Suchergebnisse

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. ; This work received financial support from projects AGL2011-24643 from the Ministerio de Economía y Competitividad of Spain; CONETA-PEME IN852A 2013/39-0 from Xunta de Galicia of Spain; FP7-SME-2012-315349 (FOFIND) from the European Union; Fundaçao de Amparo a Pesquisa de Sao Paulo, Brazil; and IBEROFUN 110AC0386 from Programa Iberoamericano de Ciencia y Tecnología para el Desarrollo. E. C.-H. thanks the Universidad Veracruzana and the Program for the Improvement of Teaching (PROMEP) of México for awarding the scholarship for supporting PhD studies abroad. ; Peer Reviewed