The antioxidative properties of hen egg phosvitin hydrolysate preparations were studied. Hydrolysis was performed using the bovine trypsin and protease from A. melleus. The progress and kinetics of the hydrolysis were analyzed by monitoring the degree of hydrolysis (DH), free amino group content and the RP-HPLC profiles of resulted peptides. The radical scavenging capacity on DPPH, ferric reducing activity (FRAP) and chelating activity on iron (II) were measured. The degrees of hydrolysis of final hydrolysates were 33,7% and 23,2% for protease from A. melleus and trypsin, respectively. The progress of reaction was also confirmed by determination of the free amino group content, which finally reached 3816 μM · g^-1 and 1198,5 μM · g^-1 for protease from A. melleus and trypsin. The twenty four-hour tryptic hydrolysate (0,27 μM Trolox · mg^-1) exhibited stronger scavenging activity on DPPH free radicals than that of protease from A. melleus (0,21 μM Trolox · mg-1). The hydrolysates exhibited also very strong chelating activity on iron (II). The hydrolysate with protease from A. melleus (24 -h) showed the highest level of this activity: 1466,3 μg Fe2+ · mg-1.

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