The aim of this work was to study the suitability of camel milk for the production of dairy products by lactic acid fermentation. Sixty strains of lactic acid bacteria (LAB) were isolated from camel milk. The strains were tested for their acidification activity, ability to use citrate, exopolysaccharide production, lipolytic, proteolytic activities and resistance to antibiotics. Ten strains were investigated for their ability to metabolize carbohydrates and that resulted in the identification of 5 Lactococcus lactis, 1 Lactobacillus pentosus, 2 Lactobacillus plantarum, 1 Lactobacillus brevis and 1 Pediococcus pentosaceus strains. Two strains of Lactococcus lactis SCC133 and SLch14 were selected to produce traditional Tunisian fermented dairy products (Lben, Raib, Jben cheese and Smen). These strains were chosen based on their acid production capacity and their ability to produce a high yield of biomass.

The transformation of camel milk into cheese is an operation considered very delicate because of several difficulties encountered in achieving coagulation. The present study aims to improve coagulation abilities of camel milk using enzyme extracts from pineapple, kiwi, and ginger. Our results concerning the characterization of the enzymatic extract showed an extraction yield that varies according to the type of extract (pineapple: 75.28% ± 4.59, kiwi: 63.97% ± 5.22, and ginger: 28.64% ± 1.47). The optimum coagulation conditions of the 3 types of extract were as follows: for pineapple: pH = 5 and temperature = 45°C; for kiwifruit: pH = 6.6 and temperature = 40°C; and for ginger: pH = 6.6 and temperature = 45°C. A fresh cheese was made from camel milk with a particular nutritional quality and consistency. The kiwi proteases displayed chymosin-like properties and thus hold the best potential for use as a milk coagulant in cheese production.

The aim of this study was to explore the antibacterial peptides derived from dromedary lactoferrin (LFc). The LFc was purified from colostrum using a batch procedure with a cation exchange chromatography support and was hydrolyzed with pepsin to generate peptic digest. This peptic digest was fractionated by cation exchange chromatography, and the antilisterial activity of LFc, peptic digest, and obtained fractions was investigated using the bioscreen method. The growth of Listeria innocua ATCC 33090 and LRGIA 01 strains was not inhibited by LFc and its hydrolysates. Two fractions of dromedary lactoferrin peptic hydrolysate were active against both strains. A tandem mass spectroscopy analysis revealed that the 2 active fractions comprised at least 227 different peptides. Among these peptides, 9 found in the first fraction had at least 50% similarity with 10 known antimicrobial peptides (following sequence alignments with the antimicrobial peptide database from the University of Nebraska Medical Center, Omaha). Whereas 9 of these peptides presented homology with honeybee, frog, or amphibian peptides, the 10th peptide, F 152 SASCVPCVDGKEYPNLCQL-CAGTGENKCACSSQEPYFGY 192 (specifically found in 1 separated fraction), exibited 54% homology with a synthetic antibacterial peptide (AP00481) derived from human lactoferrin named kaliocin-1. Similarly, the second fraction contained 1 peptide similar to lactoferrampin B, an antibacterial peptide derived from bovine milk. This result suggests that peptic hydrolysis of LFc releases more active antimicrobial peptides than their protein source and thus provides an opportunity for their potential use to improve food safety by inhibiting undesirable and spoilage bacteria.

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