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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.   +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 ...
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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
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Location of κ-casein in milk micelles

Biochimica et Biophysica Acta (BBA) - Protein Structure, 1969
Abstract An attempt was made to determine the whereabouts of κ-casein in the milk casein system by locating antibodies to κ-casein through electron microscopy. No evidence could be found for the occurrence of a κ-casein stabilizing “coat” on casein micelles using either purified antibody or ferritin conjugated antibody.
R M, Parry, R J, Carroll
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Interaction of ionic materials with casein micelles

Journal of Dairy Research, 1979
SUMMARYA suspension of casein micelles in a milk-salts solution bound highly cationic polypeptides and charged surfactants extensively, and globular proteins and low molecular weight amines less extensively. All additives were bound equally to native micelles and to a rennet coagulum.
M.L. Green, R.J. Marshall
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Rennet coagulation of casein micelles and heated casein micelles in presence of sucrose or lactose

Food Research International, 2004
Abstract The effects of sucrose and lactose on the kinetics of the aggregation step of milk enzymic coagulation were studied by turbidimetric measurements for casein micelles previously heated (HCM) or not heated (CM). The initial aggregation rate showed an initial destabilizing effect by addition of polysaccharides, which could be attributed to ...
Miryam Pires   +3 more
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Casein micelle interactions

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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