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

• Published in: Journal of dairy science 2016-01, Vol.99 (1), p.77-82
• Main Authors: Cruz-Huerta, Elvia, Maqueda, Daniel Martínez, de la Hoz, Lucia, Nunes da Silva, Vera S., Pacheco, Maria Teresa Bertoldo, Amigo, Lourdes, Recio, Isidra
• Format: Article
• Language: English
• Subjects: enzymatic hydrolysis; iron-binding peptide; reversed phase HPLC-tandem mass spectrometry; whey protein
• ISSN: 0022-0302; 1525-3198
• DOI: 10.3168/jds.2015-9839

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.