The casein micelle and its reactivity

2007 ◽  
Vol 87 (4-5) ◽  
pp. 385-387 ◽  
Author(s):  
Douglas G. Dalgleish
Keyword(s):  
Casein Micelle

A Rheo-optical Investigation into the Viscoelastic Moduli of Acidified Milk Gel

1999 ◽  
Vol 9 (6) ◽  
pp. 246-253 ◽  
Author(s):  
E. O. Arikainen ◽  
J. C. Earnshaw ◽  
A. Wehling ◽  
E. Waghorne
Keyword(s):  
Correlation Function ◽  
Mean Square Displacement ◽  
Slow Motion ◽  
Casein Micelle ◽  
Optical Investigation ◽  
Viscoelastic Moduli ◽  
Decay Times ◽  
Delay Times ◽  
Intensity Correlation Function ◽  
Viscoelastic Modulus

Abstract Diffusing wave spectroscopy (DWS) in the backscattering geometry was employed to observe the evolution of the intensity correlation function during the acidification of skimmed milk by gluconic-δ-lactone (GDL). At the stage when the formation of casein particle gel is largely complete the correlation function at shorter decay times reveals the local structural arrest of the casein micelles, whereas at longer delay times it illustrates the hindered slow motion of casein micelle aggregates. We use the principles of the approach suggested by Mason, Gang and Weitz, linking the optically measured mean square displacement, <Δr2(t)>, of the microscopic particles in a dense colloid to its viscoelastic properties, to provide an estimate of the frequency dependent viscoelastic modulus of the acidified milk gel (AMG). We compare the viscoelastic moduli measured by the conventional mechanical rheometry with the optically measured ones. The results of the two different experimental methods are found to be in reasonable agreement.

Contribution of casein micelle size and proteolysis on protein distribution and sediment formation in UHT milk during storage

2021 ◽  
Vol 117 ◽  
pp. 104980
Author(s):  
Marije Akkerman ◽  
Lene Buhelt Johansen ◽  
Valentin Rauh ◽  
Nina Aagaard Poulsen ◽  
Lotte Bach Larsen
Keyword(s):  
Casein Micelle ◽  
Protein Distribution ◽  
Uht Milk ◽  
Micelle Size ◽  
Sediment Formation

Hydrophobic interactions in human casein micelle formation: β-casein aggregation

1989 ◽  
Vol 56 (3) ◽  
pp. 427-433 ◽  
Author(s):  
Charles W. Slattery ◽  
Satish M. Sood ◽  
Pat Chang
Keyword(s):  
Light Scattering ◽  
Conformational Transition ◽  
Hydrophobic Interactions ◽  
Micelle Formation ◽  
Tryptophan Fluorescence ◽  
Phosphate Esters ◽  
Casein Micelle ◽  
Protein Association ◽  
P Protein ◽  
Micelle Size

SummaryThe association of non-phosphorylated (0-P) and fully phosphorylated (5-P) human β-caseins was studied by fluorescence spectroscopy and laser light scattering. The tryptophan fluorescence intensity (FI) level increased between 20 and 35 °C, indicating a change in the environment of that residue. A similar transition occurred when ANS was used as a probe. Transition temperatures were slightly lower in 10 mM-CaCl2 but were not affected by an equivalent increase in ionic strength caused by NaCl. The magnitude of the FI change was less for the 5-P than the 0-P protein but was increased for both by CaCl2 addition. These FI data were characteristic of a conformational change and this was supported by fluorescence polarization which indicated that with CaCl2, tryptophan and ANS mobility increased at the transition temperature even though the extent of protein association also increased. Light scattering suggested that protein association proeeeded with the primary formation of submicellar aggregates containing 20–30 monomers which then associated further to form particles of minimum micelle size (12–15 submicelles), and eventually larger. The temperature of precipitation of the 5-P form in the presence of CaCl2 was lower than the conformational transition and suggested that both hydrophobic interactions and Ca bridges between phosphate esters on adjacent molecules are important in micelle formation.

scholarly journals Aggregation of casein micelle from bovine milk by wheat germ lectin.

1978 ◽  
Vol 42 (10) ◽  
pp. 1923-1926 ◽  
Author(s):  
Masaaki YOSHIKAWA ◽  
Kyoya TAKAHATA ◽  
Ryuzo SASAKI ◽  
Hideo CHIBA
Keyword(s):  
Wheat Germ ◽  
Bovine Milk ◽  
Casein Micelle ◽  
Wheat Germ Lectin

The Structure of the Casein Micelle of Milk and Its Changes During Processing

2012 ◽  
Vol 3 (1) ◽  
pp. 449-467 ◽  
Author(s):  
Douglas G. Dalgleish ◽  
Milena Corredig
Keyword(s):  
Casein Micelle

Mineral partitioning in milk and milk permeates at high temperature

2011 ◽  
Vol 79 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Divina D Kaombe ◽  
Yanhong Du ◽  
Michael J Lewis
Keyword(s):  
High Temperature ◽  
Calcium Phosphate ◽  
Temperature Dependence ◽  
Casein Micelle ◽  
Soluble Phase ◽  
Ionic Calcium ◽  
Separation Temperature ◽  
Two Temperatures ◽  
Lower Temperature ◽  
Mineral Partitioning

The soluble phase of milk was separated at 20 and 80°C using ultrafiltration. The resulting permeates were then subjected to further ultrafiltration and dialysis at close to these two temperatures. It was found that pH, Ca2+ and soluble Ca decreased as the separation temperature increased both in original UF permeates and in dialysates obtained from these permeates, but P decreased only slightly. The major reason for these changes was due to the precipitation of calcium phosphate/citrate complexes onto the casein micelle with concomitant release of H+. The pH of both permeates and dialysates from milk at 20°C were slightly higher than for milk. When UF permeates collected at 20 and 80°C, were each dialysed at both these temperatures, the dialysate collected at 80°C showed much less temperature dependence for pH and ionic calcium compared with that collected at 20°C. This is in contrast to milk, which shows considerable temperature dependence for pH and ionic calcium. Further experiments revealed that the pH and Ca2+ concentration of permeates showed high temperature dependence above the temperature at which they were separated, but a much lower temperature dependence below that temperature. These findings suggest that dialysis and UF of milk at high temperature provide the best means yet for estimating the pH and ionic calcium of milk at that temperature.

Hydration of casein micelles and caseinates: Implications for casein micelle structure

2017 ◽  
Vol 74 ◽  
pp. 1-11 ◽  
Author(s):  
Thom Huppertz ◽  
Inge Gazi ◽  
Hannemieke Luyten ◽  
Hans Nieuwenhuijse ◽  
Arno Alting ◽  
...  
Keyword(s):  
Casein Micelle ◽  
Casein Micelles ◽  
Micelle Structure

scholarly journals Sedimentation Analysis of Bovine Milk Casein Micelle at pH 6.8 and pH 5.8

1973 ◽  
Vol 20 (10) ◽  
pp. 473-477 ◽  
Author(s):  
I LIANG ◽  
ZENICHIRO HAMAUZU ◽  
SACHIO MATSUMOTO ◽  
DAIZO YONEZAWA
Keyword(s):  
Bovine Milk ◽  
Casein Micelle ◽  
Sedimentation Analysis ◽  
Milk Casein

scholarly journals Structural Insights into the Bovine Casein Micelle: Small Angle X-Ray Scattering Studies and Correlations with Spectroscopy

1990 ◽  
Vol 73 (12) ◽  
pp. 3592-3601 ◽  
Author(s):  
H.M. Farrell ◽  
H. Pessen ◽  
E.M. Brown ◽  
T.F. Kumosinski
Keyword(s):  
Small Angle ◽  
Casein Micelle ◽  
X Ray ◽  
X Ray Scattering ◽  
Structural Insights ◽  
Ray Scattering
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