Characterization of casein lactosylation by capillary electrophoresis and mass spectrometry
2006
Capillary electrophoresis (CE) and mass spectrometry have been used to verify the formation of lactosylated casein variants. CE was performed in a hydrophilically coated capillary at low pH and in the presence of urea. Lactosylated α-casein, β-casein, and κ-casein migrate shortly after the unmodified proteins. Evidence for casein lactosylation was obtained by electrospray ionization-mass spectrometry (ESI-MS). Lactosylated β-casein can be monitored not only in milk and milk powders but also in the complex protein mixture of processed cheese. The formation of lactosylated β-casein A1 and A2 during heating of processed cheese was found to correlate with the furosine content. Consequently, CE of casein may be a possible method for directly assessing the extent of the early Maillard reaction in dairy products.
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