Structural modifications induced by industrial treatments on milk proteins
have been investigated using a new analytical protocol based on mass spectr
ometric procedures (electrospray and matrix assisted laser desorption ioniz
ation mass spectrometry) providing a direct correlation between the severit
y of the treatment and the damages observed. The application of this proced
ure to the analysis of whey proteins from milli samples submitted to differ
ent thermal processes cofirmed that under these conditions protein modifica
tion is essentially due to the nonenzymatic glycation of amino groups by la
ctose (Maillard reaction). A detailed structural investigation of the modif
ication sites, carried out by the mass mapping strategy, revealed the occur
rence of preferentially lactosylated sites in both alpha-lactalbumin and be
ta-lactoglobulin.