Solubility casein

K-Casein is soluble in Ca2+ at all concentrations up to those at which general salting-out occurs. Solubility is independent of temperature and pH (outside the pH range at which isoelectric precipitation occurs). Not only is K-casein soluble in the presence of Ca2+ but it is capable of stabilizing asl-, as2- and /9-caseins against precipitation by Ca2+ (section 4.5.8). 

Most commercial aluminum formate is monobasic aluminum diformate because of the difficulties involved in triformate preparation. The main appHcation is in textile waterproofing. Aluminum formate reacts with casein to form a water-soluble complex, which can emulsify paraffin and certain other waxes. Fabrics immersed in these emulsions are rendered water repellent (26—28). 

Whey concentration, both of whole whey and ultrafiltration permeate, is practiced successfully, but the solubility of lactose hmits the practical concentration of whey to about 20 percent total sohds, about a 4x concentration fac tor. (Membranes do not tolerate sohds forming on their surface.) Nanofiltration is used to soften water and clean up streams where complete removal of monovalent ions is either unnecessary or undesirable. Because of the ionic character of most NF membranes, they reject polyvalent ions much more readily than monovalent ions. NF is used to treat salt whey, the whey expressed after NaCl is added to curd. Nanofiltration permits the NaCl to permeate while retaining the other whey components, which may then be blended with ordinaiy whey. NF is also used to deacidify whey produced by the addition of HCl to milk in the production of casein. 

Both acids and alkalis will adversely affect the material. Strong alkalis and acids will cause decomposition. The water absorption is high and consequently casein is easily stained. As a corollary to this it may be dyed without difficulty. Acidic and basic water-soluble dyes are normally used. Typical properties of casein plastics are given in Table 30.2. 

Nitrogen sources include proteins, such as casein, zein, lactalbumin protein hydrolyzates such proteoses, peptones, peptides, and commercially available materials, such as N-Z Amine which is understood to be a casein hydrolyzate also corn steep liquor, soybean meal, gluten, cottonseed meal, fish meal, meat extracts, stick liquor, liver cake, yeast extracts and distillers solubles amino acids, urea, ammonium and nitrate salts. Such inorganic elements as sodium, potassium, calcium and magnesium and chlorides, sulfates, phosphates and combinations of these anions and cations in the form of mineral salts may be advantageously used in the fermentation. 

Milk from cows contains 3.2% protein, about 80% of which is casein. Casein is isolated by a precipitation process from milk, involving heating, rinsing to remove whey, and drying to a powder. The yield is about 3 kg/ 100 kg skim milk. Rennet casein is obtained when the casein is precipitated by chymosin enzyme, also known as rennet, and acid casein is produced when precipitation is accomplished by acidification. Acid casein is usually found in the form of sodium caseinate or calcium caseinate, which are water-soluble salts. Caseinates are made by reacting NaOH or CaOH with a slurry of casein curd or powder and then spray drying (Southward, 2010). 

Casein exists in milk in the form of a calcium derivative pH 4.6 is the isoelectric point of free casein, which is soluble to the extent of only 0.11 g. per liter.1... 

The present process is based in large part upon that of Van Slyke and Baker, the modifications depending upon the observation that casein forms far more soluble compounds with univalent than with bivalent bases at neutral reactions. 

CCP in milk is mentioned in connection with casein above (Section VI.C). Fluorapatite is a major constituent of phosphate rocks, and a constituent, probably important, of human tooth enamel for those whose drinking water contains significant amounts of naturally occurring or added fluoride. Fluorapatite is significantly less soluble than hydroxyapatite - the relationship between the solubilities of fluorapatite and hydroxyapatite parallels (but is much less extreme than) that between calcium fluoride (Ksp — 3.9 x 10 11 mol3 dm-9) and calcium hydroxide (Ksp = 7.9 x 10 6 mol3 dm 9). Calcium diphosphate, Ca2P207, is believed to be the least soluble of the calcium phosphates. 

Furthermore, addition of lysine to soy protein markedly increased the rate of lipid absorption and addition of arginine to casein slowed lipid absorption. The slowed absorption of lipids in animals fed soy protein is similar to that reported for soluble fibers such as pectin and guar gum that act to lower serum cholesterol concentrations in a number of animal species, including humans. 

Another fat-soluble vitamin, E, was found by Evans and Bishop in 1923. Pregnant rats on a defined diet (alcohol-extracted casein, cornstarch, and lard) supplemented with butter (vitamins A and D) and yeast extract (vitamin B group) produced few young because of fetal resorption. Male rats on the same diet were sterile. The disorders, which have not been identified in man, were corrected by wheat-germ oil, from which tocopherol, the active ingredient, was isolated in 1936. In spite of intensive investigations and a recognition that the vitamin is an antioxidant and destroyer of free radicals, the function of vitamin E remains obscure. 

Chemical reactions Polymerization of casein and whey proteins are due to some kind of chemical reactions. The different proteins as found in the supernatant of milk after precipitation at pH 4.6 are collectively called whey proteins. These globular proteins are more water soluble than caseins and are subject to heat dena-turation. Denaturation increases their water-binding capacity. The principal fractions are P-lactoglobulin, a-lactalbumin, bovine serum albumin (BSA), and immunoglobulins (Ig). 

Only proteins that contain proline bind polyphenols. Asano et al. (1982) demonstrated that the haze-forming activity of a protein is roughly proportional to the mole percentage of proline it contains (see Fig. 2.3). DNA has codes for exactly 20 amino acids. If each of these were equally present in a protein, there would be 5 mol% of each one. In fact, most proteins have much less proline than this. There are a few exceptions. Casein has about 8 mol% proline and the grain prolamins (proline-rich, alcohol-soluble proteins) are even higher. Hordein, the barley prolamin, contains about 20 mol% proline. As a result, it readily forms haze with polyphenols and is the main beer haze-active (HA) protein. Hordein contains even more glutamine (Q) than proline (P), and often these amino acids are adjacent in the protein (see Fig. 2.4). In fact, the sequence P-Q-Q-P occurs... 

This kind of experiment was performed in an attempt to show that reduction in labelled amino acid uptake into the soluble pool, observed after as little as 15 min of ozonation (Fig. 6), could be an early or primary event in ozone damage to the soybean trifoliate leaf. It was necessary in this case for the pools to be loaded with unlabelled casein hydrolysate after treatment of the plant, in order to maintain vivo ozone treatment and because it has been reported that high endogenous amino acid levels can confer a degree of resistance to ozone damage (14, 15). 

Table IV shows typical results of the pool overloading experiments in the soybean trifoliate leaf. Visible damage to ozonated plants after 24 hr incubation was, as usual, taken as necessary for an experiment to be valid. Clearly, incorporation of label into protein was reduced where casein hydrolysate had been used in control and treated discs to overload the soluble pools. Just as clearly, total counts present in the soluble pool of treated tissue were reduced by ozonation whatever the after-treatment. The reduction of label in the soluble pool in control and ozonated discs due to casein treatment was approximately 30% in each case the reduction of label incorporation due to ozone was about 36% in the case of water treatment and about 14% in the case of casein treatment.

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