Antioxidant Activity of Egg Yolk Protein Hydrolysates Obtained by Enzymatic and Sub-Critical Water Hydrolysis

Obtaining peptides with antioxidant properties by enzymatic hydrolysis has been widely described; however, the use of non-enzymatic methods to obtain peptides with antioxidant capacities has been poorly investigated. In this study, non-soluble proteins obtained from delipidated egg yolk granules were hydrolyzed with trypsin, and with a non-enzymatic method using sub-critical water hydrolysis under a non-oxidizing (nitrogen) and oxidizing (oxygen) atmosphere. The effect of the sub-critical water hydrolysis on the amino acids' composition of the hydrolysates was assessed. Furthermore, the antioxidant capacities of the hydrolysates were evaluated using the ABTS center dot+ scavenging assay, the DPPH radical scavenging activity assay, and by measuring the reducing power of the peptides, the peptides' ferrous ion chelating capacities, and the antioxidant effect of the peptides on beef homogenates. The hydrolysate obtained by sub-critical water hydrolysis under a nitrogen stream showed similar or better results in the antioxidant tests than those obtained using trypsin hydrolysis, except in the ferrous chelating capacity, where the trypsin hydrolysate showed the best performance. The oxidizing environment promoted by the oxygen in the other sub-critical water hydrolysis method tested produced the peptides with the lowest antioxidant capacities, due to changes in the primary structure of the peptides. These results suggest that the sub-critical water hydrolysis method under a nitrogen stream, in comparison with the enzymatic hydrolysis, is a reliable method to obtain peptides with good antioxidant capacities.