Inhibition of lipid oxidation in cooked beef patties by hydrolyzed potato protein is related to its reducing and radical scavenging ability.

Protein hydrolysates were prepared by limited alcalase hydrolysis (0.5, 1, and 6 h, corresponding to degrees of hydrolysis of 0.72, 1.9, and 2.3, respectively) of heat-coagulated potato protein. The hydrolysates were characterized for peptide composition, ferric reducing/antioxidant power (FRAP), 2,2'-azinobis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical-scavenging activity, and Fe2+- and Cu2+-chelation capacity. Hydrolyzed and intact proteins were formulated (4%, w/w) into beef patties to determine in situ antioxidant efficacy. Thiobarbituric acid-reactive substances (TBARS) and peroxide value (PV) formed in cooked and PVC-packaged patties during storage (4 degrees C, 0-7 days) were analyzed. Hydrolysis increased the protein solubility by 14-19-fold and produced numerous short peptides (< 6 kDa). The FRAP values of the protein sample (23 micromol/g) increased markedly after hydrolysis but were similar between the three hydrolysates (597-643 micromol/g). Similarly, the ABTS radical-scavenging activity also was increased by hydrolysis and was the greatest for the 1-h hydrolysate. Hydrolysis increased the Cu2+-chelation activity but decreased the Fe2+-chelation ability of the protein. The production of PV in patties after 7 days of storage was lowered 44.9% and 74.5% (P < 0.05), and that of TBARS was reduced 40.9% and 50.3% (P < 0.05), by intact and hydrolyzed proteins, respectively.