Chickpea protein hydrolysates obtained with alcalase and flavourzyme were used for purification ofcopper chelatin
g peptides by affinity chromato
graphy usin
g copper immobilized on solid supports.The chelatin
g activity of purified peptides was indirectly measured by the inhibition of
![](/ima<font color=)
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gif" BORDER=0 ALIGN="middle">-caroteneoxidation in the presence of copper. Two protein hydrolysates, obtained after 10 and 100 min ofhydrolysis, were the most inhibitory of
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gif" BORDER=0 ALIGN="middle">-carotene oxidation. Purified copper chelatin
g peptides fromthese protein hydrolysates contained 19.7 and 35.1% histidine, respectively, in comparison to 2.7and 2.6% in the protein hydrolysates. Chelatin
g peptides from hydrolysate obtained after 10 min ofhydrolysis were the most antioxidative bein
g 8.3 times more antioxidative than the hydrolysate, whilechelatin
g peptides purified from protein hydrolysate obtained after 100 min were 3.1 times moreantioxidative than its hydrolysate. However, the histidine content was hi
gher in peptides derived fromthe 100 min hydrolysate (19.7 a
gainst 35.1% in 10 min hydrolysate), indicatin
g that this amino acidis not the only factor involved in the antioxidative activity, and other factors such as peptide size oramino acid sequence are also determinant. This manuscript shows that affinity chromato
graphy is auseful procedure for purification of copper chelatin
g peptides. This method can be extended to othermetals of interest in nutrition, such as calcium, iron, or zinc. Purified chelatin
g peptides, in additionto their antioxidative properties, may also be useful in food mineral fortification for increasin
g thebioavailability of these metals.