This review summarises current knowledge on camel milk proteins, with focus on significant peculiarities in protein composition and molecular properties. Camel milk is traditionally consumed as a fresh or naturally fermented product. Within the last couple of years, an increasing quantity is being processed in dairy plants, and a number of consumer products have been marketed. A better understanding of the technological and functional properties, as required for product improvement, has been gained in the past years. Absence of the whey protein β-LG and a low proportion of к-casein cause differences in relation to dairy processing. In addition to the technological properties, there are also implications for human nutrition and camel milk proteins are of interest for applications in infant foods, for food preservation and in functional foods. Proposed health benefits include inhibition of the angiotensin converting enzyme, antimicrobial and antioxidant properties as well as an antidiabetogenic effect. Detailed investigations on foaming, gelation and solubility as well as technological consequences of processing should be investigated further for the improvement of camel milk utilisation in the near future.

αs1-, αs2-, β- and κ-caseins from Somali camels (Camelus dromedarius) were purified by acid precipitation at pH 4·4, crudely separated into an α-CN and a β-CN fraction and further purified by reversed-phase HPLC. Fragments of tryptic digests were sequenced. Amino acid patterns obtained were used to screen a cDNA library constructed from mRNA from lactating udder tissue. Full length clones corresponding to the four caseins were sequenced. The numbers of residues in the sequences deduced were αs1-CN 207, αs2-CN 178, β-CN 217, κ-CN 162. Percentage similarity to bovine proteins was αs1-CN A 39, αs2-CN 56, β-CN 64, κ-CN 56. Acid-precipitated casein of pooled milk was separated by reversed-phase HPLC and monitored at 220 nm, and its composition, estimated from peak integration, was (g/kg total casein) αs1-CN 220, αs2-CN 95, β-CN 650, κ-CN 35. Degrees of phosphorylation and glycosylation were determined by laser ionization mass spectrometry and sequence pattern analysis. Molecular masses determined were (kDa) αs1-CN A, 24·755 and 24·668; αs1-CN B, 25·293; αs2-CN 21·993; β-CN, 24·900; κ-CN 22·294–22·987. The pH values of the most probable isoelectric points were: αs1-CN A 6P 4·41, αs1-CN B 6P 4·40, αs2-CN 9P 4·58, β-CN 4P 4·66, κ-CN 1P, with ten sialic acid residues bound, 4·10.