2026-04-17T14:44:59Zhttps://recercat.cat/oai/request

oai:recercat.cat:2445/1915882025-12-04T19:36:19Zcom_2072_1057col_2072_478813col_2072_478913col_2072_478917

00925njm 22002777a 4500 dc Ghafoori, Zahra author Tehrani, Tahereh author Pont Villanueva, Laura author Benavente Moreno, Fernando J. (Julián) author 2022-12-14T17:36:38Z 2022-12-14T17:36:38Z 2022 2022-12-14T17:36:38Z Protein profiling of major bovine milk proteins (i.e. whey and casein proteins) is of great interest in food science and technology. This complex set of protein proteoforms may vary with breed, genetics, lactation stage, health and nutritional status of the animal. Current routine methods for bovine milk protein profiling at the intact level are typically based on CE-UV, which does not allow confirming unequivocally the identity of the separated proteins. As an alternative, in this study, we describe for the first time a novel and simple CE-MS method in positive ESI mode. Under the optimized conditions, CE-MS allowed the separation and identification at the intact level of major bovine milk whey and casein proteins in less than 15 min. Furthermore, high-resolution MS confirmed its importance in the reliable characterization of bovine milk protein proteoforms, especially those with slight molecular mass differences, such as β-casein A1 and A2, which are relevant to unequivocally identify milks with specific β-casein compositions (e.g. A2A2 milks, which are widely known as A2 milks). This differentiation was not possible by MALDI-MS, which provided rapidly and easily a rich but less accurate fingerprint of bovine milk proteins due to the lower mass resolution. Proteïnes de la llet Electroforesi capil·lar Espectrometria de masses Milk proteins Capillary electrophoresis Mass spectrometry Separation and characterization of bovine milk proteins by capillary electrophoresis-mass spectrometry