Casein modifications

The six major proteins of milk, asl-, o s2-, and /c-casein, jS-lactoglobulin, and a-lactalbumin, contain at least one tryptophan residue [57], the fluorescence of which allows the monitoring of the structural modifications of proteins and their physicochemical environment during the coagulation processes. Emission fluorescence spectra of the protein tryptophanyl residues were recorded for the milk coagulation kinetics induced by... 

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. 

All of the studies were conducted with weanling, male albino rats of the Sprague-Dawley strain (Holtzman company). The basal diet used for these studies consisted of casein, starch, vegetable oil, vitamin and mineral mixtures, and cellulose. The Wesson Modification of the Osborne-Mendel mineral mixture was used in all studies. This mineral mixture contained no zinc, but it was adequate in the other minerals required by the rat. Most of the non-zinc-supplemented diets used in the various experiments contained approximately 7 ppm zinc. The level of mineral mixture used in the basal diets was 4%, and based on the chemical composition of the mixture, the basal diets contained approximately 0.57% calcium and 0.41% phosphorus ... 

Difficulties in detecting nucleolin on the cell surface could be explained by its very low concentration in this compartment (Hovanessian et al, 2000). Moreover, this cell surface expressed nucleolin protein has a different isoelectric point and it is recognized by only one monoclonal antibody (mAb D3) in its native conformation (Hovanessian et al, 2000). This probably reflects specific post-translational modifications undergone by nucleolin on the cell surface. Consistent with this hypothesis, extracellular nucleolin is a substrate of ecto-protein kinases including casein kinase II (Dumler et al, 1999 Jordan et al., 1994). Interestingly, indirect evidence suggests... 

Tandy, P., Fares, K., Lorient, D., and Voilley, A. Effect of chemical modification of sodium caseinate on diffusivity of aroma compounds in aqueous solutions, / Agric. Food Chem., 45(7) 2649-2653, 1997. 

Avseenko et al. (2001) immobilized antigens onto aluminum-coated Mylar films by electrospray (ES) deposition. Various surface modifications of the metallized films were studied to determine their abilities to enhance sensitivity. The plastic surfaces were firsf cleaned by plasma discharge treatment, followed by coating with proteins (BSA and casein) or polymers such as poly (methyl methacrylate) or oxidized dextran, or they were exposed to dichlorodimethyl silane to create hydrophobic surfaces. Protein antigen was prepared in 10-fold excess sucrose and sprayed onto the surfaces to form arrays with spot diameters between 7 and 15 pm containing 1 to 4 pg protein. 

Soy protein is a low-cost food protein with good nutritional value, but its uses in foods are limited because of inferior functional properties as compared to those of commonly used animal proteins such as casein and albumin (1.2). Therefore, modifications are often required to make soy protein more suitable for food use. Improved functional properties, particularly in the pH range of 3 to 7 where most food systems belong, have been achieved by non-enzymatic methods, including succinylation (3-5), deamidation (6.7), and phosphorylation (8.9). 

Modler, H.W. (1985). Functional properties of nonfat dairy ingredients — a review. Modification of products containing casein. Journal of Dairy Science, 68, 2195-2205. 

It is essential to consider the physico-chemical properties of each WPC and casein product in order to effectively evaluate their emulsification properties. Otherwise, results merely indicate the previous processing conditions rather than the inherent functional properties for these various products. Those processing treatments that promote protein denaturatlon, protein-protein Interaction via disulfide interchange, enzymatic modification and other basic alterations in the physico-chemical properties of the proteins will often result in protein products with unsatisfactory emulsification properties, since they would lack the ability to unfold at the emulsion interface and thus would be unable to function. It is recommended that those factors normally considered for production of protein products to be used in foam formation and foam stabilization be considered also, since both phenomena possess similar physico-chemical and functionality requirements (30,31). 

The properties of many dairy products, in fact their very existence, depend on the properties of milk proteins, although the fat, lactose and especially the salts, exert very significant modifying influences. Casein products are almost exclusively milk protein while the production of most cheese varieties is initiated through the specific modification of proteins by proteolytic enzymes or isoelectric precipitation. The high heat treatments to which many milk products are subjected are possible only because of the exceptionally high heat stability of the principal milk proteins, the caseins. 

Enzymatic coagulation of milk. The enzymatic coagulation of milk involves modification of the casein micelles via limited proteolysis by selected proteinases, called rennets, followed by calcium-induced aggregation of the rennet-altered micelles ... 

The proteins of milk fall into several classes of polypeptide chains. These have been delineated most completely in bovine milk, and a system of nonmenclature has been developed for them (Chapter 3 Eigel et al. 1984). One group, called caseins, consists of four kinds of polypeptides asr, as2-. and 3-, and k- with some genetic variants, post translational modifications, and products of proteolysis. Almost all of the caseins are associated with calcium and phosphate in micelles 20-300 fim in diameter (see Chapter 9). The other milk proteins, called whey proteins, are a diverse group including /3-lactoglobulin, a-lactalbumin, blood serum albumin, and immunoglobulins (Chapter 3). Almost all... 

In this unit, Basic Protocol 1 presents a procedure using casein as substrate. The Alternate Protocol describes the modification of this procedure for use with a denatured hemoglobin substrate. Basic Protocol 2 presents a procedure using a chromaphore-conjugated casein derivative, azocasein. For quantitation, the authors have chosen to use either the BCA-based colorimetric assay unitbli) for soluble protein/peptides (in Basic Protocol 1) or the intrinsic absorbance of the chromaphore-conjugated peptide products (in Basic Protocol 2). 

Such SMP stored at 52 °C developed a brown colour and caramel odour in only 3.5 weeks, no peaks being evident on the e-gram. Even with storage at 37 °C, both /J-lactoglobulin and /J-casein suffered more modification than at lower temperatures, starting at week 2. 

The whey produced during cheese and casein manufacturing contains approximately 20% of all milk proteins. It represents a rich and varied mixture of secreted proteins with wide-ranging chemical, physical and functional properties (Smithers et al., 1996). Due to their beneficial functional properties, whey proteins are used as ingredients in many industrial food products (Cheftel and Lorient, 1982). According to Kinsella and Whitehead (1989), functional properties of foods can be explained by the relation of the intrinsic properties of the proteins (amino acid composition and disposition, flexibility, net charge, molecular size, conformation, hydrophobicity, etc.), and various extrinsic factors (method of preparation and storage, temperature, pH, modification process, etc.). 

Proteolytic modification has special importance for the improvement of solubility of proteins. This effect becomes significant even after very limited proteolysis. Hydrolysis of casein to DH of 2 and 6.7% with Staphylococcus aureus V8 protease increased the isoelectric solubility to 25 and 50%, respectively (Chobert et al., 1988a). However, it should be noted that the solubility profiles were not identical, due to a shift of the isoelectric point of the modified proteins. Solubility of a protein hydrolysate depends on the enzyme used (Adler-Nissen, 1986a). Protamex (a Bacillus proteinase complex) hydrolysates of sodium caseinate (DH 9 and 15%) displayed 85-90% solubility between pH 4 and 5 (Slattery and FitzGerald, 1998). 

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