Quantitative determination of bovine κ-casein macropeptide in dairy products by Liquid chromatography/Electrospray coupled to mass spectrometry (LC-ESI/MS) and Liquid chromatography/Electrospray coupled to tamdem mass spectrometry (LC-ESI/MS/MS)

Health effects and technological features of caseinomacropeptide

“…Recently Molle´and Le´onil (2005) published a quantitative method using RP-HPLC with electrospray-tandemmass-spectrometry (ESI-MS/MS). The method is based on the detection of specific multiple charged ions in combination with the determination of an enzyme-released peptide, k-casein f(162-169).…”

“…Glycosylated forms represent about 50% of the total bovine CMP, which is also referred to as glycomacropeptide (GMP) (Molle´& Le´onil, 2005). Five different mucin-type carbohydrate chains, composed of N-acetylneuraminyl (NeuAc), galactosyl (Gal) and N-acetylgalactosamine (GalNAc), have been identified in GMP (Saito & Itoh, 1992):…”

Enzyme-linked immunosorbent assay for the detection of bovine rennet whey powder in milk powder and buttermilk powder

“…The specificity of the ELISA and the EU screening method (GPC) were comparable, as a lower or comparable number of false positive test results were obtained analysing industrial samples. Using (tandem) mass spectrometry, the amino acid sequence or the exact molecular weight of (pseudo) CMP can be determined (Molle´& Le´onil, 2005) which would give ultimate specificity. However, these methods are labour intensive and require expensive equipment and materials, and might therefore be suitable for confirmation analysis but not for routine screening.…”

“…Several methods have been developed for the detection of CMP in dairy products, e.g., colorimetric (De Koning, Eisses, & De Vries, 1966;Fukada, Roig, & Prata, 2004), chromatographic (Elgar et al, 2000;Kawakami, Kawasaki, Dosako, Tanimoto, & Nakajima, 1992;Le´onil & Molle´, 1991;Olieman & van den Bedem, 1983;Olieman & van Riel, 1989), immunological (Bitri, Rolland, & Besanc -on, 1993;Picard, Plard, Rongdaux-Gaida, & Collin, 1994) and, more recently, methods based on capillary zone electrophoresis (Cherkaoui, Doumenc, Tachon, Neeser, & Veuthey, 1997;Recio, Lo´pez-Fandinˇo, Olano, Olieman, & Ramos, 1996;Recio et al, 2000;Van Riel & Olieman, 1995), mass spectrometry (De Noni & Resmini, 2005;Molle´& Le´onil, 2005) and biosensors (Haasnoot, 2005;Haasnoot, Marchesini, & Koopal, 2006 immunoassays were developed for the detection of CMP as a marker for proteolysis in raw milk or as a marker for bovine milk in sheep and goat milk products and not for the detection of rennet whey. The biosensor immunoassays are suitable for the detection of BRW powder in milk powder above 1% (w/w).…”

Reduced β-lactoglobulin IgE binding upon in vitro digestion as a result of the interaction of the protein with casein glycomacropeptide

“…2B G0) and presented two main peaks corresponding to aglyco-CMP A (indicated as aCMP A ) and aglyco-CMP B (indicated as aCMP B ) and several minor peaks corresponding to glycosylated forms of CMP A and CMP B (indicated as gCMP A and gCMP B ). As it was previously reported by several authors (Minkiewicz et al, 1996;Mollé & Leonil, 2005; CMP is very heterogeneous arising from the existence of four genetic variants (A, B, C, E) and several phosphorylation and glycosylation sites. CMP was rapidly hydrolyzed by pepsin during the gastric digestion (Fig.…”