Mustapha Mbye

The camel milk (CM) industry has witnessed a notable expansion in recent years. This expansion is primarily driven by the rising demand for CM and its fermented products. The perceived health and nutritional benefits of these products are mainly responsible for their increasing popularity. The composition of CM can vary significantly due to various factors, including the breed of the camel, its age, the stage of lactation, region, and season. CM contains several beneficial substances, including antimicrobial agents, such as lactoferrin, lysozyme, immunoglobulin G, lactoperoxidase, and N-acetyl-D-glucosaminidase, which protect it from contamination by spoilage and pathogenic bacteria, and contribute to its longer shelf life compared to bovine milk (BM). Nevertheless, certain harmful bacteria, such as Listeria monocytogenes, Yersinia enterocolitica, and Escherichia coli, have been detected in CM, which is a significant public health concern. Therefore, it is crucial to understand and monitor the microbial profile of CM and follow good manufacturing practices to guarantee its safety and quality. This review article explores various aspects of CM, including the types of beneficial and harmful bacteria present in it, the composition of the milk, its antimicrobial properties, its shelf life, and the production of fermented CM products.

The milk of mammals is a complex fluid mixture of various proteins, minerals, lipids, and other micronutrients that play a critical role in providing nutrition and immunity to newborns. Casein proteins together with calcium phosphate form large colloidal particles, called casein micelles. Caseins and their micelles have received great scientific interest, but their versatility and role in the functional and nutritional properties of milk from different animal species are not fully understood. Caseins belong to a class of proteins that exhibit open and flexible conformations. Here, we discuss the key features that maintain the structures of the protein sequences in four selected animal species: cow, camel, human, and African elephant. The primary sequences of these proteins and their posttranslational modifications (phosphorylation and glycosylation) that determine their secondary structures have distinctively evolved in these different animal species, leading to differences in their structural, functional, and nutritional properties. The variability in the structures of milk caseins influence the properties of their dairy products, such as cheese and yogurt, as well as their digestibility and allergic properties. Such differences are beneficial to the development of different functionally improved casein molecules with variable biological and industrial utilities.