Lipid oxidation protein hydrolysates

Zhang, X., Xiong, Y.L., Chen, J., Zhou, L., 2013. Synergistic inhibition of lipid oxidation by pea protein hydrolysate coupled with licorice extract in a liposomal model system. Journal of Agricultural and Food Chemistry 61, 8452—8461. 

Antioxidative activities of the hydrolysates from porcine myofibrillar protein were measured in a linolenic acid oxidation system The hydrolysates at the concentration of 0.02, 0.2 and 2% exhibited antioxidative activities. All hydrolysates exhibited stronger antioxidative activity, as the concentration was higher in the production of hydroperoxides. On the other hand, the addition of 0.2% hydrolysate suppressed the production of TEARS most strongly, and the antioxidative activity in the addition of 2% hydrolysate was lower than that of 0.2% in the method of TEARS. It is well known that 2-thiobarbituric acid (TEA) reacts with aldehyde compounds including malondialdehyde (MDA) formed by Upid peroxidation. Two percent hydrolysates contained a lot of amino confounds including free amino acids and peptides. Therefore, the production of aldehyde compounds seems to be accelerated by amino-carbonyl reaction between hydrolysate and lipid in lipid peroxidation system including 2% hydrolysate. This might be the reason why the antioxidative activity of 2% hydrolysate was lower than that of 0.2 % hydrolysate in the method of TEARS. 

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