Author(s): Caetano-Silva, Maria Elisa ; Alves, Renata Carolina [UNESP] ; Lucena, Guilherme Nunes [UNESP] ; Frem, Regina Célia Galvão [UNESP] ; Bertoldo-Pacheco, Maria Teresa ; Lima-Pallone, Juliana Azevedo ; Netto, Flavia Maria
Date: 2018
Persistent ID: http://hdl.handle.net/11449/170094
Origin: Oasisbr
Subject(s): Coordination compounds; Food fortification; Infrared spectroscopy; Iron salts; Iron-binding peptides; Whey protein hydrolysate
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Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Iron-binding peptides are an alternative for increasing the bioavailability of iron and to decreasing its pro-oxidant effect. This study aimed to synthesize and characterize peptide-iron complexes using FeCl2 or FeSO4 as the iron precursor compounds. Whey protein isolate (WPI), WPI hydrolyzed with pancreatin, and its fractions obtained via ultrafiltration (cut-off 5 kDa) were used as ligands. The fluorescence intensity of the ligands significantly decreased as the iron concentration increased as a result of metal coordination with the iron-binding sites, which may have led to changes in the microenvironment of tryptophan. For both iron precursor compounds, the primary iron-binding site was carboxylate groups, and the linkage occurred via a bidentate coordination mode with two vibrational modes assigned to the COO–Fe linkage. However, infrared spectroscopy and thermal analysis results showed that the dynamics of the interaction is different for the iron precursor. The iron source may be of great importance because it may impact iron absorption and the pro-oxidant effect of the mineral.
Faculty of Food Engineering University of Campinas UNICAMP, Monteiro Lobato 80
Institute of Chemistry São Paulo State University UNESP, Prof. Francisco Degni 55, PO Box 355
Center of Food Science and Quality Institute of Food Technology ITAL, Brasil Ave 2880
Institute of Chemistry São Paulo State University UNESP, Prof. Francisco Degni 55, PO Box 355
FAPESP: 2013/10356-7
