Production and properties of an extracellular protease from thermophilic Bacillus sp

Detalhes bibliográficos
Autor(a) principal: Nascimento,Wellingta Cristina Almeida do
Data de Publicação: 2004
Outros Autores: Martins,Meire Lelis Leal
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=S1517-83822004000100015
Resumo: Protease production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing trisodium citrate reached a maximum in 9h, with levels of 1.93U/mg protein. The microorganism utilized several carbon sources for the production of protease. Starch was the best substrate, followed by trisodium citrate, citric acid and sucrose. Among the various organic and inorganic nitrogen sources, ammonium nitrate was found to be the best. Studies on the protease characterization revealed that the optimum temperature of this enzyme was 60ºC. The enzyme was stable for 2h at 30ºC, while at 40ºC and 80ºC, 14% and 84% of the original activities were lost, respectively. The optimum pH of the enzyme was found to be 8.0. After incubation of crude enzyme solution for 24h at pH 5.5, 8.0 and 9.0, a decrease of about 51%, 18% and 66% of its original activity was observed respectively. A stronger inhibitory effect was observed in the presence of K+, Hg2+and Cu2+. Hg+ resulted in the complete loss of activity at 1mM concentrations. Activity was stimulated by Mn2+ and Ca+2, indicating that these ions had a functional role in the molecular structure of the enzyme.
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spelling Production and properties of an extracellular protease from thermophilic Bacillus spproteasethermophilic bacteriumBacillus sp.Protease production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing trisodium citrate reached a maximum in 9h, with levels of 1.93U/mg protein. The microorganism utilized several carbon sources for the production of protease. Starch was the best substrate, followed by trisodium citrate, citric acid and sucrose. Among the various organic and inorganic nitrogen sources, ammonium nitrate was found to be the best. Studies on the protease characterization revealed that the optimum temperature of this enzyme was 60ºC. The enzyme was stable for 2h at 30ºC, while at 40ºC and 80ºC, 14% and 84% of the original activities were lost, respectively. The optimum pH of the enzyme was found to be 8.0. After incubation of crude enzyme solution for 24h at pH 5.5, 8.0 and 9.0, a decrease of about 51%, 18% and 66% of its original activity was observed respectively. A stronger inhibitory effect was observed in the presence of K+, Hg2+and Cu2+. Hg+ resulted in the complete loss of activity at 1mM concentrations. Activity was stimulated by Mn2+ and Ca+2, indicating that these ions had a functional role in the molecular structure of the enzyme.Sociedade Brasileira de Microbiologia2004-06-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100015Brazilian Journal of Microbiology v.35 n.1-2 2004reponame:Brazilian Journal of Microbiologyinstname:Sociedade Brasileira de Microbiologia (SBM)instacron:SBM10.1590/S1517-83822004000100015info:eu-repo/semantics/openAccessNascimento,Wellingta Cristina Almeida doMartins,Meire Lelis Lealeng2004-11-16T00:00:00Zoai:scielo:S1517-83822004000100015Revistahttps://www.scielo.br/j/bjm/ONGhttps://old.scielo.br/oai/scielo-oai.phpbjm@sbmicrobiologia.org.br||mbmartin@usp.br1678-44051517-8382opendoar:2004-11-16T00:00Brazilian Journal of Microbiology - Sociedade Brasileira de Microbiologia (SBM)false
dc.title.none.fl_str_mv Production and properties of an extracellular protease from thermophilic Bacillus sp
title Production and properties of an extracellular protease from thermophilic Bacillus sp
spellingShingle Production and properties of an extracellular protease from thermophilic Bacillus sp
Nascimento,Wellingta Cristina Almeida do
protease
thermophilic bacterium
Bacillus sp.
title_short Production and properties of an extracellular protease from thermophilic Bacillus sp
title_full Production and properties of an extracellular protease from thermophilic Bacillus sp
title_fullStr Production and properties of an extracellular protease from thermophilic Bacillus sp
title_full_unstemmed Production and properties of an extracellular protease from thermophilic Bacillus sp
title_sort Production and properties of an extracellular protease from thermophilic Bacillus sp
author Nascimento,Wellingta Cristina Almeida do
author_facet Nascimento,Wellingta Cristina Almeida do
Martins,Meire Lelis Leal
author_role author
author2 Martins,Meire Lelis Leal
author2_role author
dc.contributor.author.fl_str_mv Nascimento,Wellingta Cristina Almeida do
Martins,Meire Lelis Leal
dc.subject.por.fl_str_mv protease
thermophilic bacterium
Bacillus sp.
topic protease
thermophilic bacterium
Bacillus sp.
description Protease production by thermophilic Bacillus sp strain SMIA-2 cultivated in liquid cultures containing trisodium citrate reached a maximum in 9h, with levels of 1.93U/mg protein. The microorganism utilized several carbon sources for the production of protease. Starch was the best substrate, followed by trisodium citrate, citric acid and sucrose. Among the various organic and inorganic nitrogen sources, ammonium nitrate was found to be the best. Studies on the protease characterization revealed that the optimum temperature of this enzyme was 60ºC. The enzyme was stable for 2h at 30ºC, while at 40ºC and 80ºC, 14% and 84% of the original activities were lost, respectively. The optimum pH of the enzyme was found to be 8.0. After incubation of crude enzyme solution for 24h at pH 5.5, 8.0 and 9.0, a decrease of about 51%, 18% and 66% of its original activity was observed respectively. A stronger inhibitory effect was observed in the presence of K+, Hg2+and Cu2+. Hg+ resulted in the complete loss of activity at 1mM concentrations. Activity was stimulated by Mn2+ and Ca+2, indicating that these ions had a functional role in the molecular structure of the enzyme.
publishDate 2004
dc.date.none.fl_str_mv 2004-06-01
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=S1517-83822004000100015
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S1517-83822004000100015
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S1517-83822004000100015
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.35 n.1-2 2004
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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