The enzymatic hydrolysate, which was rich in ferrous peptides, were reacted with FeCl2 at a ratio of 2:1 in a water bath at 50 ℃ for 1 h in the presence of antioxidants, then the mixtures were centrifuged at 15000 r/min for 10 min and the supernatant was precipitated by ethanol. The precipitate was washed several times by ethanol, followed by a vacuum dry. Ferrous peptides were obtained with content of total iron being of 127.34 mg/g (heme-enriched peptide), 128.70 mg/g (permeate peptide) and 47.83 mg/g (retentate peptide), respectively. The structure of the new compound was identified by Infrared spectrometry. It was also found that oxidation stability of ferrous heme-enriched peptide was higher than that of FeCl2 but lower than that of heme-enriched peptide or permeate peptide.