Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade

Detalhes bibliográficos
Autor(a) principal: Araújo,Jéssica Morais de
Data de Publicação: 2014
Outros Autores: Alves,Jussara Cristina, Peixoto,Thayane Kerbele Oliveira das Neves, Medeiros,Amanda Fernandes de, Machado,Richele Janaína de Araújo, Serquiz,Alexandre Coelho, Neves,Renata Alexandra Moreira das, Santos,Elizeu Antunes dos, Uchôa,Adriana Ferreira, Morais,Ana Heloneida de Araújo
Tipo de documento: Artigo
Idioma: por
Título da fonte: Química Nova (Online)
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422014001000008
Resumo: The peanut is an oleaginous plant of high nutritional value, a source of protein and a trypsin inhibitor. Trypsin inhibitors are proteins present in the vegetable kingdom, considered anti-nutritional factors for animals. However, there have been several recent reports about their heterologous and beneficial effects on human health. These important effects have been the focus of studies investigating these inhibitors in foods. The aim of the present study was to isolate and determine the estimated molecular mass and specific inhibitory activity, for trypsin in the Japanese peanut, peanut butter, and peanut nougat using the techniques of precipitation with ammonium sulfate and affinity chromatography on trypsin - Sepharose CNBr 4B. The techniques used in this study were efficient for isolating the protein inhibitors with antitryptic specific activity of 694 UI mg-1, 823 UI mg-1 and 108 UI mg-1 for the Japanese peanut, peanut nougat, and peanut butter, respectively. The techniques featured high selectivity of the adsorbent, with consequent efficiency in isolation, given the low amount of dosed proteins and specific antitryptic activity presented by the products studied. The various health-related benefits show the importance of detecting and isolating efficient trypsin inhibitors in foods, taking into account the health claims attributed to the vegetable and its high consumption by humans.
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spelling Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidadeArachis hypogaea L.japanese peanutpeanut nougatpeanut buttertrypsin inhibitorThe peanut is an oleaginous plant of high nutritional value, a source of protein and a trypsin inhibitor. Trypsin inhibitors are proteins present in the vegetable kingdom, considered anti-nutritional factors for animals. However, there have been several recent reports about their heterologous and beneficial effects on human health. These important effects have been the focus of studies investigating these inhibitors in foods. The aim of the present study was to isolate and determine the estimated molecular mass and specific inhibitory activity, for trypsin in the Japanese peanut, peanut butter, and peanut nougat using the techniques of precipitation with ammonium sulfate and affinity chromatography on trypsin - Sepharose CNBr 4B. The techniques used in this study were efficient for isolating the protein inhibitors with antitryptic specific activity of 694 UI mg-1, 823 UI mg-1 and 108 UI mg-1 for the Japanese peanut, peanut nougat, and peanut butter, respectively. The techniques featured high selectivity of the adsorbent, with consequent efficiency in isolation, given the low amount of dosed proteins and specific antitryptic activity presented by the products studied. The various health-related benefits show the importance of detecting and isolating efficient trypsin inhibitors in foods, taking into account the health claims attributed to the vegetable and its high consumption by humans.Sociedade Brasileira de Química2014-01-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422014001000008Química Nova v.37 n.10 2014reponame:Química Nova (Online)instname:Sociedade Brasileira de Química (SBQ)instacron:SBQ10.5935/0100-4042.20140254info:eu-repo/semantics/openAccessAraújo,Jéssica Morais deAlves,Jussara CristinaPeixoto,Thayane Kerbele Oliveira das NevesMedeiros,Amanda Fernandes deMachado,Richele Janaína de AraújoSerquiz,Alexandre CoelhoNeves,Renata Alexandra Moreira dasSantos,Elizeu Antunes dosUchôa,Adriana FerreiraMorais,Ana Heloneida de Araújopor2014-11-28T00:00:00Zoai:scielo:S0100-40422014001000008Revistahttps://www.scielo.br/j/qn/ONGhttps://old.scielo.br/oai/scielo-oai.phpquimicanova@sbq.org.br1678-70640100-4042opendoar:2014-11-28T00:00Química Nova (Online) - Sociedade Brasileira de Química (SBQ)false
dc.title.none.fl_str_mv Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
title Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
spellingShingle Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
Araújo,Jéssica Morais de
Arachis hypogaea L.
japanese peanut
peanut nougat
peanut butter
trypsin inhibitor
title_short Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
title_full Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
title_fullStr Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
title_full_unstemmed Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
title_sort Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
author Araújo,Jéssica Morais de
author_facet Araújo,Jéssica Morais de
Alves,Jussara Cristina
Peixoto,Thayane Kerbele Oliveira das Neves
Medeiros,Amanda Fernandes de
Machado,Richele Janaína de Araújo
Serquiz,Alexandre Coelho
Neves,Renata Alexandra Moreira das
Santos,Elizeu Antunes dos
Uchôa,Adriana Ferreira
Morais,Ana Heloneida de Araújo
author_role author
author2 Alves,Jussara Cristina
Peixoto,Thayane Kerbele Oliveira das Neves
Medeiros,Amanda Fernandes de
Machado,Richele Janaína de Araújo
Serquiz,Alexandre Coelho
Neves,Renata Alexandra Moreira das
Santos,Elizeu Antunes dos
Uchôa,Adriana Ferreira
Morais,Ana Heloneida de Araújo
author2_role author
author
author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Araújo,Jéssica Morais de
Alves,Jussara Cristina
Peixoto,Thayane Kerbele Oliveira das Neves
Medeiros,Amanda Fernandes de
Machado,Richele Janaína de Araújo
Serquiz,Alexandre Coelho
Neves,Renata Alexandra Moreira das
Santos,Elizeu Antunes dos
Uchôa,Adriana Ferreira
Morais,Ana Heloneida de Araújo
dc.subject.por.fl_str_mv Arachis hypogaea L.
japanese peanut
peanut nougat
peanut butter
trypsin inhibitor
topic Arachis hypogaea L.
japanese peanut
peanut nougat
peanut butter
trypsin inhibitor
description The peanut is an oleaginous plant of high nutritional value, a source of protein and a trypsin inhibitor. Trypsin inhibitors are proteins present in the vegetable kingdom, considered anti-nutritional factors for animals. However, there have been several recent reports about their heterologous and beneficial effects on human health. These important effects have been the focus of studies investigating these inhibitors in foods. The aim of the present study was to isolate and determine the estimated molecular mass and specific inhibitory activity, for trypsin in the Japanese peanut, peanut butter, and peanut nougat using the techniques of precipitation with ammonium sulfate and affinity chromatography on trypsin - Sepharose CNBr 4B. The techniques used in this study were efficient for isolating the protein inhibitors with antitryptic specific activity of 694 UI mg-1, 823 UI mg-1 and 108 UI mg-1 for the Japanese peanut, peanut nougat, and peanut butter, respectively. The techniques featured high selectivity of the adsorbent, with consequent efficiency in isolation, given the low amount of dosed proteins and specific antitryptic activity presented by the products studied. The various health-related benefits show the importance of detecting and isolating efficient trypsin inhibitors in foods, taking into account the health claims attributed to the vegetable and its high consumption by humans.
publishDate 2014
dc.date.none.fl_str_mv 2014-01-01
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=S0100-40422014001000008
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-40422014001000008
dc.language.iso.fl_str_mv por
language por
dc.relation.none.fl_str_mv 10.5935/0100-4042.20140254
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 Química
publisher.none.fl_str_mv Sociedade Brasileira de Química
dc.source.none.fl_str_mv Química Nova v.37 n.10 2014
reponame:Química Nova (Online)
instname:Sociedade Brasileira de Química (SBQ)
instacron:SBQ
instname_str Sociedade Brasileira de Química (SBQ)
instacron_str SBQ
institution SBQ
reponame_str Química Nova (Online)
collection Química Nova (Online)
repository.name.fl_str_mv Química Nova (Online) - Sociedade Brasileira de Química (SBQ)
repository.mail.fl_str_mv quimicanova@sbq.org.br
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