European Food Research and Technology

, Volume 232, Issue 4, pp 637–646 | Cite as

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

  • Estelle Yaba Adje
  • Rafik Balti
  • Mostafa kouach
  • Didier Guillochon
  • Naïma Nedjar-Arroume
Original Paper


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.


Bovine hemoglobin Hydrolysis Antimicrobial peptides ACE inhibitory activity 



Electrospray ionization mass spectrometry


Electrospray ionization tandem mass spectrometry


Reversed-phase high-performance liquid chromatography


Degree of hydrolysis




Hippuric acid


Angiotensin I-converting enzyme



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


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Copyright information

© Springer-Verlag 2011

Authors and Affiliations

  • Estelle Yaba Adje
    • 1
  • Rafik Balti
    • 1
    • 2
  • Mostafa kouach
    • 3
  • Didier Guillochon
    • 1
  • Naïma Nedjar-Arroume
    • 1
  1. 1.Laboratoire de Procédés BiologiquesGénie Enzymatique et MicrobienVilleneuve d’Ascq CedexFrance
  2. 2.Laboratoire de Génie Enzymatique et de MicrobiologieEcole Nationale d’Ingénieurs de SfaxSfaxTunisia
  3. 3.Laboratoire d’Application de Spectrométrie de Masse, Service Commun de Physicochimie, Faculté de Médecine H. WarembourgPôle RecherchePlace de Verdun, Lille IIFrance

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