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Updated: Jun 1, 2026

Bacterial Peptide Display for the Selection of Novel Biotinylating Enzymes
Published on: October 3, 2019
RYH: a minimal peptidic sequence obtained from beta-chain hemoglobin exhibiting an antimicrobial activity
Lucie Catiau1, Johnatan Traisnel, Nour-Eddine Chihib
1Laboratoire ProBioGEM, Bâtiment Polytech-Lille, Boulevard Paul Langevin, 59655 Villeneuve d'Ascq, France.
Abstract:
Bovine hemoglobin is an animal protein described as source of bioactive peptides. Enzymatic hydrolysis of this protein results into some peptides exhibiting antimicrobial activity against Gram-positive and Gram-negative bacteria. In this study, a family of peptides from the beta chain (beta-114-145 derived peptides) obtained by peptic hydrolysis of bovine hemoglobin, was purified by reverse-phase HPLC and characterized by different analytical techniques (mass spectrometry, circular dichroism). The minimum inhibitory concentration was determined to show the antimicrobial activity of these peptides. Four bacterial strains were used: two Gram-negative (Escherichia coli and Salmonella Enteritidis) and two Gram-positive strains (Listeria innocua and Micrococcus luteus). The effect of these peptides on artificial membrane was also measured. Our findings showed that the peptide β114-145 and its peptic derivatives contain the RYH sequence. The most antimicrobial peptide is the RYH peptide which was the shortest one.
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