Antibacterial activity of new peptide from bovine casein hydrolyzed by a serine metalloprotease of Lactococcus lactis subsp lactis BR16

Journal of Functional Foods

Abdelkader Dilmi-Bouras¹  Christophe Flahaut²  Nedjar Naima²  Faiza Adoui²  Pascal Dhulster²  Hacene Elhameur³  Fateh Bougherra⁴  Rafik Balti⁴  Mickaël Chevalier⁴  Rémi Przybylski⁵ 

[1]Corresponding author.

[2]Institut Charles Viollette, équipe ProBioGEM, Polytech’Lille, Boulevard Paul Langevin, 59655 Villeneuve d’Ascq, France

[3]Institut de la Nutrition de l’Alimentation et des Technologies Agro-alimentaires (I.N.A.TA.A.), 25000 Constantine, Algeria

[4]Laboratoire de Bio-ressources Naturelles, Université Hassiba Benbouali de Chlef, BP 151, Hay Salem, 02000 Chlef, Algeria

[5]Laboratoire d’Amélioration de Plantes et Valorisation des Agro-ressources (LAPVA), National School of Engineering, University of Sfax, Km 4 Road Soukra, 3038 Sfax, Tunisia

关键词: Serine metalloprotease;    Lactococcus lactis subsp lactis BR16;    Bovine casein;    Adsorption/desorption;    Antibacterial peptide;   

DOI  :  

来源: DOAJ

【 摘 要 】

An extracellular serine metalloprotease produced by Lactococcus lactis subsp lactis BR16 isolated from Algerian traditional fermented food was used for hydrolyzing bovine casein in order to identify antibacterial peptide. Antibacterial peptide was separated from peptic hydrolysates by adsorption/desorption then analyzed using reverse phase high performance liquid chromatography (RP-HPLC) and active fraction was analyzed by MALDI-TOF mass spectrometry. A new antibacterial peptide was identified as SSSEESII from the subunit αs2 of casein corresponding of the fragment (24–31). This peptide demonstrated antibacterial activity against two Gram-positive bacteria: Listeria innocua ATCC 33090 and Micrococcus luteus ATCC 4698, and two Gram-negative bacteria: Escherichia coli ATCC 25922 and Salmonella enteritidis ATCC13076. Prediction of peptide secondary structure indicated that this peptide is anionic and must have random coil structure with a small region of hydrophobicity, which confers to the peptide unusual behavior compared to conventional antimicrobial peptides.

【 授权许可】

Unknown