CURRENT KNOWLEDGE AND FUTURE PERSPECTIVES ON CHICKPEA PROTEIN-DERIVED METAL-CHELATING PEPTIDES
Abstract
Chickpea (Cicer arietinum L.) is a valuable plant protein source containing peptides that can interact with metal ions and can serve as a functional ingredient for mineral supplementation. This review summarizes the literature on metal-chelating peptides and peptide-metal complexes obtained from chickpea protein hydrolysates, focusing on their enzymatic production, purification, structural properties, metal-binding, and biological activity. Initial studies focused on copper-chelating peptides. Chickpea protein hydrolysates prepared using Alcalase® and Flavourzyme® were subjected to copper affinity chromatography, resulting in peptide fractions with high CuІ⁺ ion chelation and antioxidant activity. It was found that the purified fractions were rich in histidine, and that peptide size and amino acid sequence also affected the activity. Subsequent hydrolysis with pepsin and pancreatin followed by affinity and gel-filtration chromatography demonstrated particularly high CuІ⁺-chelating activity in small peptides containing approximately 20-30% histidine. Similar approaches were subsequently applied to iron, with purified chickpea peptide fractions exhibiting enhanced Fe-chelating activity, particularly in fractions containing more than 20% histidine.
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