Caseins processing

Chobert, J.-M., Briand, L., and Haertle, T. 1998b. Influence of G187W/K188F/D189Y mutation in the substrate-binding pocket of trypsin on (3-casein processing. J. Food Biochem. 22, 529-545. 

J. Morgan, From milk to manicure sets the casein process , Plastiquarian, Spring 1989, 2, 12-13. 

Minerals, particularly Bentonite, ate used to remove proteins that tend to cause haze in white wines. The natural tannin of ted wines usually removes unstable proteins from them. Excess tannin and related phenols can be removed and haze from them prevented by addition of proteins or adsorbents such as polyvinylpyttohdone. Addition of protein such as gelatin along with tannic acid can even be used to remove other proteins from white wines. Egg whites or albumen ate often used to fine ted wines. Casein can be used for either process, because it becomes insoluble in acidic solutions like wines. 

Protein-Based Substitutes. Several plant and animal-based proteins have been used in processed meat products to increase yields, reduce reformulation costs, enhance specific functional properties, and decrease fat content. Examples of these protein additives are wheat flour, wheat gluten, soy flour, soy protein concentrate, soy protein isolate, textured soy protein, cottonseed flour, oat flour, com germ meal, nonfat dry milk, caseinates, whey proteins, surimi, blood plasma, and egg proteins. Most of these protein ingredients can be included in cooked sausages with a maximum level allowed up to 3.5% of the formulation, except soy protein isolate and caseinates are restricted to 2% (44). 

In the late 1800s, when the demand for coated paper for the halftone printing process increased, casein rapidly replaced glue. Casein forms a hard, tough film when dry, and can be waterproofed easily with formaldehyde (qv). The properties of soy protein are similar to those of casein, and soy protein has been substituted for it in many types of coated papers requiring a casein-type binder (see Soybeans and other oilseeds). Casein, a valuable food product, is seldom used as a paper adhesive, in spite of its excellent adhesive properties. 

Reclaimed mbber, which is widely used in dry mbber, has Htde use in latex compounding. A dispersion or artificial latex of the red aim must be made by a rather expensive process of milling in dispersing agents, eg, soaps and casein, and water. Some reclaim dispersions are used in latex compounds for such things as spread mbber goods and adhesives and fiber binders to reduce cost. However, for most latex compounds, it is not desirable because of the poor physical properties it imparts and the resultant darkening of the compound. 

Membrane-retained components are collectively called concentrate or retentate. Materials permeating the membrane are called filtrate, ultrafiltrate, or permeate. It is the objective of ultrafiltration to recover or concentrate particular species in the retentate (eg, latex concentration, pigment recovery, protein recovery from cheese and casein wheys, and concentration of proteins for biopharmaceuticals) or to produce a purified permeate (eg, sewage treatment, production of sterile water or antibiotics, etc). Diafiltration is a specific ultrafiltration process in which the retentate is further purified or the permeable sohds are extracted further by the addition of water or, in the case of proteins, buffer to the retentate. 

Phosphates, which react with calcium to reduce the calcium ion activity, assist in stabilizing calcium-sensitive proteins, eg caseinate and soy proteinate, during processing. Phosphates also react with milk proteins. The extent of the reaction depends upon chain length. Casein precipitates upon addition of pyrophosphates, whereas whey proteins do not. Longer-chain polyphosphates cause the precipitation of both casein and whey proteins. These reactions are complex and not fully understood. Functions of phosphates in different types of dairy substitutes are summarized in Table 9 (see also Food additives). 

Fig. 3. Schematic process flow diagram for an imitation cheese product having the following formulation dry ingredients, calcium caseinate (or rennet casein), 24.5 wt % tapioca flour, 3.0 wt % salt, 2.16 wt % adipic acid, 0.6 wt % vitamins and minerals, 0.1 wt % sorbic acid (mold inhibitor), 0.5 wt % fat—color blend, soybean oil hydrogenated to a Wiley melting point of 36°C, 21.3 wt % lactylated monoglycerides, 0.05 wt % red-orange coloring, 0.01 wt...

Casein may be considered to be a conjugated protein, that is the protein is associated in nature with certain non-protein matter known as prosthetic groups. In the case of casein the prosthetic group is phosphoric acid. The protein molecule is also associated in some way with calcium. The presence of these inorganic materials has an important bearing on the processability and subsequent use of casein polymers. 

Addition of acetic or mineral acid to skimmed milk to reduce the pH value to 4.6, the isoelectric point, will cause the casein to precipitate. As calcium salts have a buffer action on the pH, somewhat more than the theoretical amount of acid must be used. Lactic acid produced in the process of milk souring by fermentation of the lactoses present by the bacterium Streptococcus lactis will lead to a similar precipitation. 

In the rennet coagulation process fresh skimmed milk is adjusted to a pH of six and about 40 ounces of a 10% solution of rennet are added per 100 gallons of milk. The initial reaction temperature is about 35°C and this is subsequently raised to about 60°C. The coagulation appears to take place in two stages. Firstly the calcium caseinate is converted to the insoluble calcium paracaseinate and this then coagulates. 

Great care is essential in controlling the temperature and the coagulation process as otherwise impurities, particularly other proteins, will be brought down with the casein. Such impurities will adversely affect the transparency of the product. 

Casein plastics are today produced by the dry process . Although a wet process was used originally in Great Britain it has been obsolete for over 50 years and need not be discussed here. 

The use of casein plastics was severely curtailed with the development of synthetic polymers, particularly after the Second World War. In addition stricter regulations concerning health and safety at work will have caused attention to be drawn to the formolising process. In the experience of the author the environment surrounding the formolising baths is most unpleasant and this will have accelerated the demise of the casein manufacturing industry. 

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. 

Of these materials zein, the maize protein, has been used for plastics on a small scale. It can be cross-linked by formaldehyde but curing times are very long. Complicated bleaching processes have led to the production of almost colourless samples in the laboratory but the process cannot readily be extended to large-scale operation. The cured product has a greater water resistance than casein. Proteins from soya bean, castor bean and blood have also been converted into plastic masses but each have the attendant dark colour. 

In addition to their nutrient value, casein proteins have many other uses. They are good emulsifiers, helping fats to stay suspended in water-based products such as milkshakes, coffee creamers, and ice creams. They are used as binders in processed meats (lunch meats, sausages, etc.). 

Seven diets were constructed from purified natural ingredients obtained from either C3 (beet sugar, rice starch, cottonseed oil, wood cellulose, Australian Cohuna brand casein, soy protein or wheat gluten for protein) or C4 foodwebs (cane sugar, corn starch, com oil, processed corn bran for fiber, Kenya casein for protein) supplemented with appropriate amounts of vitamins and minerals (Ambrose and Norr 1993 Table 3a). The amino acid compositions of wheat gluten and soy protein differ significantly from that of casein (Ambrose and Norr 1993). 

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 refers to a family of proteins, namely, ttgi-, 0. 2-, p-, and k-caseins (Table 5.1). Digestion of a- and p-caseins leads to production of peptides that may bind to opioid receptors that exist in the nervous, endocrine, immime, or gastrointestinal system (Kampa et ah, 1996 Meisel, 2004). These compoimds may modulate absorption processes in the gut and can potentially affect gastrointestinal fimction through transit... 

Coextrusion is the process of extruding two or more materials simultaneously or in tandem. It allows a combination of an ingredient such as wheat flour, which is inexpensive and easily enriched with vitamins and minerals, with dairy protein, which provides functionality and texture. For example, an early coextrusion of wheat flour and rennet casein was performed by van de Voort et al. (1984), who obtained products with varying characteristics depending on process parameters. 

Helstad, K. M., Bream, A. D., Trckova, J., Paulsson, M., and Dejmek, P. (2005). Nano-heological properties of casein. In "Food Colloids Interactions, Microstructure and Processing", (E. Dickinson, Ed.), pp. 218-229. The Royal Society of Chemistry, Cambridge. 

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