scholarly journals Interactions of whey proteins with milk fat globule membrane proteins during heat treatment of whole milk

2004 ◽  
Vol 84 (3) ◽  
pp. 269-283 ◽  
Author(s):  
Aiqian Ye ◽  
Harjinder Singh ◽  
Michael W. Taylor ◽  
Skelte Anema
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.


1977 ◽  
Vol 44 (3) ◽  
pp. 495-507 ◽  
Author(s):  
J. C. Allen ◽  
Catherine Humphries

SummaryBovine milk-fat globule membrane was solubilized with a zwitterionic surfactant and subjected to chromatography on agarose, with the surfactant in the eluant. Fractions were tested for their effects on the oxidation of buffered linoleate. The maximum oxidative capability was greatly enhanced by the addition of Cu, and became associated with the phospholipids.Further chromatography of the retarded protein peak from agarose on Sephadex G-200, again in the presence of surfactant, gave 2 protein peaks. Oxidative effectiveness resided almost entirely in the first peak, which was devoid of phospholipid, but high in xanthine oxidase activity. This fraction was subjected to isoelectric focusing, and the xanthine oxidase from this was highly pro-oxidative. Furthermore, its oxidative capability was almost doubled on heat treatment.


1992 ◽  
Vol 59 (2) ◽  
pp. 187-195 ◽  
Author(s):  
Avis V. Houlihan ◽  
Philippa A. Goddard ◽  
Stephen M. Nottingham ◽  
Barry J. Kitchen ◽  
Colin J. Masters

SummaryHeating raw milk at 80 °C for 2·5–20 min was found to result in compositional changes in the milk fat globule membrane (MFGM). The yield of protein material increased with the duration of heating, owing to incorporation of skim milk proteins, predominantly β-lactoglobulin, into the membrane. Lipid components of the MFGM were also affected, with losses of triacylglycerols on heating.


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