Production of copper-chelating peptides after hydrolysis of sunflower proteins with pepsin and pancreatin
2007; Elsevier BV; Volume: 41; Issue: 10 Linguagem: Inglês
10.1016/j.lwt.2007.11.010
ISSN1096-1127
AutoresCristina Megías, Justo Pedroche, María del Mar Yust, Julio Girón‐Calle, Manuel Alaiz, Francisco Millán, Javier Vioque,
Tópico(s)Meat and Animal Product Quality
ResumoSunflower protein hydrolysates obtained with pepsin and pancreatin were used for purification of copper-chelating peptides by affinity chromatography with copper immobilized on solid supports. The chelating activity of purified peptides was indirectly measured by the inhibition of β-carotene oxidation in the presence of copper. The protein hydrolysate obtained after 180 min incubation with pepsin plus 60 min with pancreatin was the most inhibitory of β-carotene oxidation. Purified chelating peptides were 2.5 times more antioxidant than the parent protein hydrolysate. Chelating peptides were enriched in certain amino acids, such as histidine and arginine, with respect to the original hydrolysate. This work shows that chelating peptides may be generated during digestion of sunflower proteins and have a protective role, due to their antioxidative activity, and favour mineral bioavailability.
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