Caseinates commercial

Casein commercially available 15-25 9 Resistant little or no change in weight small effect on mechanical properties generally suitable for practical use Fluorosint Quadrant EPP... 

All hydrophilic colloids possess some degree of protective action and gelatin, starch and casein are used commercially for this purpose. 

To the remainder of the casein solution add 0 5 to o 8 g. of finely powdered commercial trypsin, shake to dissolve, and place in a thermostat (or in an incubator) at 40 . After 15 minutes, remove 25 ml. and add a few drops of phenolphthalein it will now be found that the solution remains colourless. Run in carefully Mj 10 NaOH solution until the colour of the solution is just pink, add 5 ml, of neutralised formalin and then titrate against Mj 10 NaOH solution until the pink colour is just restored note the amount required. Remove fiirther quantities (rf 25 ml. at intervals which must be determined by the speed of the reaction. The following will probably make a suitable series i, 2, 3,... 

Products prepared from soy protein products and resembling chicken, ham, frankfurters, and bacon are available commercially. Soy protein isolates are used in place of milk proteins or sodium caseinate in products such as coffee creamers, whipped toppings, yogurt, and infant formulas (see Dairy substitutes). Soy protein products also are used in snacks and in baked foods. 

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). 

Casein is a protein found in a number of animal and vegetable materials but only one source is of commercial interest, cow s skimmed milk. The amount of casein in milk will vary but a typical analysis of cow s milk is ... 

Destruction of the casein micelles in the milk with subsequent precipitation of the casein can be accomplished in a number of ways. The action of heat or the action of alcohols, acids, salts and the enzyme rennet all bring about precipitation. In commercial practise the two techniques used employ either acid coagulation or rennet coagulation mechanisms. 

Formolised casein is a rigid hom-like material which may be made available in a wide variety of colours and patterns. By common consent it is recognised as having a pleasant feel and appearance and it is properties which are relevant to cuiTent commercial application. 

Casein is the only protein that has achieved commercial significance as a plastics raw material. Many other proteins are readily available in many vegetable material residues which arise from such processes as the extraction of oils and starches from seeds. It would be advantageous to countries possessing such residues if plastics could be successfully exploited commercially. Although plastics materials have been produced they have failed to be of value since they are invariably dark in colour and still have the water susceptibility and long curing times, both of which are severe limitations of casein. 

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. 

Tryptophane.—In an 8-1. (2-gal.) bottle is placed 600 g. of commercial casein (coarse powder), which is then covered with about 3200 cc. of tap water at 370 (Note 1). The bottle is shaken until all of the casein is moistened. A solution of 60 g. of anhydrous sodium carbonate (Note 2) and 6 g. of sodium fluoride (Note 3) in 1 1. of water at 37° is added. A thin paste of 20 g. of commercial pancreatin in roo cc. of water (370) is poured in. The mixture is covered with a layer of toluene (80 cc.), diluted to 6 1., stoppered, shaken thoroughly, and placed in a warm room or bath at 370. 

Though animal glue was used as an adhesive for more than 3000 years but its commercial manufacture started only in 1808. Later on starch, casein and rubber based adhesives also came into use. After 1940, several synthetic resin adhesives have been developed. Polyacrylates are used commercially. 

In addition to more rapid absorption of lipids in animals fed casein, another mechanism that may be operative is decreased clearance of circulating lipids. Rabbits fed a casein-based semipurified diet excreted significantly less cholesterol but more bile acids in their feces than animals fed a commercial diet (18). The total sterol excretion in feces of the animals fed the casein diet was half that of the rabbits fed the stock diet. Huff and Carroll (19) found that rabbits fed soy protein had a much faster turnover rate of cholesterol and a significantly reduced rapidly exchangeable cholesterol pool compared with rabbits fed casein. Similar studies performed in our laboratory revealed that the mean transit time for cholesterol was 18.4 days in rabbits fed soy protein, 36.8 days in rabbits fed casein, 33.7 days in rabbits fed soy plus lysine, and 36.3 days in rabbits fed casein plus arginine. These data suggest that addition of lysine to soy protein... 

Whole milk (2 litres) is diluted with an equal volume of water at 30°-40° and commercial rennet (0-1 g.), dissolved in a few cubic centimetres of water, is added. The mixture is then left at the same temperature until separation of the casein is complete (about two hours). The whey is filtered through a filter cloth, and after the liquid has run off the residue is pressed down well. The casein, which contains a great deal of fat, is ground in a mortar with a little 1 per cent sodium hydroxide solution 1 to 1-5 litres of sodium hydroxide solution of the same concentration are then poured on to the resulting paste, and the mixture is gently warmed in a porcelain basin until all but the fat dissolves. 

Which of the following is polydisperse with respect to chain length (a) casein, (b) commercial PS, (c) paraffin wax, (d) cellulose, or (e) Hevea brasiliensisl... 

Till this time, polymer science was largely empirical, instinctive, and intuitive. Several polymers were commercially available prior to World War I celluloid, shellac, Galalith (casein), Bakelite, and cellulose acetate plastics hevea rubber, cotton, wool, and silk rayon fibers Glyptal polyester coatings bitumen or asphalt, and coumarone-indene and petroleum resins. However, as evidenced by the chronological data shown in Table 1.1, there was little... 

Lucey, J.A., Srinivasan, M., Singh, H., Munro, P.A. (2000). Characterization of commercial and experimental sodium caseinate by multiangle laser light scattering and size-exclusion chromatography. Journal of Agricultural and Food Chemistry, 48, 1610— 1616. 

Figure 3. The effect of blending on solubility (I). Samples A, B, D, and E are soy protein isolates. Sample C is a commercial sodium caseinate. T is the temperature of the slurry after blending.

In comparison with sucrose (the annual production of which is 93 x 106 tonnes) and glucose or glucose-fructose syrups, only relatively small quantities of lactose are produced. However, it attracts commercial interest because it has some interesting properties and is readily available from whey, a by-product in the production of cheese or casein. World production of cheese is c. 1.4 x 107 tonnes, the whey from which contains c. 6 x 106 tonnes of lactose c. 0.3 x 106 tonnes of lactose are contained in the whey produced during casein manufacture. According to Horton (1993),... 

Addition of CaCl2 to about 0.2 M causes aggregation of the casein such that it can be readily removed by low-speed centrifugation. If calcium is added at 90°C, the casein forms coarse aggregates which precipitate readily. This principle is used in the commercial production of some casein co-precipitates in which the whey proteins, denatured on heating milk at 90°C for 10 min, co-precipitate with the casein. Such products have a very high ash content. 

Casein can be precipitated from solution by any of several salts. Addition of (NH4)2S04 to milk to a concentration of 260 g 1 1 causes complete precipitation of the casein together with some whey proteins (immunoglobulins, Ig). MgS04 may also be used. Saturation of milk with NaCl at 37°C precipitates the casein and Igs while the major whey proteins remain soluble, provided they are undenatured. This characteristic is the basis of a commercial test used for the heat classification of milk powders which contain variable levels of denatured whey proteins. 

Filtration through cross-linked dextrans (e.g. Sephadex, Pharmacia, Uppsala, Sweden) makes it possible to fractionate molecules, including proteins, on a commercial scale. It is possible to separate the casein and whey proteins by gel filtration but the process is uneconomical on an industrial scale. 

Casein, in a mainly micellar form, is destabilized and precipitated by freezing milk or, preferably, concentrated milk, at about — 10°C casein prepared by this method has some interesting properties but is not produced commercially at present. 

Since the caseins differ in lysine content (14, 24, 11 and 9 residues for asl-, xs2-, / - and tc-caseins, respectively) they have different dye-binding capacities. This feature may be of some commercial significance in connection with dye-binding methods for protein analysis if the ratio of the caseins in the milks of individual animals varies (as it probably does). It should also be considered when calculating the protein concentration of zones on electrophoretograms stained with these dyes. 

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