title: Iron-chelating activity of chickpea protein hydrolysate peptides.
abstract: Chickpea-chelating peptides were purified and analysed for their iron-chelating activity. These peptides were purified after affinity and gel filtration chromatography from a chickpea protein hydrolysate produced with pepsin and pancreatin. Iron-chelating activity was higher in purified peptide fractions than in the original hydrolysate. Histidine contents were positively correlated with the iron-chelating activity. Hence fractions with histidine contents above 20% showed the highest chelating activity. These results show that iron-chelating peptides are generated after chickpea protein hydrolysis with pepsin plus pancreatin. These peptides, through metal chelation, may increase iron solubility and bioavailability and improve iron absorption.
authors.affiliation: Instituto de la Grasa (CSIC), Avda. Padre García Tejero 4, 41012-Sevilla, Spain.
authors.forename: Cristina
authors.initials: C
authors.lastname: Torres-Fuentes
authors.forename: Manuel
authors.initials: M
authors.lastname: Alaiz
authors.forename: Javier
authors.initials: J
authors.lastname: Vioque
mesh_terms: D029863:Cicer / Q000737:chemistry*; D007501:Iron / Q000737:chemistry*; D007502:Iron Chelating Agents; D010455:Peptides / Q000737:chemistry*; D011492:Protein Hydrolysates / Q000737:chemistry*
chemical_list: D007502:Iron Chelating Agents; D010455:Peptides; D011492:Protein Hydrolysates; D007501:Iron