Results 21 to 30 of about 9,140 (274)
Darwinian transformation of a 'scarcely nutritious fluid' into milk [PDF]
, 2012 In an early challenge to an aspect of Darwin’s theory of natural selection, Jackson Mivart contended that milk could not have evolved ‘from a scarcely nutritious fluid from an accidentally hypertrophied cutaneous gland’.
Carver, J.A., Holt, C.
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Electrosorption of Pectin onto Casein Micelles [PDF]
Biomacromolecules, 2002 Pectin, a polysaccharide derived from plant cells of fruit, is commonly used as stabilizer in acidified milk drinks. To gain a better understanding of the way that pectin stabilizes these drinks, we studied the adsorption and layer thickness of pectin on casein micelles in skim milk dispersions.
Tuinier, R., Rolin, C., de Kruif, C.G.
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Research Progress on Structural Properties of Casein Micelles and Their Application in Delivery Systems [PDF]
Shipin KexueMilk is considered an important source of protein in human diets. As the major protein component in milk, casein has attracted extensive attention from scholars due to its biparental structure and self-assembly properties. However, the poor pH, Ca2+, and
YE Jingying, WU Fan, ZHANG Zhaoyue, WEN Xin, NI Yuanying, LI Mo
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BMC Cell Biology, 2010 Background Caseins, the main milk proteins, aggregate in the secretory pathway of mammary epithelial cells into large supramolecular structures, casein micelles.
Le Parc Annabelle +2 more
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Journal of Dairy Science, 2023 : Liquid micellar casein concentrate (MCC) is an ideal milk-based protein ingredient for neutral-pH ready-to-drink beverages. The texture and mouthfeel of liquid MCC-based beverages depend on the beverage protein content, as well as the composition of ...
Joice Pranata +3 more
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Implications of kappa-casein evolutionary diversity for the self-assembly and aggregation of casein micelles [PDF]
Royal Society Open Science, 2019 Milk alpha-, beta- and kappa-casein proteins assemble into casein micelles in breast epithelial cells. The glycomacropeptide (GMP) tails of kappa-casein that extend from the surface of the micelle are key to assembly and aggregation.
Jean Manguy, Denis C. Shields
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Milk lacking α-casein leads to permanent reduction in body size in mice.
PLoS ONE, 2011 The major physiological function of milk is the transport of amino acids, carbohydrates, lipids and minerals to mammalian offspring. Caseins, the major milk proteins, are secreted in the form of a micelle consisting of protein and calcium-phosphate.We ...
Andreas F Kolb +9 more
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The influence of high temperatures on milk proteins [PDF]
Hemijska Industrija, 2002 High temperatures Induce certain changes in milk constituents, but the degree of these changes depends on both the temperature and time of heat treatment. The most pronounced changes take place in milk proteins. The forewarming of milk causes an increase
Maćej Ognjen D. +2 more
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Structural studies of hydrated samples of amorphous calcium phosphate and phosphoprotein nanoclusters [PDF]
, 2016 There are abundant examples of nanoclusters and inorganic microcrystals in biology. Their study under physiologically relevant conditions remains challenging due to their heterogeneity, instability, and the requirements of sample preparation.
Holt, Carl +8 more
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Preparation of Casein Phosphopeptides from Casein Micelles by Ultrafiltration [PDF]
Bioscience, Biotechnology, and Biochemistry, 1995 Casein phosphopeptides (CPPs), which inhibit the precipitation of calcium phosphate in the intestines, were prepared as CPP-calcium phosphate complexes from casein micelles by the ultrafiltration method. The prepared CPPs hardly contained any other peptides, so there was no need to treat with active carbon to remove the bitter peptides.
T, Ono, T, Ohotawa, Y, Takagi, T, Ito
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