High-melting-point triglycerides and the milk-fat globule membrane

1975 ◽  
Vol 42 (3) ◽  
pp. 419-426 ◽  
Author(s):  
F. B. P. Wooding ◽  
P. Kemp

SummaryThe initial milk-fat globule membrane (MFGM) consists of a unit membrane with a layer of dense material 10–20 nm thick on one side. Extraction of isolated initial MFGM preparations 3 times with chloroform: methanol removes 90% of the triglycerides and most of the phospholipids. This extraction has no significant effect on the width or morphology of the dense material examined subsequently in the electron microscope, although all trace of the unit membrane disappears. This indicates that the dense material is more likely to be derived from protein from the secretory cell cytoplasm than from high-melting-point triglycerides from the milk-fat globule as has previously been asserted.

Author(s):  
F.B.P. Wooding

The MFGM has been suggested (Patton and Keenan 1975) to be a very convenient and readily available source of plasma membrane from an active secretory cell. It can easily be isolated in pure form by churning or freeze thawing washed cream. However, there is also evidence (Wooding 1977) that the MFGM is not only a simple unit membrane structure such as is found for other isolated plasmalemmas. Characteristically, it has a coat of material 10-20 nm thick on one side which is derived from the cytoplasm of the mammary alveolar secretory cell.The milk fat globule secreted from the mammary alveolar cell has a continuous unit membrane boundary with a thin but uniform zone of cytoplasmic material between this membrane and the fat droplet core (Fig 1, inset). Immediately after the release of the milk fat globule from the secretory cell this “initial” MFGM undergoes rapid changes which produce a stable inhomogeneous “secondary” milk fat globule boundary characteristic of the fat globules in the milk of any species.


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.


2021 ◽  
pp. 106378
Author(s):  
Iolly Tábata Oliveira Marques ◽  
Fábio Roger Vasconcelos ◽  
Juliana Paula Martins Alves ◽  
Assis Rubens Montenegro ◽  
César Carneiro Linhares Fernandes ◽  
...  

1994 ◽  
Vol 1199 (1) ◽  
pp. 87-95 ◽  
Author(s):  
Naohito Aoki ◽  
Hidenori Kuroda ◽  
Miho Urabe ◽  
Yoshimi Taniguchi ◽  
Takahiro Adachi ◽  
...  

2002 ◽  
Vol 69 (4) ◽  
pp. 555-567 ◽  
Author(s):  
SUNG JE LEE ◽  
JOHN W. SHERBON

The effects of heat treatment and homogenization of whole milk on chemical changes in the milk fat globule membrane (MFGM) were investigated. Heating at 80 °C for 3–18 min caused an incorporation of whey proteins, especially β-lactoglobulin (β-lg), into MFGM, thus increasing the protein content of the membrane and decreasing the lipid. SDS-PAGE showed that membrane glycoproteins, such as PAS-6 and PAS-7, had disappeared or were weakly stained in the gel due to heating of the milk. Heating also decreased free sulphydryl (SH) groups in the MFGM and increased disulphide (SS) groups, suggesting that incorporation of β-lg might be due to association with membrane proteins via disulphide bonds. In contrast, homogenization caused an adsorption of caseins to the MFGM but no binding of whey proteins to the MFGM without heating. Binding of caseins and whey proteins and loss of membrane proteins were not significantly different between milk samples that were homogenized before and after heating. Viscosity of whole milk was increased when milk was treated with both homogenization and heating.


DNA Sequence ◽  
2004 ◽  
Vol 15 (5-6) ◽  
pp. 326-331 ◽  
Author(s):  
T.K. Bhattacharya ◽  
S.S. Misra ◽  
Feroz D. Sheikh ◽  
S. Dayal ◽  
V. Vohra ◽  
...  

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