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ABSTRACT: 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.
European Food Research and Technology 02/2006; 222(3):467-471. DOI:10.1007/s00217-005-0177-9 · 1.56 Impact Factor