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α 67-106 of bovine hemoglobin: a new family of antimicrobial and angiotensin I-converting enzyme inhibitory peptides


Protein hydrolysates are of a significant interest, due to their potential application as a source of bioactive peptides in nutraceutical and pharmaceutical domains. The present study was focused on bovine hemoglobin hydrolysate obtained with pig pepsin in the presence of 30% ethanol. This hydrolysate was fractioned by reversed-phase high-performance liquid chromatography (RP-HPLC) into 12 major fractions (F1–F12). All fractions were analyzed by ESI/MS and ESI/MS/MS, in order to characterize and identify the peptides in these fractions. This hydrolysis permitted to generate a new serial of bioactive peptides with both antimicrobial and ACE inhibitory activities. Identified peptides were TKAVEHLDDLPGALSELSDLHAHKLRVDPVNFKLLSHSLL, LDDLPGALSELSDLHAHKLRVDPVNFKLLSHSL, KLLSHSL, and LLSHSL corresponding respectively to the 67-106, 73-105, 99-105, and 100-105 fragments of the α chain of bovine hemoglobin. They were the first found from bovine hemoglobin. These purified peptides have an antibacterial activity against four bacteria strains: Kocuria luteus A270, Listeria innocua, Escherichia coli, and Staphylococcus aureus with a MIC between 187.1 and 35.2 μM. On the other hand, these peptides displayed at the same time ACE inhibitory activity with an IC50 range from 42.55 to 1,095 μM.

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Electrospray ionization mass spectrometry


Electrospray ionization tandem mass spectrometry


Reversed-phase high-performance liquid chromatography


Degree of hydrolysis




Hippuric acid


Angiotensin I-converting enzyme


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This work was supported by the University of Lille I. Estelle Yaba Adje has a fellowship from Ivorian government.

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Correspondence to Rafik Balti.

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Adje, E.Y., Balti, R., kouach, M. et al. α 67-106 of bovine hemoglobin: a new family of antimicrobial and angiotensin I-converting enzyme inhibitory peptides. Eur Food Res Technol 232, 637–646 (2011).

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  • Bovine hemoglobin
  • Hydrolysis
  • Antimicrobial peptides
  • ACE inhibitory activity