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Affinity Purification of Copper-Chelating Peptides from Sunflower Protein Hydrolysates

AuthorsMegías, Cristina ; Pedroche, Justo ; Yust, María del Mar ; Girón-Calle, Julio ; Alaíz Barragán, Manuel ; Millán, Francisco ; Vioque, Javier
KeywordsChelating peptides
Protein hydrolysate
Issue Date2007
PublisherAmerican Chemical Society
CitationJournal of Agricultural and Food Chemistry 55(16): 6509-6514 (2007)
AbstractCopper-chelating peptides were purified from sunflower protein hydrolysates by affinity chromatography using immobilized copper. A variety of protein hydrolysates were obtained by incubation with the proteases Alcalase and Flavourzyme for different periods of time. Chelating activity was indirectly determined by measuring the inhibitory effect of hydrolysates on the oxidation of β-carotene by copper. Copper-binding peptides purified from the two hydrolysates that inhibited oxidation by copper the most contained 25.4 and 42.0% histidine and inhibited β-carotene oxidation 8 and 3 times more than the original hydrolysates, which had 2.4 and 2.6% histidine, respectively. Thus, histidine content is not the only factor involved in antioxidant activity, and probably other factors such as peptide size and amino acid sequence are also important. This work shows that affinity chromatography can be used for the purification of copper-chelating peptides and probably other metals of nutritional interest such as calcium, iron, and zinc. In addition to their antioxidant potential, chelating peptides are of nutritional interest because they increase bioavailability of minerals.
Description6 páginas, 8 figuras, 1 tabla.
Publisher version (URL)http://dx.doi.org/10.1021/jf0712705
Appears in Collections:(IG) Artículos
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