Glycosphingolipids from bovine milk and milk fat globule membranes: a comparative study. Adhesion to enterotoxigenic Escherichia coli strains

2009 ◽  
Vol 390 (1) ◽  
Author(s):  
Fernando Sánchez-Juanes ◽  
Josefa M. Alonso ◽  
Lorena Zancada ◽  
Pablo Hueso

AbstractSeveral components of milk fat globule membranes (MFGMs) have been reported to display beneficial health properties and some of them have been implicated in the defense of newborns against pathogens. These observations prompted us to determine the glycosphingolipid content of MFGMs and their interaction with pathogens. A comparative study with whole milk components was also carried out. Milk fat globules and MFGMs were isolated from milk. Gangliosides and neutral glycosphingolipids were obtained from MFGMs and whole milk and their fatty acid contents were determined by gas chromatography-mass spectrometry (GC-MS). MFGMs and whole milk showed similar ganglioside and neutral glycosphingolipid contents, with whole milk having more GM3 and glucosylceramide and less GD3,O-acetyl GD3,O-acetyl GT3, and lactosylceramide. The fatty acid content of gangliosides from both sources showed a similar composition. However, the neutral glycosphingolipid fatty acid content seemed to be quite different. Whole milk had fewer very-long-chain fatty acids (18.1% vs. 46.4% in MFGMs) and more medium-chain and unsaturated C18:1 and C18:2 fatty acids. Milk fat globules, MFGMs, lactosylceramide, and gangliosides GM3 and GD3 were observed to bind enterotoxigenicEscherichia colistrains. Furthermore, bacterial hemagglutination was inhibited by MFGMs and glycosphingolipids.

1996 ◽  
Vol 63 (3) ◽  
pp. 441-449 ◽  
Author(s):  
Milena Corredig ◽  
Douglas G. Dalgleish

SummaryThe heat-induced binding of whey proteins to milk fat globule membranes in whole milk was investigated by quantitative electrophoresis and laser scanning densitometry. Both α-lactalbumin and β-lactoglobulin bound to the surfaces of fat globules when milk was heated in a water bath in the temperature range 65–85 °C. The interaction behaviour of α-lactalbumin did not seem to change with temperature, and the total amount of protein bound was ∼ 0·2 mg/g fat contained in the cream. The quantity of βlactoglobulin interacting with the milk fat globules increased with temperature from 02 to 0·7 mg/g fat between 65° and 85 °C. Even in whole milk heated at batch pasteurization temperatures (60–65 °C), α-lactalbumin and β-lactoglobulin were found attached to the fat globules. The interactions of the whey proteins with intact fat globule membranes were also investigated in milk heated in an industrial system (a pilot scale UHT and high temperature short time module), and the results were compared with those from the laboratory treatment (simple batch heating). The binding of the whey proteins to fat globules differed between milk heated by UHT using indirect steam heating or direct steam injection (DSI). However, the surface load in milk treated by DSI was not comparable to that of milk treated by batch heating or indirect steam heating, because of the changes in fat globule size and membrane composition caused by the DSI process.


2016 ◽  
Vol 27 (19) ◽  
pp. 2946-2964 ◽  
Author(s):  
Edith Honvo-Houéto ◽  
Céline Henry ◽  
Sophie Chat ◽  
Sarah Layani ◽  
Sandrine Truchet

During lactation, mammary epithelial cells secrete huge amounts of milk from their apical side. The current view is that caseins are secreted by exocytosis, whereas milk fat globules are released by budding, enwrapped by the plasma membrane. Owing to the number and large size of milk fat globules, the membrane surface needed for their release might exceed that of the apical plasma membrane. A large-scale proteomics analysis of both cytoplasmic lipid droplets and secreted milk fat globule membranes was used to decipher the cellular origins of the milk fat globule membrane. Surprisingly, differential analysis of protein profiles of these two organelles strongly suggest that, in addition to the plasma membrane, the endoplasmic reticulum and the secretory vesicles contribute to the milk fat globule membrane. Analysis of membrane-associated and raft microdomain proteins reinforces this possibility and also points to a role for lipid rafts in milk product secretion. Our results provide evidence for a significant contribution of the endoplasmic reticulum to the milk fat globule membrane and a role for SNAREs in membrane dynamics during milk secretion. These novel aspects point to a more complex model for milk secretion than currently envisioned.


Dairy ◽  
2021 ◽  
Vol 2 (2) ◽  
pp. 202-217
Author(s):  
Michele Manoni ◽  
Donata Cattaneo ◽  
Sharon Mazzoleni ◽  
Carlotta Giromini ◽  
Antonella Baldi ◽  
...  

Milk lipids are composed of milk fat globules (MFGs) surrounded by the milk fat globule membrane (MFGM). MFGM protects MFGs from coalescence and enzymatic degradation. The milk lipid fraction is a “natural solvent” for macronutrients such as phospholipids, proteins and cholesterol, and micronutrients such as minerals and vitamins. The research focused largely on the polar lipids of MFGM, given their wide bioactive properties. In this review we discussed (i) the composition of MFGM proteome and its variations among species and phases of lactation and (ii) the micronutrient content of human and cow’s milk lipid fraction. The major MFGM proteins are shared among species, but the molecular function and protein expression of MFGM proteins vary among species and phases of lactation. The main minerals in the milk lipid fraction are iron, zinc, copper and calcium, whereas the major vitamins are vitamin A, β-carotene, riboflavin and α-tocopherol. The update and the combination of this knowledge could lead to the exploitation of the MFGM proteome and the milk lipid fraction at nutritional, biological or technological levels. An example is the design of innovative and value-added products, such as MFGM-supplemented infant formulas.


1970 ◽  
Vol 44 (1) ◽  
pp. 80-93 ◽  
Author(s):  
T. W. Keenan ◽  
D. James Morré ◽  
Diane E. Olson ◽  
W. N. Yunghans ◽  
Stuart Patton

Purified plasma membrane fractions from lactating bovine mammary glands and membranes of milk fat globules from the same source were similar in distribution and fatty acid composition of phospholipids. The sphingomyelin content of the phospholipid fraction of both membranes was higher than in these fractions from other cell components, ß-carotene, a constituent characteristic of milk fat, was present in the lipid fraction of the plasma membrane. Cholesterol esters of plasma membrane were similar in fatty acid composition to those of milk fat globule membranes. Disc electrophoresis of either membrane preparation on polyacrylamide gels revealed a single major protein component characteristic of plasma membrane from other sources. Distinct morphological differences between plasma membrane and milk fat globule membranes were observed in both thin sections and in negatively stained material. Plasma membrane was vesicular in appearance while milk fat globule membranes had a platelike aspect. These observations are consistent with derivation of fat globule membrane from plasma membrane accompanied by structural rearrangement of membrane constituents.


Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1251 ◽  
Author(s):  
Michele Manoni ◽  
Chiara Di Lorenzo ◽  
Matteo Ottoboni ◽  
Marco Tretola ◽  
Luciano Pinotti

Milk is a lipid-in-water emulsion with a primary role in the nutrition of newborns. Milk fat globules (MFGs) are a mixture of proteins and lipids with nutraceutical properties related to the milk fat globule membrane (MFGM), which protects them, thus preventing their coalescence. Human and bovine MFGM proteomes have been extensively characterized in terms of their formation, maturation, and composition. Here, we review the most recent comparative proteomic analyses of MFGM proteome, above all from humans and bovines, but also from other species. The major MFGM proteins are found in all the MFGM proteomes of the different species, although there are variations in protein expression levels and molecular functions across species and lactation stages. Given the similarities between the human and bovine MFGM and the bioactive properties of MFGM components, several attempts have been made to supplement infant formulas (IFs), mainly with polar lipid fractions of bovine MFGM and to a lesser extent with protein fractions. The aim is thus to narrow the gap between human breast milk and cow-based IFs. Despite the few attempts made to date, supplementation with MFGM proteins seems promising as MFGM lipid supplementation. A deeper understanding of MFGM proteomes should lead to better results.


PEDIATRICS ◽  
1988 ◽  
Vol 81 (1) ◽  
pp. 141-146
Author(s):  
Wolfgang Buchheim ◽  
Ulrich Welsch ◽  
Gail E. Huston ◽  
Stuart Patton

Freeze-etch electron microscopy was applied to milk fat globules to observe surface details. A remarkable array of filaments, approximately 0.5 µm in length, was seen on human, but not bovine, globules. Heating human globules removed the filaments that were identified as high molecular weight glycoproteins by freezeetch and gel electrophoretic analysis of the heating medium. Extraction of these globule glycoproteins was slight at 60°C for one minute but substantial and tending to plateau at 80°C for one minute. Such heat-induced alterations of the milk fat globule surface provide an alternative or additional explanation to milk lipase inactivation as the cause of reduced milk fat absorption from heated milk by the preterm infant.


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