ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins
Autor(a) principal: | |
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Data de Publicação: | 2015 |
Outros Autores: | , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Food Science and Technology (Campinas) |
Texto Completo: | http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000100167 |
Resumo: | Phaseolus lunatus protein concentrates and the proteases Alcalase(R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase(R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. On the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high- performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides’ inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase(R) and Pepsin-Pancreatin. |
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Food Science and Technology (Campinas) |
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ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteinsP. lunatushydrolysatespeptidesACE inhibitory activityPhaseolus lunatus protein concentrates and the proteases Alcalase(R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase(R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. On the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high- performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides’ inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase(R) and Pepsin-Pancreatin.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2015-03-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000100167Food Science and Technology v.35 n.1 2015reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/1678-457X.6551info:eu-repo/semantics/openAccessMagaña,Mario DomínguezSegura-Campos,MairaDávila-Ortiz,GloriaBetancur-Ancona,DavidChel-Guerrero,Luiseng2015-05-06T00:00:00Zoai:scielo:S0101-20612015000100167Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2015-05-06T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false |
dc.title.none.fl_str_mv |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
title |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
spellingShingle |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins Magaña,Mario Domínguez P. lunatus hydrolysates peptides ACE inhibitory activity |
title_short |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
title_full |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
title_fullStr |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
title_full_unstemmed |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
title_sort |
ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins |
author |
Magaña,Mario Domínguez |
author_facet |
Magaña,Mario Domínguez Segura-Campos,Maira Dávila-Ortiz,Gloria Betancur-Ancona,David Chel-Guerrero,Luis |
author_role |
author |
author2 |
Segura-Campos,Maira Dávila-Ortiz,Gloria Betancur-Ancona,David Chel-Guerrero,Luis |
author2_role |
author author author author |
dc.contributor.author.fl_str_mv |
Magaña,Mario Domínguez Segura-Campos,Maira Dávila-Ortiz,Gloria Betancur-Ancona,David Chel-Guerrero,Luis |
dc.subject.por.fl_str_mv |
P. lunatus hydrolysates peptides ACE inhibitory activity |
topic |
P. lunatus hydrolysates peptides ACE inhibitory activity |
description |
Phaseolus lunatus protein concentrates and the proteases Alcalase(R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase(R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. On the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high- performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides’ inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase(R) and Pepsin-Pancreatin. |
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=S0101-20612015000100167 |
url |
http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000100167 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.1590/1678-457X.6551 |
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 Ciência e Tecnologia de Alimentos |
publisher.none.fl_str_mv |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos |
dc.source.none.fl_str_mv |
Food Science and Technology v.35 n.1 2015 reponame:Food Science and Technology (Campinas) instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) instacron:SBCTA |
instname_str |
Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
instacron_str |
SBCTA |
institution |
SBCTA |
reponame_str |
Food Science and Technology (Campinas) |
collection |
Food Science and Technology (Campinas) |
repository.name.fl_str_mv |
Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA) |
repository.mail.fl_str_mv |
||revista@sbcta.org.br |
_version_ |
1752126319469002752 |