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

European Food Research and Technology volume 232, pages 637–646 (2011)Cite this article

Abstract

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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Abbreviations

ESI/MS:

Electrospray ionization mass spectrometry

ESI/MS/MS:

Electrospray ionization tandem mass spectrometry

RP-HPLC:

Reversed-phase high-performance liquid chromatography

DH:

Degree of hydrolysis

HHL:

Hippuryl-l-histidyl-l-leucine

HA:

Hippuric acid

ACE:

Angiotensin I-converting enzyme

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Acknowledgments

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

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Authors and Affiliations

  1. Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien, IUT «A» Polytech’Lille -Lille I, BP 179, 59653, Villeneuve d’Ascq Cedex, France

    Estelle Yaba Adje, Rafik Balti, Didier Guillochon & Naïma Nedjar-Arroume

  2. Laboratoire de Génie Enzymatique et de Microbiologie, Ecole Nationale d’Ingénieurs de Sfax, B.P. “1173”, 3038, Sfax, Tunisia

    Rafik Balti

  3. Laboratoire d’Application de Spectrométrie de Masse, Service Commun de Physicochimie, Faculté de Médecine H. Warembourg, Pôle Recherche, Place de Verdun, Lille II, France

    Mostafa kouach

Authors
  1. Estelle Yaba Adje
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  2. Rafik Balti
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  3. Mostafa kouach
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  4. Didier Guillochon
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  5. Naïma Nedjar-Arroume
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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). https://doi.org/10.1007/s00217-011-1430-z

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  • DOI: https://doi.org/10.1007/s00217-011-1430-z

Keywords

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