Affinity Purification of Copper Chelating Peptides from Chickpea Protein Hydrolysates
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Chickpea protein hydrolysates obtained with alcalase and flavourzyme were used for purification ofcopper chelating peptides by affinity chromatography using copper immobilized on solid supports.The chelating activity of purified peptides was indirectly measured by the inhibition of ges/gifchars/beta2.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 ges/gifchars/beta2.gif" BORDER=0 ALIGN="middle">-carotene oxidation. Purified copper chelating peptides fromthese protein hydrolysates contained 19.7 and 35.1% histidine, respectively, in comparison to 2.7and 2.6% in the protein hydrolysates. Chelating peptides from hydrolysate obtained after 10 min ofhydrolysis were the most antioxidative being 8.3 times more antioxidative than the hydrolysate, whilechelating peptides purified from protein hydrolysate obtained after 100 min were 3.1 times moreantioxidative than its hydrolysate. However, the histidine content was higher in peptides derived fromthe 100 min hydrolysate (19.7 against 35.1% in 10 min hydrolysate), indicating 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 chromatography is auseful procedure for purification of copper chelating peptides. This method can be extended to othermetals of interest in nutrition, such as calcium, iron, or zinc. Purified chelating peptides, in additionto their antioxidative properties, may also be useful in food mineral fortification for increasing thebioavailability of these metals.

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