Casein Protein

Vitamin A (845 RE/L) and vitamin D (913 RE/L) may be added to fortify evaporated milk. Other possible ingredients are sodium citrate, disodium phosphate, and salts of carrageenan. Phosphate ions maintain an appropriate salt balance to prevent coagulation of the protein (casein) during sterilization. The amount of phosphate added depends on the amount of calcium and magnesium present. 

Nitric add also reacts with proteins (casein in milk [test tube] and albumen in eggs) to give a characteristic yellow color. 

Prior to the study by Chen et al. (140), only one publication discussed the use of the protein casein as a drug carrier (141). Chen et al. systematically compared the many features of albumin and casein microspheres—morphology, drug (adriamycin) incorporation, and release—in an effort to identify important factors in the antitumor effect of this delivery system. 

Figure 16.5 Immunostained peptide arrays after various treatments of fixation, protein cross-linking, and antigen retrieval, as indicated at the top. Each row has a different peptide that is immunoreactive for the antibody denoted to the left. Column A represents the baseline condition, without any treatment whatsoever. Column B shows immunoreactivity of each peptide after overnight formalin fixation. Column C shows the immunoreactivity after first coating the array with an irrelevant protein (casein) followed by overnight formalin fixation. Column D illustrates the immunoreactivity of the peptides after the treatment of column C, and then antigen retrieval. Reproduced with permission from Reference 15, 2006 American Society for Clinical Pathology.

These products are made by adding protein to flour. While whey protein, soya protein, casein and yeast can be used the protein normally employed is pure vital wheat gluten. 

Protein Caseins (3-Lactoglobulin cx-Lactalbumin Serum albumin IgG... 

Table I. Serum Lipids and Aortic Atherosclerosis in Rabbits fed Casein, Soy Protein, Casein Arginine, or Soy Lysine...

A greater effect is apparent in postmenopausal women compared with men. The protein component seems to play a crucial role in the cardio-protective effect of soy. When soy-extracted phytoestrogens are added to animal-derived protein (casein), no effects on lipids are observed (Greaves et al., 1999). It is therefore clear that both the proteins from soy and the phytoestrogens need to be present to have a beneficial effect on lipid. In the presence of soy protein, the lipid-lowering effect is dose dependent on the phytoestrogen present (Crouse et al., 1999). 

The milk protein casein is a well-known self-assembling food protein (see section 1.1 in chapter six for further details). Semo and coworkers (2007) have demonstrated that casein-based nanoparticles reassembled from sodium caseinate and ionic calcium can provide partial protection... 

Co-preclpltate is an insoluble milk protein product that is produced by heating skinimllk to high temperatures ( > 90 C) to denature the whey proteins and complex them with the casein micelles. The heated system is subsequently adjusted to isoelectric point conditions of pH 4.5-5 to precipitate the complexed whey protein-casein micelles, centrifuged or filtered to recover the precipitate, washed and dryed. The resulting product, which is virtually insoluble, exhibits only minor functionality in most typical emulsification applications. 

Milk has a relatively high content of the protein casein, which acts as an inexpensive blocking agent. 

Nitrogenous Substances,—These consist mainly of proteins (casein, albumin) and to a small extent of other substances (lecithin, etc.). They may be determined together or separately from the nitrogen estimated by the Kjeldahl-Ulsch method (Vol. I, p. 122) ... 

Synthetic fibres made from proteins are Aralac from milk protein casein, Vicara from corn protein zein, and Saralon from peanut protein. These fibres look like wool and can also be dyed just like wool or silk is dyed. These fibres are blended with wool to add strength. 

Our laboratory has completed a series of studies designed to evaluate the simultaneous effects of dietary protein and fat on 7,12-dimethylbenz(a)anthracene (DMBA)-induced breast cancer in rats. Sprague-Dawley female rats were assigned to nine diets in a 3 x 3 factorial arrangement with protein (casein) at 8, 16, and 32% of kcals and fat (corn oil) at 12, 24, and 48% of kcals. As fat content was increased, all nutrients other than carbohydrate were adjusted to remain constant with respect to calories. Forty rats were assigned to each diet for each of three experiments (Figure 1) to examine initiation, promotion, and the combined phases of chemically-induced carcinogenesis. 

Other spices, too, for example, mustard, paprika, flour additives, and garlic (Dannaker and White 1987, Scholl and Jensen-Jarolim 2004) as well as many food products, such as milk proteins (casein), whey proteins (a-lactalbumin, P-lactoglobulin), and wheat proteins, which are not always obvious food ingredients (hidden ingredients) (Lopata and Potter 2000, Chapters 6 and 13), may cause adverse reactions. 

It is interesting to see that proteins with high Q-values above 1400 as e.g. soybean protein, casein wheat gluten, potato protein, Zein are the "parents" of bitter peptides, whereas no bitter peptides have been isolated from hydrolysates prepared from collagen or gelatin, proteins with Q-values below 1300. 

Milk proteins can be classified into two groups, caseins and whey proteins. Their proportion differs widely in human and cow s milk. The whey proteins/ caseins ratio is 20 80 in cow s milk and 60 40 in human milk. On the other hand, water-soluble whey proteins are much less abundant than caseins in cow s milk. 

Among its effects on the epithelial cells of the mammary alveoli prolactin stimulates the production of the major milk proteins casein and lactalbumin [64,66-69,74-76]. Mouse mammary explants incubated in vitro with insulin and a corticosteroid produce very little of these proteins, but addition of prolactin to the culture medium induces their synthesis 10-20-fold within about 24 h. As has already been discussed, there is some uncertainty about the importance of glucocor-... 

The adverse effects of PPO on noctuid larvae result from reduced bioavailability of amino acids caused by the covalent binding of oxidized chlorogenic acid to protein. When dietary protein (casein) was treated with PPO and chlorogenic acid, a substantial reduction in in vitro protein digestibility occurred. This reduction in digestibility may result from alkylation of lysine and/or protein cross-linking, which may impair the ability of the insect s trypsin to hydrolyze the protein. 

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