Peptide separation of commercial fermented milk during refrigerated storage

Detalhes bibliográficos
Autor(a) principal: González-Olivares,Luis Guillermo
Data de Publicação: 2014
Outros Autores: Añorve-Morga,Javier, Castañeda-Ovando,Araceli, Contreras-López,Elizabeth, Jaimez-Ordaz,Judith
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=S0101-20612014000400005
Resumo: Milk is an important source of bioactive compounds. Many of these compounds are released during fermentation and refrigerated storage. The aim of this study was to determine the release of peptides by lactic acid bacteria in commercial fermented milk during refrigerated storage. The size and profile of peptides were analyzed by polyacrylamide gel electrophoresis and sizeexclusion HPLC. During electrophoresis, it was observed that the peptides were released from caseins, whereas β-lactoglobulin was the whey protein with the highest degradation. HPLC analysis confirmed the pattern of peptide formation observed in electrophoresis. Two fractions lower than 2 kDa with aromatic amino acids in their structure were separated. These results were consistent with those reported for structures of peptides with antihypertensive activity. Therefore, the presence of aromatic amino acids in the peptide fractions obtained increases the likelihood of finding peptides with such activity in refrigerated commercial fermented milk. In conclusion, during cold storage, peptides with different molecular weights are released and accumulated. This could be due to the action of proteinases and peptidases of the proteolytic system in lactic acid bacteria.
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spelling Peptide separation of commercial fermented milk during refrigerated storagebioactive peptidefermented milkcold storageantihypertensive activitylactic acid bacteriaMilk is an important source of bioactive compounds. Many of these compounds are released during fermentation and refrigerated storage. The aim of this study was to determine the release of peptides by lactic acid bacteria in commercial fermented milk during refrigerated storage. The size and profile of peptides were analyzed by polyacrylamide gel electrophoresis and sizeexclusion HPLC. During electrophoresis, it was observed that the peptides were released from caseins, whereas β-lactoglobulin was the whey protein with the highest degradation. HPLC analysis confirmed the pattern of peptide formation observed in electrophoresis. Two fractions lower than 2 kDa with aromatic amino acids in their structure were separated. These results were consistent with those reported for structures of peptides with antihypertensive activity. Therefore, the presence of aromatic amino acids in the peptide fractions obtained increases the likelihood of finding peptides with such activity in refrigerated commercial fermented milk. In conclusion, during cold storage, peptides with different molecular weights are released and accumulated. This could be due to the action of proteinases and peptidases of the proteolytic system in lactic acid bacteria.Sociedade Brasileira de Ciência e Tecnologia de Alimentos2014-12-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612014000400005Food Science and Technology v.34 n.4 2014reponame:Food Science and Technology (Campinas)instname:Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)instacron:SBCTA10.1590/1678-457X.6415info:eu-repo/semantics/openAccessGonzález-Olivares,Luis GuillermoAñorve-Morga,JavierCastañeda-Ovando,AraceliContreras-López,ElizabethJaimez-Ordaz,Juditheng2015-01-30T00:00:00Zoai:scielo:S0101-20612014000400005Revistahttp://www.scielo.br/ctaONGhttps://old.scielo.br/oai/scielo-oai.php||revista@sbcta.org.br1678-457X0101-2061opendoar:2015-01-30T00:00Food Science and Technology (Campinas) - Sociedade Brasileira de Ciência e Tecnologia de Alimentos (SBCTA)false
dc.title.none.fl_str_mv Peptide separation of commercial fermented milk during refrigerated storage
title Peptide separation of commercial fermented milk during refrigerated storage
spellingShingle Peptide separation of commercial fermented milk during refrigerated storage
González-Olivares,Luis Guillermo
bioactive peptide
fermented milk
cold storage
antihypertensive activity
lactic acid bacteria
title_short Peptide separation of commercial fermented milk during refrigerated storage
title_full Peptide separation of commercial fermented milk during refrigerated storage
title_fullStr Peptide separation of commercial fermented milk during refrigerated storage
title_full_unstemmed Peptide separation of commercial fermented milk during refrigerated storage
title_sort Peptide separation of commercial fermented milk during refrigerated storage
author González-Olivares,Luis Guillermo
author_facet González-Olivares,Luis Guillermo
Añorve-Morga,Javier
Castañeda-Ovando,Araceli
Contreras-López,Elizabeth
Jaimez-Ordaz,Judith
author_role author
author2 Añorve-Morga,Javier
Castañeda-Ovando,Araceli
Contreras-López,Elizabeth
Jaimez-Ordaz,Judith
author2_role author
author
author
author
dc.contributor.author.fl_str_mv González-Olivares,Luis Guillermo
Añorve-Morga,Javier
Castañeda-Ovando,Araceli
Contreras-López,Elizabeth
Jaimez-Ordaz,Judith
dc.subject.por.fl_str_mv bioactive peptide
fermented milk
cold storage
antihypertensive activity
lactic acid bacteria
topic bioactive peptide
fermented milk
cold storage
antihypertensive activity
lactic acid bacteria
description Milk is an important source of bioactive compounds. Many of these compounds are released during fermentation and refrigerated storage. The aim of this study was to determine the release of peptides by lactic acid bacteria in commercial fermented milk during refrigerated storage. The size and profile of peptides were analyzed by polyacrylamide gel electrophoresis and sizeexclusion HPLC. During electrophoresis, it was observed that the peptides were released from caseins, whereas β-lactoglobulin was the whey protein with the highest degradation. HPLC analysis confirmed the pattern of peptide formation observed in electrophoresis. Two fractions lower than 2 kDa with aromatic amino acids in their structure were separated. These results were consistent with those reported for structures of peptides with antihypertensive activity. Therefore, the presence of aromatic amino acids in the peptide fractions obtained increases the likelihood of finding peptides with such activity in refrigerated commercial fermented milk. In conclusion, during cold storage, peptides with different molecular weights are released and accumulated. This could be due to the action of proteinases and peptidases of the proteolytic system in lactic acid bacteria.
publishDate 2014
dc.date.none.fl_str_mv 2014-12-01
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=S0101-20612014000400005
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612014000400005
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/1678-457X.6415
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.34 n.4 2014
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
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