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The porcine cruor represents a co-product from slaughterhouses. It mainly contains hemoglobin which is rich in bioactive peptides obtained by hydrolysis by porcine pepsin. The aim of this study is to valorize this new source rich of bioactive peptides to be used as feed additives. An in silico study on the potential of porcine cruor to contain bioactive peptides was studied by comparing it with peptides derived from bovine hemoglobin. The blast results showed a high similarity between porcine cruor hydrolysate peptides and bovine hemoglobin hydrolysates for both α and β chains with identities of 87% and 83% respectively. Cleavage sites of porcine cruor were also predicted using Peptide Cutter software and compared with bovine hemoglobin. Results reveal the preservation of most of peptides of porcine cruor hydrolysates comparing to bovine hemoglobin hydrolysates. The presence of bioactive peptides was then determined by mass spectrometry analysis. Results showed the presence of 37 bioactive peptides defined by their sequences found in previous study with mainly antibacterial and opioid peptides. The antibacterial activity was then verified by in vitro analysis against 4 bacterial strains. Results showed interesting MIC values comparing with tested synthetic peptides (4.53 µM for M.luteus and L.innocua, 35.94 µM for E.coli and 312 µM for S.newport). The antioxidant activity was also verified by studying DPPH•+ trapping and results showed an antiradical activity for porcine cruor hydrolysate greater than neokyotorphin which was previously validated as a natural preservative to substitute synthetic additives against food alteration (14% and 10% respectively). These similarities of porcine cruor hydrolysate in peptic profiles as well as biological activities make it a new interesting source of bioactive peptides.

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