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2022
Caseins play a central role in the dairy sector, as it is their controlled coagulation that allows the conversion of milk into cheese, yoghurt and caseinates, but also the creation of high-quality co-products from whey. Understanding caseins, their association into casein micelles and the properties of casein micelles is thus very important.
Huppertz, Thom, Gazi, Inge
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Caseins play a central role in the dairy sector, as it is their controlled coagulation that allows the conversion of milk into cheese, yoghurt and caseinates, but also the creation of high-quality co-products from whey. Understanding caseins, their association into casein micelles and the properties of casein micelles is thus very important.
Huppertz, Thom, Gazi, Inge
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Hydration of casein micelles and caseinates: Implications for casein micelle structure
International Dairy Journal, 2017Abstract By studying the hydration of casein micelles using a variety of techniques, a distinction could be made between water that appeared bound by the protein (∼0.5 g g−1 protein), water associated with the κ-casein brush (∼1.0 g g−1 protein) and water entrapped in the casein micelles (∼1.8 g g−1 protein), yielding a total micellar hydration of ∼3.
Thom Huppertz +5 more
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Glycation Reactions of Casein Micelles
Journal of Agricultural and Food Chemistry, 2016After suspensions of micellar casein or nonmicellar sodium caseinate had been heated, respectively, in the presence and absence of glucose for 0-4 h at 100 °C, glycation compounds were quantitated. The formation of Amadori products as indicators for the "early" Maillard reaction were in the same range for both micellar and nonmicellar caseins ...
Ulrike, Moeckel +4 more
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Stability of buffalo casein micelles
Journal of Dairy Research, 1979SUMMARYBuffalo skim-milk is less heat stable than cow skim-milk. Interchanging ultracentrifugal whey (UCW) and milk diffusate with micellar casein caused significant changes in the heat stability of buffalo casein micelles (BCM) and cow casein micelles (CCM).
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Casein Micelles and Micelles of ϰ- and β-Casein
1982The tendency of proteins to associate in aqueous solution is well known. Most proteins form oligomers or undergo a series of consecutive association steps. A limited number, however, among which are ϰ- and β-casein, exhibit soaplike micellization.
T. A. J. Payens, H. J. Vreeman
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International Dairy Journal, 1999
Native casein micelles are considered as an association colloid, sterically stabilized by a layer of κ-casein hairs. This hairy or furry layer, as it is traditionally called, is considered as a polyelectrolyte brush. Its stability or extension is related to the brush density (renneting), charge density (pH) along the chain, concentration of (divalent ...
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Native casein micelles are considered as an association colloid, sterically stabilized by a layer of κ-casein hairs. This hairy or furry layer, as it is traditionally called, is considered as a polyelectrolyte brush. Its stability or extension is related to the brush density (renneting), charge density (pH) along the chain, concentration of (divalent ...
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Disulphide-linked caseins and casein micelles
International Dairy Journal, 1999Abstract Here we report the disulphide arrangement as well as the multimeric structure of α s2 - and κ -casein in various species. Furthermore, the structure of the casein micelle based on liquid-state and solid-state NMR studies is discussed.
Rasmussen, L.K. +7 more
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Casein micelle structure: location of κ-casein
Journal of Dairy Research, 1972SummaryThe effect of heat treatment on the rennet coagulation times (RCTs) of various casein–whey protein systems, the effect of pre-renneting centrifugal serum on the RCT of casein subsequently mixed with such serum, the influence of repeated centrifugation and resuspension at constant protein level on the RCT of such suspensions, and the rate and ...
P. F. Fox, P. A. Morrissey
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