Identification of Peptides Released from Casein Micelles by Limited Trypsinolysis

1996 ◽  
Vol 44 (9) ◽  
pp. 2517-2522 ◽  
Author(s):  
Olga Diaz ◽  
Adam M. Gouldsworthy ◽  
Jeffrey Leaver
Keyword(s):  
Casein Micelles ◽  
Limited Trypsinolysis

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.

Model mixtures evidence the respective roles of whey protein particles and casein micelles during acid gelation

2014 ◽  
Vol 37 ◽  
pp. 203-212 ◽  
Author(s):  
Robi Andoyo ◽  
Fanny Guyomarc'h ◽  
Chantal Cauty ◽  
Marie-Hélène Famelart
Keyword(s):  
Whey Protein ◽  
Casein Micelles ◽  
Protein Particles ◽  
Acid Gelation

Casein micelles: the colloid-chemical approach

1979 ◽  
Vol 46 (2) ◽  
pp. 291-306 ◽  
Author(s):  
Theodoor A. J Payens
Keyword(s):  
Rate Constants ◽  
Dlvo Theory ◽  
Lag Phase ◽  
Rate Theory ◽  
Casein Micelles ◽  
Protective Colloid ◽  
Colloidal Properties ◽  
Micellar Casein ◽  
Clot Structure ◽  
Flocculation Rate

SUMMARYThe colloidal properties of micellar casein are reviewed. It is shown that the behaviour of intact micelles is much at variance with the predictions from the Schulze–Hardy rule, and that therefore their stability cannot be explained by the principles of the DLVO theory. Towards electrolyte, micelles behave as a protein rather than a lyophobic colloid.Casein is a strong protective colloid. In the micelle, however, it does not completely cover the inorganic constituent which remains sensitive to changes in the ionic environment.The rate theory of the enzyme-induced clotting of casein micelles is summarized. It is shown that the lag phase in the clotting is due to the second order of the coagulation reaction. Flocculation rate constants of micelles have been deduced from clotting times. Their relatively low values can be attributed to an orientational constraint. Practical consequences of the theory with respect to clot structure, gelation of sterilized products and cheese manufacture are discussed.

Modelling of heat stability and heat-induced aggregation of casein micelles in concentrated skim milk using a Weibullian model

2018 ◽  
Vol 71 (3) ◽  
pp. 601-612 ◽  
Author(s):  
Joseph Dumpler ◽  
Felicitas Peraus ◽  
Verena Depping ◽  
Bryndís Stefánsdóttir ◽  
Martin Grunow ◽  
...  
Keyword(s):  
Skim Milk ◽  
Heat Stability ◽  
Casein Micelles ◽  
Induced Aggregation

Physico-chemical stability of casein micelles cross-linked by transglutaminase as a function of acidic pH

2019 ◽  
Vol 19 ◽  
pp. 100103 ◽  
Author(s):  
Márcio H. Nogueira ◽  
Guilherme M. Tavares ◽  
Naaman F. Nogueira Silva ◽  
Federico Casanova ◽  
Paulo C. Stringheta ◽  
...  
Keyword(s):  
Chemical Stability ◽  
Acidic Ph ◽  
Casein Micelles ◽  
Physico Chemical

Use of a papain superpolymer to elucidate the structure of bovine casein micelles

1971 ◽  
Vol 229 (2) ◽  
pp. 423-430 ◽  
Author(s):  
S.H. Ashoor ◽  
R.A. Sair ◽  
N.F. Olson ◽  
T. Richardson
Keyword(s):  
Casein Micelles
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