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    Quantitation of lysinoalanine in dairy products by liquid chromatography–mass spectrometry with selective ion monitoring

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    The unnatural amino acid lysinoalanine (LAL) has been identified in milk and cheese products by liquid chromatography mass spectrometry (LC/ESI/MS) with selective ion monitoring (SIM) of the 9-fluorenyl-methylchloro-formate (FMOC) derivative. LAL is not present in raw milk or derived from Mozzarella cheese; however, high amounts of LAL are found in calcium caseinate and milk powder. As expected, milk fortified with caseinate or whey protein powder produces cheese with higher LAL content. Our analytical procedure is based on the simultaneous detection of specific ion masses of the FMOC–LAL derivative and the N-ε-methyl-lysine internal standard. A linear relationship was observed within the 0.2–20 ppm concentration range, in addition to a high correlation coefficient and 3% relative standard deviation

    Milk protein and their antigenicity

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    The main elements of milk proteins can be summarized as follows: variable phosphorylation degree of the four caseins, variable glycosylation of κ-CN and α-La, frequent presence of casein peptides generated by the action of endogenous and bacterial enzymes, wide molecular mass range whey proteins, easy thermodenaturation of whey proteins. With more knowledge of the primary structure, the location of the phosphate groups on the casein chains, and intra-and inter-protein disulphide bond exchanges during milk processing, particularly during digestion by proteolytic enzyme, the function and the role of most importantmilk proteins are now better understood. Further insight into the basic properties of milk proteins should lead to a greater understanding of the natural function of milk and the roles its components play in human nutrition. In this paper milk proteins are reviewed in the perspective of preventing milk allergies in newborns
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