Determinação da atividade antitríptica em proteínas de produtos do amendoim isoladas por cromatografia de afinidade
Autor(a) principal: | |
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Data de Publicação: | 2014 |
Outros Autores: | , , , , , , , , |
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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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 |
_version_ |
1750318116308516864 |