Short communication: Identification of iron-binding peptides from whey protein hydrolysates using iron (III)-immobilized metal ion affinity chromatographyand reversed phase-HPLC-tandem mass spectrometry
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.
Main Authors: | , , , , , , |
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Other Authors: | |
Format: | artículo biblioteca |
Published: |
Elsevier
2016
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Subjects: | Reversed phase HPLC-tandem mass spectrometry, Enzymatic hydrolysis, Whey protein, Iron-binding peptide, |
Online Access: | http://hdl.handle.net/10261/150457 http://dx.doi.org/10.13039/501100004848 http://dx.doi.org/10.13039/501100003329 http://dx.doi.org/10.13039/501100000780 http://dx.doi.org/10.13039/501100001807 http://dx.doi.org/10.13039/501100003141 http://dx.doi.org/10.13039/501100010801 |
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