2016
Cruz-Huerta, Elvia; Maqueda, Daniel Martínez; de la Hoz, Lucia; da Silva, Vera S Nunes; Pacheco, Maria Teresa Bertoldo; Amigo, Lourdes; Recio, Isidra
En: J Dairy Sci, vol. 99, no 1, pp. 77–82, 2016, ISSN: 1525-3198.
Resumen | Enlaces | BibTeX | Etiquetas: enzymatic hydrolysis, iron-binding peptide, reversed phase HPLC-tandem mass spectrometry, Whey protein
@article{pmid26601589,
title = {Short communication: 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 = {Elvia Cruz-Huerta and Daniel Martínez Maqueda and Lucia de la Hoz and Vera S Nunes da Silva and Maria Teresa Bertoldo Pacheco and Lourdes Amigo and Isidra Recio},
doi = {10.3168/jds.2015-9839},
issn = {1525-3198},
year = {2016},
date = {2016-01-01},
urldate = {2016-01-01},
journal = {J Dairy Sci},
volume = {99},
number = {1},
pages = {77--82},
abstract = {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 iron-binding 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. },
keywords = {enzymatic hydrolysis, iron-binding peptide, reversed phase HPLC-tandem mass spectrometry, Whey protein},
pubstate = {published},
tppubtype = {article}
}
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 iron-binding 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.
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