instacron:ABC |
instname_str |
Academia Brasileira de Ciências (ABC) |
instacron_str |
ABC |
institution |
ABC |
reponame_str |
Anais da Academia Brasileira de Ciências (Online) |
collection |
Anais da Academia Brasileira de Ciências (Online) |
repository.name.fl_str_mv |
Anais da Academia Brasileira de Ciências (Online) - Academia Brasileira de Ciências (ABC) |
repository.mail.fl_str_mv |
||aabc@abc.org.br |
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1754302860462391297 |