Applications of caseins

World production of casein and caseinates is about 250 000 tonnes per annum. While some casein is still used for industrial applications, the vast majority is used in foods, in which it has numerous applications, as summarized in Table 4.9. 

Many whey proteins possess interesting functional, nutritional, physiological or pharmaceutical properties. Unfortunately, all the proteins in whey are present at low concentrations and hence are relatively expensive to produce, although at least some of them are capable of carrying high production 

Used in Bread, biscuits/cookies, breakfast cereals, cake mixes, pastries, frozen cakes and 

Effect Nutritional, sensory, emulsifier, dough consistency, texture, volume/yield 

Used in Imitation cheeses (vegetable oil, caseins/caseinates, salts and water) 

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Chemical nature Isolation of casein from milk Production of casein plastics Properties of casein Applications Miscellaneous Protein Plastics Derivatives of Natural Rubber Gutta Percha and Related Materials Shellac... 

Quinn and Paton (16) observed that the intensity and duration of mixing influenced the water uptake of the materials investigated, and that the measurement was not reproducible unless the time of agitation was constant (2 min was chosen). One product, sodium caseinate, required longer than a 2-min mixing time. These investigators state that the proposed technique measures water absorbed and retained under specific conditions, which may or may not apply to particular manufacturing applications. They do, however, state that this method with the application of limited... 

Addeo, F., Chobert, J.-M. and Ribadeau-Dumas, B. 1977. Fractionation of whole casein on hydroxyapatite. Application of a study of buffalo kappa-casein. J. Dairy Res. 44, 63-68. 

Morr, C. V., Van Winkle, Q. and Gould, I. A. 1962. Application of polarization of fluorescence technique to protein studies. III. The interaction of x-casein and (3-lacto-globulin. J. Dairy Sci. 45, 823-826. 

The detection of cow s milk in ewe s or goat s milk and cheese is yet another application of the HPLC analysis of peptides. Tobler et al. (125) used HPLC to examine the differences between the caseins in the milks of various species. Goat s- and cow s-milk cheese caseins were hydrolyzed with trypsin, and the peptides thus obtained were separated by reversed-phase HPLC. The chromatograms for the caseins of each species were reproducible and distinct. Subsequently,... 

S Visser, KJ Slangen, HS Rollema. High-performance liquid chromatography of bovine caseins with the application of various stationary phases. Milchwissenschaft 41 559-562, 1986. 

AK Hewavitharana. Method for the extraction of riboflavin for high-performance liquid chromatography and application to casein. Analyst 121 1671-1676, 1996. 

Fluorimetric methods for the determination of amino acids are generally more sensitive than colorimetric methods. Fluorescamine (4-phenyl-spiro[furan-2(3H),l -phthalan]-3,3 -dione) and o-phthaldialdehyde (OPA) substances are used for protein analysis. Fluorescamine reacts with amino groups to form fluorophores that excite at 390 nm and emit at 475 nm (Weigele et al., 1972). Applications of fluorescamine include monitoring the hydrolysis of K-casein (Beeby, 1980 Pearce, 1979) and quantification of proteins, peptides, amino acids in extracts (Creamer et al., 1985). OPA produces fluorescence on reaction with 2-mercaptoethanol and primary amines, with strong absorption at 340 nm. Lemieux et al. (1990) claimed that this method was more accurate, convenient, and simple for estimating free amino acids than the TNBS, ninhydrin, or fluorescamine methods. 

There could be applications that could address specific groups of proteins as those described with the stabilization of white wines (presence of low traces of casein). In these cases, assay kits could comprise also all ingredients for an ELISA test after having treated the sample with CPLL. 

One of the applications of enzymes in the preparation of food gels is the production of cheese. During this process, chymosin hydrolyzes a specific bond of K-casein, resulting in the destabilization of the micelle structure followed by aggregation and formation of an insoluble coagulum. 

The applications of colloid solutions are not restricted to paints and clay. They are also to be found in inks, mineral suspensions, pulp and paper making, pharmaceuticals, cosmetic preparations, photographic films, foams, soaps, micelles, polymer solutions and in many biological systems, for example within the cell. Many food products can be considered colloidal systems. For example, milk is an interesting mixture containing over 100 proteins, mainly large casein and whey proteins [6,7]. 

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