Quantitative multivalent binding model of the structure, size distribution and composition of the casein micelles of cow milk

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.

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Size distribution of casein micelles in camels′ milk

Journal of Dairy Research ◽

10.1017/s0022029900024183 ◽

1985 ◽

Vol 52 (2) ◽

pp. 303-307 ◽

Cited By ~ 10

Author(s):

Mohmed Z. Ali ◽

Richard K. Robinson

Keyword(s):

Size Distribution ◽

Casein Micelles

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Casein Micelles: Size Distribution in Milks from Individual Cows

Journal of Agricultural and Food Chemistry ◽

10.1021/jf301397w ◽

2012 ◽

Vol 60 (18) ◽

pp. 4649-4655 ◽

Cited By ~ 59

Author(s):

C. G. (Kees) de Kruif ◽

Thom Huppertz

Keyword(s):

Size Distribution ◽

Casein Micelles

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2D-Cross Correlation Spectroscopy Coupled with Molecular Fluorescence Spectroscopy for Analysis of Molecular Structure Modification of Camel Milk and Cow Milk Mixtures during Coagulation

Foods ◽

10.3390/foods9060724 ◽

2020 ◽

Vol 9 (6) ◽

pp. 724 ◽

Cited By ~ 1

Author(s):

Oumayma Boukria ◽

El Mestafa El Hadrami ◽

Shaxnoza Sultanova ◽

Jasur Safarov ◽

Françoise Leriche ◽

...

Keyword(s):

Molecular Structure ◽

Fluorescence Spectroscopy ◽

Correlation Spectroscopy ◽

Cow Milk ◽

Structure Modification ◽

Casein Micelles ◽

Molecular Fluorescence ◽

Camel's Milk ◽

Hydrolysis Of ◽

Rate Of Response

Synchronous fluorescence spectroscopy (SFS) coupled with two-dimensional correlation spectroscopy (2DCOS) was employed to monitor, at the molecular level, the coagulation of five mixture ratios of camel’s milk (CaM) and cow’s milk (CM) (100% CaM, 75% CaM:25% CM, 50% CaM:50% CM, 25% CaM:75% CM and 100% CM). The dissimilarities among the different formulations are highlighted on the synchronous 2DCOS-SFS. In addition, according to the cross-peak symbols in synchronous and asynchronous spectra, the rate of response modification in riboflavin, protein and vitamin A matched with common coagulation phenomena usually reported during chymosin coagulation (hydrolysis of κ-casein, destabilization of casein micelles and aggregation). This study demonstrated that 2DCOS-SFS is a successful strategy to discriminate milk mixtures and to monitor molecular structure modifications during coagulation process.

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

Biochemistry ◽

10.1021/bi00801a029 ◽

1971 ◽

Vol 10 (25) ◽

pp. 4788-4793 ◽

Cited By ~ 61

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

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

Journal of Dairy Research ◽

10.1017/s0022029900023177 ◽

1983 ◽

Vol 50 (3) ◽

pp. 341-348 ◽

Cited By ~ 70

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.

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