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Milk fat globule membrane (MFGM) proteins are receiving increased attention due to their reported benefits for human health, particularly in infant populations. Challenges exist in MFGM protein quantification due to their low quantities, complex chemistry, interactions with other matrix components, and the high matrix complexity. In this study, a subset of four MFGM proteins were selected as relevant targets for identification and quantification in an infant formula (IF) matrix: butyrophilin, mucin 1, xanthine dehydrogenase/oxidase, and perilipin 2. An analytical protocol for absolute quantification of these four MFGM proteins in IF was successfully developed and validated. Additionally, the feasibility to apply the method in selected MFGM ingredients was also demonstrated. The method demonstrated good performance; high accuracy and robustness, low LOQ and uncertainty, while controlling the matrix effect. This study represents a report of an analytical method to quantify selected MFGM proteins in IF., Competing Interests: Declaration of competing interest The authors declare that they have no known competing financial interest or personal relationships that could have appeared to influence the work reported in this paper., (Copyright © 2024 Elsevier Ltd. All rights reserved.)

Recent studies have demonstrated the positive effects of regular intake of milk fat globule membranes (MFGMs) on neural and cognitive development, as well as immune and gastrointestinal health in infants and elders. Dairy products and by-products generated from the butter and butter oil manufacturing process are valuable sources of MFGM. Thus, in view of the growing need to reduce by-products and waste, it is crucial to foster research aimed at the valorization of dairy by-products rich in MFGM. For this purpose, all the by-products coming from butter and butter oil production (from raw milk to the related by-products) were used to study the MFGM isolated fractions, followed by their characterization through a combined lipidomic and proteomic approach. The patterns of polar lipids and proteins indicated that buttermilk (BM), butterserum (BS), and their mix (BM-BS blend) are the most suitable by-products to be employed as starting material for the isolation and purification of MFGMs, thus obtaining MFGM-enriched ingredients for the manufacture of products with high biological activity. [ABSTRACT FROM AUTHOR]

[Display omitted] • The effect mechanism of MFGM proteins on the acid-tolerant survival of Lactobacillus was first revealed. • MFGM proteins could improve the survival ability of bacteria under low acid conditions. • Protein differences were analyzed by Tandem Mass Tags (TMT) proteomics. The prerequisite for lactic acid bacteria to perform their probiotic function is that they could survive the acid-stressed environment of production and application. In this experiment, the protective mechanism of milk fat globule membrane (MFGM) proteins on lactic acid bacteria under acid stress was investigated. Scanning electron microscopy and fluorescence probe were used to analyze the condition of the acid-treated bacteria, which showed that MFGM proteins could enhance the survival ability of Lactobacillus acidophilus CICC 6074 under acid stress by maintaining cell morphology, elevating intracellular pH and H+-ATPase activity. Furthermore, Tandem Mass Tags (TMT) proteomic analysis revealed that MFGM protein could exert protective effects on L. acidophilus CICC 6074 by regulating amino acid metabolism, ATPase activity, peptidoglycan synthesis, gene repair and heritage, etc. The results will provide a new approach for the protection and development of functional lactic acid bacteria. [ABSTRACT FROM AUTHOR]