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Protease hydrolysis porcine haemoglobin(Hb) , purification of heme peptide i ron, prediction of the molecular structure and function activity were carried out to evaluate the trypsin digestion properties of porcine haemoglobin on pulsed electric field (PEF) un der the condition of vacuum, leaded to massive release kinds of heme peptide-iron, and a kind of heme peptide-iron was separated using metal chelate affinity chromatography (MCAC).The results suggested that the cleavage effect on trypsin of hydrolysis haemo globin at 37 ℃C for 4 hours on the PEF was better than that of the single trypsin without PEF or under vacuum, Which compare with SDS-PAGE electrophoresis and high perform ance gel chromatography (HPGC).The molecular structure and function activity of heme peptide-iron was predicted that the molecular weight was 16 065.08 Da, theoretical isoe lectric point was 8.10, extinction coefficient was 6990 by way of MALDI-TOF MS and World Wide Web server, such as www.Expasy.org.