Changes in the Protein Composition and Size Distribution of Bovine Casein Micelles Induced by Cooling

1990 ◽  
Vol 54 (6) ◽  
pp. 1385-1392
Author(s):  
Tomotada Ono ◽  
Tamaki Murayama ◽  
Setu Kaketa ◽  
Satoshi Odagiri
Keyword(s):  
Size Distribution ◽  
Protein Composition ◽  
Casein Micelles

scholarly journals Changes in the protein composition and size distribution of bovine casein micelles induced by cooling.

1990 ◽  
Vol 54 (6) ◽  
pp. 1385-1392 ◽  
Author(s):  
Tomotada ONO ◽  
Tamaki MURAYAMA ◽  
Setu KAKETA ◽  
Satoshi ODAGIRI
Keyword(s):  
Size Distribution ◽  
Protein Composition ◽  
Casein Micelles

Formation and Structure of Casein Micelles in Lactating Mammary Tissue

1970 ◽  
Vol 28 ◽  
pp. 150-151
Author(s):  
Robert J. Carroll ◽  
Marvin P. Thompson ◽  
Harold M. Farrell
Keyword(s):  
Size Distribution ◽  
G Protein ◽  
Milk Proteins ◽  
Mammary Tissue ◽  
Colloidal System ◽  
Casein Micelles ◽  
The Stability

Milk is an unusually stable colloidal system; the stability of this system is due primarily to the formation of micelles by the major milk proteins, the caseins. Numerous models for the structure of casein micelles have been proposed; these models have been formulated on the basis of in vitro studies. Synthetic casein micelles (i.e., those formed by mixing the purified αsl- and k-caseins with Ca2+ in appropriate ratios) are dissimilar to those from freshly-drawn milks in (i) size distribution, (ii) ratio of Ca/P, and (iii) solvation (g. water/g. protein). Evidently, in vivo organization of the caseins into the micellar form occurs in-a manner which is not identical to the in vitro mode of formation.

Size distribution of casein micelles in camels′ milk

1985 ◽  
Vol 52 (2) ◽  
pp. 303-307 ◽  
Author(s):  
Mohmed Z. Ali ◽  
Richard K. Robinson
Keyword(s):  
Size Distribution ◽  
Casein Micelles

Casein Micelles: Size Distribution in Milks from Individual Cows

2012 ◽  
Vol 60 (18) ◽  
pp. 4649-4655 ◽  
Author(s):  
C. G. (Kees) de Kruif ◽  
Thom Huppertz
Keyword(s):  
Size Distribution ◽  
Casein Micelles

A comparison of the heat stability of fresh milk protein concentrates obtained by microfiltration, ultrafiltration and diafiltration

2019 ◽  
Vol 86 (3) ◽  
pp. 347-353 ◽  
Author(s):  
Isis Rodrigues Toledo Renhe ◽  
Zhengtao Zhao ◽  
Milena Corredig
Keyword(s):  
Membrane Filtration ◽  
Milk Protein ◽  
Ionic Composition ◽  
Protein Composition ◽  
Heat Stability ◽  
Casein Micelles ◽  
Protein Concentrates ◽  
Fresh Milk ◽  
Dairy Protein ◽  
The Impact

AbstractThe objective of this work was to evaluate the impact of changes during membrane filtration on the heat stability of milk protein concentrates. Dairy protein concentrates have been widely employed in high protein drinks formulations and their stability to heat treatment is critical to ensure quality of the final product. Pasteurized milk was concentrated three-fold by membrane filtration, and the ionic composition was modified by addition of water or permeate from filtration (diafiltration). Diafiltration with water did not affect the apparent diameter of the casein micelles, but had a positive effect on heat coagulation time (HCT), which was significantly longer (50 min), compared to the non diafiltered concentrates (about 30 min). UHT treatments increased the particle size of the casein micelles, as well as the turbidity of retentates. Differences between samples with and without diafiltration were confirmed throughout further analysis of the protein composition of the unsedimentable fraction, highlighting the importance of soluble protein composition on the processing functionality of milk concentrates.

Inelastic light-scattering study of the size distribution of bovine milk casein micelles

Biochemistry ◽  
1971 ◽  
Vol 10 (25) ◽  
pp. 4788-4793 ◽  
Author(s):  
S. H. C. Lin ◽  
R. K. Dewan ◽  
V. A. Bloomfield ◽  
C. V. Morr
Keyword(s):  
Light Scattering ◽  
Size Distribution ◽  
Bovine Milk ◽  
Casein Micelles ◽  
Inelastic Light Scattering ◽  
Scattering Study ◽  
Milk Casein

Influence of homogenization of concentrated milks on the structure and properties of rennet curds

1983 ◽  
Vol 50 (3) ◽  
pp. 341-348 ◽  
Author(s):  
Margaret L. Green ◽  
Richard J. Marshall ◽  
Frank A. Glover
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Size Distribution ◽  
Casein Micelle ◽  
Structure And Properties ◽  
Moisture Retention ◽  
Casein Micelles ◽  
Micelle Size ◽  
Whole Milk ◽  
Milk Casein

SummaryWhole milk was concentrated by ultrafiltration in a plant causing some homogenization of the fat. Comparisons were made with milk concentrated in a plant causing little homogenization and with milk homogenized conventionally. None of the processes appreciably affected the casein micelle size distribution. On rennet treatment of homogenized milk, casein micelle aggregation occurred more slowly, the protein network in the curd was less coarse and the rate of whey loss was reduced, compared with non-homogenized milk at the same concentration. In using concentrated milks for cheesemaking homogenization improved the composition of Cheddar cheese, because of increased fat and moisture retention, but curd fusion was poorer. Some aspects of the texture of the mature cheeses were improved, but the free fatty acid levels were higher. Values for the firmness of curds, formed from milks processed in different ways, did not relate to the extent of aggregation of the casein micelles. It is suggested that the complete cheesemaking process is driven by the tendency of the casein to aggregate.

A study of the properties of dissociated bovine casein micelles

1975 ◽  
Vol 42 (1) ◽  
pp. 169-183 ◽  
Author(s):  
L. K. Creamer ◽  
Gillian P. Berry
Keyword(s):  
Electron Microscopy ◽  
Ionic Strength ◽  
Gel Filtration ◽  
Protein Composition ◽  
Leading Edge ◽  
Urea Solution ◽  
Casein Micelle ◽  
Casein Micelles ◽  
Micellar Casein ◽  
Sepharose 4B

SummaryAlthough casein micelles are disrupted by removal of Ca, individual caseins remain aggregated in sub-micellar casein aggregates or sub-units. These sub-units have been studied by: (1) the use of gel filtration on Sepharose 4B at 6, 20 and 37°C at pH 6·7 and 0·1 ionic strength, (2) ultracentrifugation and (3) electron microscopy. At 37°C the protein composition of the sub-units varied across the gel-filtration peak, with κ-casein being eluted towards the leading edge and the ratio of αs1- to β-casein being almost constant across the peak. Re-chromatography of the protein from the leading edge of this peak gave a new wide peak with the κ-casein again being eluted towards the leading edge. However, αs1-casein was eluted before β-casein in the leading edge of the new peak. Prior treatment of the casein micelles by dispersion with 6 m-urea solution, precipitation with acid or reduction with 2-mercaptoethanol did not alter the gel-filtration pattern. An examination of the purified casein components and their mixtures showed that a 1:1 ratio mixture of αs1- and β-casein had the same peak maximum elution volume as casein micelle sub-units. κ-Casein by itself eluted at the void volume of the gel-filtration column, but after admixture with a sample of small micelles it eluted at the leading edge of the sub-unit peak and was indistinguishable from the κ-casein normally present. These results suggest that the sub-units are in equilibrium with their component caseins and that their size distribution is determined by only those factors (such as protein concentration, pH, temperature and ionic strength) which determine the strength of association between the casein components. The results from electron microscopy and ultracentrifugation support these conclusions.

Composition and size distribution of bovine casein micelles

1980 ◽  
Vol 630 (2) ◽  
pp. 261-270 ◽  
Author(s):  
Thomas C.A. McGann ◽  
William J. Donnelly ◽  
Robert D. Kearney ◽  
Wolfgang Buchhemm
Keyword(s):  
Size Distribution ◽  
Casein Micelles
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