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The kinetic pattern of the second step of the milk-clotting process is influenced by the cooperative nature of micellar flocculation, [16] [13] whereas the rheological properties of the gel formed depend on the type of action of the proteases, the type of milk, and the patterns of casein proteolysis. [13]
Casein (/ ˈ k eɪ s iː n / KAY-seen, from Latin caseus "cheese") is a family of related phosphoproteins (αS1, aS2, β, κ) that are commonly found in mammalian milk, comprising about 80% of the proteins in cow's milk and between 20% and 60% of the proteins in human milk. [1]
Kappa-casein is the only glycosylated casein protein and GMP, which makes up much of Kappa-casein, is also glycosylated. The glycans make GMP the only portion of the casein micelle that is water soluble after curdling has occurred, and thus, the only fraction of casein protein to dissolve into the whey.
One of the main actions of rennet is its protease chymosin cleaving the kappa casein chain. [2] Casein is the main protein of milk. Cleavage removes the slightly negatively charged glycomacropeptide (GMP) from the surface of the casein micelle. Because negative charges repel other negative charges, the GMP prevents casein micelles from adhering ...
The emulsifying property of surfactants is also the basis for emulsion polymerization. Micelles may also have important roles in chemical reactions. Micellar chemistry uses the interior of micelles to harbor chemical reactions, which in some cases can make multi-step chemical synthesis more feasible.
These casein micelles aggregated and precipitated when they approach the absolute zeta potential values at pH 4.0 – 4.5. [25] When the heat treated and denatured, whey protein is covering the casein micelle, isoelectric point of the micelle elevated to the isoelectric point of β lactoglobulin (approximately pH 5.3). [26]
Phosphate groups attached to the casein proteins in the cheese curd are highly charged but repel each other. Naturally high levels of calcium ions are found in the casein micelles of the cheese curd and allow the casein micelles to form a more rigid network by bridging the steric hindrance created by the self-repelling phosphate groups.
The largest structures in the fluid portion of the milk are "casein micelles": aggregates of several thousand protein molecules with superficial resemblance to a surfactant micelle, bonded with the help of nanometer-scale particles of calcium phosphate. Each casein micelle is roughly spherical and about a tenth of a micrometer across.
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