Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry
Autor(a) principal: | |
---|---|
Data de Publicação: | 2016 |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório do Instituto de Tecnologia de Alimentos |
Texto Completo: | http://repositorio.ital.sp.gov.br/jspui/handle/123456789/160 |
Resumo: | Peptides with iron-binding capacity obtained by hydrolysis of whey protein with Alcalase (Novozymes, Araucaria, PR, Brazil), pancreatin, and Flavourzyme (Novozymes) were identified. Hydrolysates were subjected to iron (III)-immobilized metal ion affinity chromatography, and the bound peptides were sequenced by mass spectrometry. Regardless of the enzyme used, the domains f(42–59) and f(125–137) from β-lactoglobulin enclosed most of identified peptides. This trend was less pronounced in the case of peptides derived from α-lactalbumin, with sequences deriving from diverse regions. Iron-bound peptides exhibited common structural characteristics, such as an abundance of Asp, Glu, and Pro, as revealed by mass spectrometry and AA analysis. In conclusion, this characterization of ironbinding peptides helps clarify the relationship between peptide structure and iron-chelating activity and supports the promising role of whey protein hydrolysates as functional ingredients in iron supplementation treatments. |
id |
ITAL-2_756b85c8cab70af4840266da65b129c2 |
---|---|
oai_identifier_str |
oai:http://repositorio.ital.sp.gov.br:123456789/160 |
network_acronym_str |
ITAL-2 |
network_name_str |
Repositório do Instituto de Tecnologia de Alimentos |
repository_id_str |
|
spelling |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometryWhey proteinEnzymatic hydrolysisIronbinding peptidePeptides with iron-binding capacity obtained by hydrolysis of whey protein with Alcalase (Novozymes, Araucaria, PR, Brazil), pancreatin, and Flavourzyme (Novozymes) were identified. Hydrolysates were subjected to iron (III)-immobilized metal ion affinity chromatography, and the bound peptides were sequenced by mass spectrometry. Regardless of the enzyme used, the domains f(42–59) and f(125–137) from β-lactoglobulin enclosed most of identified peptides. This trend was less pronounced in the case of peptides derived from α-lactalbumin, with sequences deriving from diverse regions. Iron-bound peptides exhibited common structural characteristics, such as an abundance of Asp, Glu, and Pro, as revealed by mass spectrometry and AA analysis. In conclusion, this characterization of ironbinding peptides helps clarify the relationship between peptide structure and iron-chelating activity and supports the promising role of whey protein hydrolysates as functional ingredients in iron supplementation treatments.99177822021-09-16T19:51:45Z2021-09-16T19:51:45Z2016info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfJournal of Dairy Science, Champaign, v. 99, n. 1, p. 77-82, 2016. http://dx.doi.org/10.3168/jds.2015-9839http://repositorio.ital.sp.gov.br/jspui/handle/123456789/160Cruz-Huerta, Elvia; et. al.engreponame:Repositório do Instituto de Tecnologia de Alimentosinstname:Instituto de Tecnologia de Alimentos (ITAL)instacron:ITALinfo:eu-repo/semantics/openAccess2022-06-28T20:14:17Zoai:http://repositorio.ital.sp.gov.br:123456789/160Repositório InstitucionalPUBhttp://repositorio.ital.sp.gov.br/oai/requestbjftsec@ital.sp.gov.br || bjftsec@ital.sp.gov.bropendoar:2022-06-28T20:14:17Repositório do Instituto de Tecnologia de Alimentos - Instituto de Tecnologia de Alimentos (ITAL)false |
dc.title.none.fl_str_mv |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
title |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
spellingShingle |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry Cruz-Huerta, Elvia; et. al. Whey protein Enzymatic hydrolysis Ironbinding peptide |
title_short |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
title_full |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
title_fullStr |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
title_full_unstemmed |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
title_sort |
Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatography and reversed phase-HPLC-tandem mass spectrometry |
author |
Cruz-Huerta, Elvia; et. al. |
author_facet |
Cruz-Huerta, Elvia; et. al. |
author_role |
author |
dc.contributor.author.fl_str_mv |
Cruz-Huerta, Elvia; et. al. |
dc.subject.por.fl_str_mv |
Whey protein Enzymatic hydrolysis Ironbinding peptide |
topic |
Whey protein Enzymatic hydrolysis Ironbinding peptide |
description |
Peptides with iron-binding capacity obtained by hydrolysis of whey protein with Alcalase (Novozymes, Araucaria, PR, Brazil), pancreatin, and Flavourzyme (Novozymes) were identified. Hydrolysates were subjected to iron (III)-immobilized metal ion affinity chromatography, and the bound peptides were sequenced by mass spectrometry. Regardless of the enzyme used, the domains f(42–59) and f(125–137) from β-lactoglobulin enclosed most of identified peptides. This trend was less pronounced in the case of peptides derived from α-lactalbumin, with sequences deriving from diverse regions. Iron-bound peptides exhibited common structural characteristics, such as an abundance of Asp, Glu, and Pro, as revealed by mass spectrometry and AA analysis. In conclusion, this characterization of ironbinding peptides helps clarify the relationship between peptide structure and iron-chelating activity and supports the promising role of whey protein hydrolysates as functional ingredients in iron supplementation treatments. |
publishDate |
2016 |
dc.date.none.fl_str_mv |
2016 2021-09-16T19:51:45Z 2021-09-16T19:51:45Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/article |
format |
article |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
Journal of Dairy Science, Champaign, v. 99, n. 1, p. 77-82, 2016. http://dx.doi.org/10.3168/jds.2015-9839 http://repositorio.ital.sp.gov.br/jspui/handle/123456789/160 |
identifier_str_mv |
Journal of Dairy Science, Champaign, v. 99, n. 1, p. 77-82, 2016. http://dx.doi.org/10.3168/jds.2015-9839 |
url |
http://repositorio.ital.sp.gov.br/jspui/handle/123456789/160 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
dc.source.none.fl_str_mv |
reponame:Repositório do Instituto de Tecnologia de Alimentos instname:Instituto de Tecnologia de Alimentos (ITAL) instacron:ITAL |
instname_str |
Instituto de Tecnologia de Alimentos (ITAL) |
instacron_str |
ITAL |
institution |
ITAL |
reponame_str |
Repositório do Instituto de Tecnologia de Alimentos |
collection |
Repositório do Instituto de Tecnologia de Alimentos |
repository.name.fl_str_mv |
Repositório do Instituto de Tecnologia de Alimentos - Instituto de Tecnologia de Alimentos (ITAL) |
repository.mail.fl_str_mv |
bjftsec@ital.sp.gov.br || bjftsec@ital.sp.gov.br |
_version_ |
1798311819117330432 |