scholarly journals Whey proteins modify the phase transition of milk fat globule phospholipids

1999 ◽  
Vol 79 (2) ◽  
pp. 217-228 ◽  
Author(s):  
Eric Dufour ◽  
Muriel Subirade ◽  
Franck Loupil ◽  
Alain Riaublanc
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.


1978 ◽  
Vol 45 (2) ◽  
pp. 197-208 ◽  
Author(s):  
Donald F. Darling ◽  
David W. Butcher

SummaryThe proteins of the milk-fat globule membrane in homogenized cream have been studied using polyacrylamide-gel electrophoresis and electron microscopy. The effects of pasteurization and subsequent storage of the homogenized cream on the strength and composition of the membrane have also been investigated. Caseins and undenatured whey proteins are adsorbed to the fat–serum interface during homogenization; the caseins are the more dominant group, but with no apparent preference for any individual protein. After homogenization, but before pasteurization, whey proteins are more easily removed by washing than are the casein components. After subsequent pasteurization, and on storage, whey proteins become more tightly bound and are no longer readily removed by washing. Electron micrographs showed that the interfacial membrane between fat droplets and the serum phase consists of a protein composite material containing casein micelles, casein micellar sub-units and molecular, or non-micellar protein.


2019 ◽  
Vol 57 (4) ◽  
pp. 448-460 ◽  
Author(s):  
Irena Barukčić ◽  
Katarina Lisak Jakopović ◽  
Rajka Božanić

Whey and buttermilk are the main by-products of the dairy industry, both having excellent nutritional properties. Buttermilk contains a unique component, the milk fat globule membrane (MFGM). MFGM contains bioactive compounds with positive health effects like antitumour or cholesterol-lowering impact. Whey proteins are found in whey and are a source of bioactive peptides acting positively on coronary, gastrointestinal, immune and nervous systems. Yet, buttermilk and whey are insufficiently utilized in functional food production. Various technological solutions have been studied in order to increase the production of foods based on whey and/or buttermilk whereby the production of beverages appear to be most acceptable from the economic and technological point of view. Thus, the aim of this paper is to give an overview of current knowledge about the possibilities of creating whey and/or buttermilk beverages.


1984 ◽  
Vol 51 (1) ◽  
pp. 113-121 ◽  
Author(s):  
Avis V. McPherson ◽  
Mary C. Dash ◽  
Barry J. Kitchen

SummaryBovine milk fat globule membrane (MFGM) material was isolated from cream by a new technique which did not involve removal of caseins and whey proteins before destabilization of the fat globules. These components were removed by centrifugation of the membrane material extract through a concentrated sucrose solution (52·5% (w/v) sucrose in 10 mM-Tris HCl buffer, pH 7·5). Membranes collected at the sample–sucrose interface, while whey proteins remained in the supernatant and caseins migrated into the concentrated sucrose solution. The yield of membrane material using this procedure was 25% less than that from conventional methods. This reduced yield was due mainly to lower levels of lipid material, in particular triglyceride. Electrophoretic analysis showed that the polypeptide composition of ‘unwashed’ membrane material was similar to that of conventionally prepared MFGM. This method is particularly suitable for the isolation of membrane material from milks and dairy products in which the fat globule stability is reduced or unknown.


RSC Advances ◽  
2014 ◽  
Vol 4 (90) ◽  
pp. 48963-48966 ◽  
Author(s):  
Jie Luo ◽  
Zi Wei Wang ◽  
Fang Wang ◽  
Hao Zhang ◽  
Jiang Lu ◽  
...  

Schematic representation of the native milk fat globule membrane: casein micelles and whey proteins on the surface of the membrane.


2007 ◽  
Vol 97 (4) ◽  
pp. 598-610 ◽  
Author(s):  
Marie-Caroline Michalski

Commercial milk is homogenized for the purpose of physical stability, thereby reducing fat droplet size and including caseins and some whey proteins at the droplet interface. This seems to result in a better digestibility than untreated milk. Various casein peptides and milk fat globule membrane (MFGM) proteins are reported to present either harmful (e.g. atherogenic) or beneficial bioactivity (e.g. hypotensive, anticarcinogenic and others). Homogenization might enhance either of these effects, but this remains controversial. The effect of homogenization has not been studied regarding the link between early cow's milk consumption and occurrence of type I diabetes in children prone to the disease and no link appears in the general population. Homogenization does not influence milk allergy and intolerance in allergic children and lactose-intolerant or milk-hypersensitive adults. The impact of homogenization, as well as heating and other treatments such as cheesemaking processes, on the health properties of milk and dairy products remains to be fully elucidated.


1984 ◽  
Vol 51 (2) ◽  
pp. 289-297 ◽  
Author(s):  
Avis V. McPherson ◽  
Mary C. Dash ◽  
Barry J. Kitchen

SummaryThe material surrounding the fat globules in commercial pasteurized homogenized milk was isolated by centrifugation of the freeze – thaw extract of the fat globules through a 52·5% (w/v) sucrose solution in simulated milk ultrafiltrate. The purified membrane material contained higher neutral lipid levels than fresh raw milk fat globule membrane (MFGM) material. Caseins and whey proteins, mainly β-lactoglobulin (β-lg) were found to be the major protein components of homogenized milk membrane material. Native MFGM polypeptides comprised only a small proportion of the total protein in these membranes. The total amount of membrane material isolated from homogenized milk was substantially higher than that from fresh raw milk. Analysis of homogenized milk membrane material by linear sucrose density gradient centrifugation showed a different pattern to that found with other milks, indicating the presence of new lipoprotein complexes. Commercial ultra heat treated (UHT) milks were also examined, but it was difficult to obtain isolated MFGM material free from core fat. However, fat globule fractions were isolated from these products by high speed centrifugation and these were analysed intact. Membrane material in these milks contained caseins and whey proteins (mainly β-1g). Natural MFGM polypeptides were present at extremely low levels. Phospholipid levels in UHT milk membranes were greatly reduced compared with membrane material isolated from other milks.


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