Results 141 to 150 of about 2,242 (180)

Casein Micelles and Micelles of ϰ- and β-Casein

1982
The 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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Destabilization of Casein Micelles by Lysozyme

Canadian Journal of Biochemistry, 1971
Lysozyme has been demonstrated to bring about coagulation of casein micelles in a manner similar to the action of rennin. Both the rennin and lysozyme catalyzed reactions show similar pH optima and calcium ion dependencies. The differences in specificities of these two enzymes suggest that the carbohydrate moiety of the casein glycoprotein plays a ...
M, Bakri, F H, Wolfe
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Stability of buffalo casein micelles

Journal of Dairy Research, 1979
SUMMARYBuffalo 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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Properties of artificial casein micelles

Journal of Dairy Research, 1979
SUMMARYA survey is given of the relationships between various properties of artificial casein micelle systems and their composition with respect to αs1-, β and κ-casein, colloidal phosphate and citrate. Properties investigated were: the amount of colloidal phosphate, the micellar size, and the stability of the micelle towards dialysis, pressure ...
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Disulphide-linked caseins and casein micelles

International Dairy Journal, 1999
Abstract 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., Johnsen, L.B., Tsiora, A., Sørensen, E.S.; id_orcid 0000-0002-7050-3354, Thomsen, J.K., Nielsen, N.C., Jakobsen, H.J., Petersen, T.E.   +7 more
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Making cow-free caseins and casein micelles

Trends in Biotechnology
A key step in the precision fermentation of casein proteins is correct phosphorylation to generate one or more short linear sequence motifs (SLiMs) containing three or more phosphorylated seryl residues. The work of Balasubramanian et al. takes us a step closer to that goal by showing that two bacterial phosphokinases are promising alternatives to the ...
openaire   +2 more sources

Rennet-induced coagulation properties of yak casein micelles: A comparison with cow casein micelles

Food Research International, 2017
It is essential for yak cheese processing to understand the rennet-induced coagulation properties of gel formation from casein micelles. We have previously discovered that yak milk requires a longer incubation time but forms stronger gels compared with cow milk. In this study, we are aiming to understand the rennet-induced coagulation properties of yak
Yan, Zhang, Yuan, Li, Pengjie, Wang, Yanbao, Tian, Qi, Liang, Fazheng, Ren   +5 more
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Casein Micelles: The Colloid Chemical Approach

Canadian Institute of Food Science and Technology Journal, 1979
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.
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Casein micelle structure: location of κ-casein

Journal of Dairy Research, 1972
SummaryThe 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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Structure of casein micelles II. ? s1-casein

Colloid & Polymer Science, 1987
Following the earlier study of theβ- andϰ-casein micelle structure, we will now report results from theαs1-casein. Static and dynamic light scattering measurements were performed in a concentration range from 0.5 to 6.0 mg/ml atT=35 °C. A constant apparent molecular weight of 3.4×106 daltons was found over the whole range.
A. Thurn, W. Burchard, R. Niki
openaire   +1 more source