Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Detalhes bibliográficos
Autor(a) principal: Brito,Mônica Silva de
Data de Publicação: 2016
Outros Autores: Melo,Mônica Brandão, Alves,Jamille Perdigão de Andrade, Fontenelle,Raquel Oliveira dos Santos, Mata,Marlene Feliciano, Andrade,Lúcia Betânia da Silva
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Hoehnea
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S2236-89062016000100011
Resumo: ABSTRACT The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds.
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spelling Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractionsantimicrobialcystatinFabaceaeproteaseABSTRACT The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds.Instituto de Pesquisas Ambientais2016-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S2236-89062016000100011Hoehnea v.43 n.1 2016reponame:Hoehneainstname:Instituto de Botânica (IBT)instacron:IBT10.1590/2236-8906-23/2015info:eu-repo/semantics/openAccessBrito,Mônica Silva deMelo,Mônica BrandãoAlves,Jamille Perdigão de AndradeFontenelle,Raquel Oliveira dos SantosMata,Marlene FelicianoAndrade,Lúcia Betânia da Silvaeng2016-03-15T00:00:00Zoai:scielo:S2236-89062016000100011Revistahttp://www.ibot.sp.gov.br/publicacoes/hoehnea/sobre_hoehnea.phpPUBhttps://old.scielo.br/oai/scielo-oai.php||hoehneaibt@gmail.com2236-89060073-2877opendoar:2016-03-15T00:00Hoehnea - Instituto de Botânica (IBT)false
dc.title.none.fl_str_mv Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
title Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
spellingShingle Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
Brito,Mônica Silva de
antimicrobial
cystatin
Fabaceae
protease
title_short Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
title_full Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
title_fullStr Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
title_full_unstemmed Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
title_sort Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions
author Brito,Mônica Silva de
author_facet Brito,Mônica Silva de
Melo,Mônica Brandão
Alves,Jamille Perdigão de Andrade
Fontenelle,Raquel Oliveira dos Santos
Mata,Marlene Feliciano
Andrade,Lúcia Betânia da Silva
author_role author
author2 Melo,Mônica Brandão
Alves,Jamille Perdigão de Andrade
Fontenelle,Raquel Oliveira dos Santos
Mata,Marlene Feliciano
Andrade,Lúcia Betânia da Silva
author2_role author
author
author
author
author
dc.contributor.author.fl_str_mv Brito,Mônica Silva de
Melo,Mônica Brandão
Alves,Jamille Perdigão de Andrade
Fontenelle,Raquel Oliveira dos Santos
Mata,Marlene Feliciano
Andrade,Lúcia Betânia da Silva
dc.subject.por.fl_str_mv antimicrobial
cystatin
Fabaceae
protease
topic antimicrobial
cystatin
Fabaceae
protease
description ABSTRACT The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds.
publishDate 2016
dc.date.none.fl_str_mv 2016-03-01
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=S2236-89062016000100011
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S2236-89062016000100011
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/2236-8906-23/2015
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 Instituto de Pesquisas Ambientais
publisher.none.fl_str_mv Instituto de Pesquisas Ambientais
dc.source.none.fl_str_mv Hoehnea v.43 n.1 2016
reponame:Hoehnea
instname:Instituto de Botânica (IBT)
instacron:IBT
instname_str Instituto de Botânica (IBT)
instacron_str IBT
institution IBT
reponame_str Hoehnea
collection Hoehnea
repository.name.fl_str_mv Hoehnea - Instituto de Botânica (IBT)
repository.mail.fl_str_mv ||hoehneaibt@gmail.com
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