Qualitative and quantitative profiling of the bovine milk fat globule membrane proteome

• Published in: Journal of proteomics Vol. 73; no. 6; pp. 1079 - 1088
• Main Authors: Affolter, Michael, Grass, Laetitia, Vanrobaeys, Frank, Casado, Begoña, Kussmann, Martin
• Format: Journal Article Conference Proceeding
• Language: English
• Published: Kidlington Elsevier B.V 18.04.2010; Elsevier
• Subjects: Amino Acid Sequence; Animals; Biological and medical sciences; Bone morphogenetic proteins; Buttermilk; Calibration; Cattle; Chromatography, Liquid - methods; Cow's milk; Diverse techniques; Fundamental and applied biological sciences. Psychology; Glycolipids - chemistry; Glycoproteins - chemistry; Isotopes; Mass Spectrometry - methods; Micronutrients; Milk; Milk - metabolism; Milk fat globule membrane; Milk fat globule membranes; Milk products; Molecular and cellular biology; Molecular Sequence Data; Neonates; Nutrigenomics; Nutrition; Progeny; Proteins - chemistry; Proteome; Proteomics; Proteomics - methods; Triglycerides - chemistry; whey protein; Nutrigenomics; Milk fat globule membrane; Nutrition; Proteomics; Milk; Bovine; Proteome; Vertebrata; Mammalia; Fat; Membrane; Artiodactyla; Ungulata
• ISSN: 1874-3919; 1876-7737
• DOI: 10.1016/j.jprot.2009.11.008

Milk is a biological fluid of unique quality and complexity. It has co-evolved with mammals and mankind to nourish offspring and contains macro- and micronutrients for growth and development of the newborn. The milk fat globule membrane (MFGM) represents an important milk fraction, which is rich in bioactive proteins. In order to better understand functionality of milk fractions and, thereby, enhance the benefits of milk products, detailed qualitative and quantitative protein knowledge of fractions such as MFGM is required. We report the qualitative and quantitative profiling of two MFGM-enriched milk fractions, a whey protein concentrate (WPC) and a buttermilk protein concentrate (BMP), as derived from three different analytical workflows. First, an LC-MS/MS-based shotgun approach revealed 244 protein identities in WPC and 133 in BMP, respectively, and provided an extensive characterisation of the protein content in those two fractions. Second, label-free profiling resulted in rapid and efficient semi-quantitative comparison and yielded valuable protein fingerprints. Third, absolute quantification of selected MFGM proteins was achieved by stable isotope dilution (SID)-MS, in combination with multiple reaction monitoring (MRM) detection. In summary, we provide new information on composition, quantity and possible health benefits of two MFGM-enriched milk fractions highly valuable for future nutritional applications. Milk fat globule and its membrane with detailed arrangement of the main targeted MFGM proteins. [Display omitted]