Casein, micelles

A useful property of the red seaweed extracts is their abiUty to form gels with water and milk. Kappa-carrageenan reacts with milk protein micelles, particularly kappa-casein micelles. The thickening effect of kappa-carrageenan in milk is 5—10 times greater than it is in water at a concentration of 0.025% in milk, a weak thixotropic gel is formed. [Pg.488]

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. [Pg.855]

Roach, A. and Harte, F. (2008). Disruption and sedimentation of casein micelles and casein micelle isolates under high-pressure homogenization. Innovative Food Sci. Emerg. Technol. 9,1-8. [Pg.86]

Caseins are the major proteins in bovine milk and about 95% of the caseins exist as casein micelles. The structure and properties of casein micelles influence a wide range of technological uses of milk. Light microscopy, SEM, and TEM have been frequently used to study casein... [Pg.217]

FIGURE 6.10 Three characteristic structures of pressure-treated casein micelles representative AFM images together with the associated size-histograms are shown. The solid lines are fit to Gauss distributions. (A) Intact micelles, P < SO MPa (B) compact reconstituted micelles, 120 MPa < P < 240 MPa (C) mini-micelles, P > 280 MPa. Reprinted with permission from Gebhardt et al. (2006). [Pg.219]

FIGURE 6.11 Young moduli (E) of casein micelles with different diameters at two temperatures (A) 20 °C and (B) 23 °C. The data in (A) were extracted at different pH 5.4 (squares), 5.2 (up triangles), and 5.0 (circles). For (B), besides the data from the same pH range (open diamonds), a few points ( ) from pH 5.6 are included. The solid line is the best fit for the linear variation at 20 °C. Reprinted with permission from Uricanu et at. (2004). [Pg.221]

Dalgleish, D. G., Spagnuolo, P. A., and Douglas Goff, H. (2004). A possible structure of the casein micelle based on high-resolution field emission scanning electron microscopy. Int. Dairy. 14,1025-1031. [Pg.238]

Farrell, H. M., Jr., Malin, E. L., Brown, E. M., and Qi, P. X. (2006). Casein micelle structure What can be learned from milk synthesis and structural biology Curr. Opin. Colloid Interface Sci. 11,135-147. [Pg.238]

Gebhardt, R., Doster, W., Friedrich, J., and Kulozik, U. (2006). Size distribution of pressure-decomposed casein micelles studied by dynamic light scattering and AFM. Eur. Biophys.. Biophys. Lett. 35,503-509. [Pg.239]

Horne, D. S. (2009). Casein micelles structure and stability. In "Milk Proteins From Expression to Food", (A. Thompson, M. Boland, and H. Singh, Eds), pp. 133-179. Academic Press, San Diego. [Pg.239]

McMahon, D. J. and McManus, W. R. (1998). Rethinking casein micelle structure using electron microscopy. /. Dairy Sci. 81,2985-2993. [Pg.239]

Spagnuolo, P. A., Dalgleish, D. G., Goff, H. D., and Morris, E. R. (2005). Kappa-carrageenan interactions in systems containing casein micelles and polysaccharide stabilizers. Food Hydrocolloids 19,371-377. [Pg.240]

The elastic modulus (G ) of MP, BCAS, and BLG5 rapidly rose to plateaus that corresponded to different G saturations (Gjat) (Table 2). MP and BCAS coagula showed the more important Gsat value (142 N/m ), meaning that the emulsions stabilized by skim milk proteins (mainly casein micelles) and 6-casein formed the coagula with the strongest protein network. [Pg.279]

Similarly, the protein in milk is very rich in colloidal chemistry. Most of the protein is bound within aggregates called casein micelles (see p. 512). The colloids in milk are essentially stable even at elevated temperatures, so a cup of milky tea, for... [Pg.509]

The most abundant milk protein is casein, of which there are several different kinds, usually designated a-, (1-, and K-casein. The different caseins relate to small differences in their amino acid sequences. Casein micelles in milk have diameters less than 300 nm. Disruption of the casein micelles occurs during the preparation of cheese. Lactic acid increases the acidity of the milk until the micelles crosslink and a curd develops. The liquid portion, known as whey, containing water, lactose and some protein, is removed. Addition of the enzyme rennet (chymosin) speeds up the process by hydrolysing a specific peptide bond in K-casein. This opens up the casein and encourages further cross-linking. [Pg.391]

The Daily Industiy. The first step in cheese manufacture is the coagulation of milk. Coagulation can be divided into two distinct phases, enzymatic and the non-enzymatic. In the primary enzymatic phase a proteol ic enzyme such as chymosin (rennet), or less effectively, pepsin, carries out an extremely specific and limited proteolysis, cleaving a phenylalanine-methionine bond of /c-casein, making the casein micelle metastabie. In the second, non-enzymatic phase, the... [Pg.68]

A colloid suspension of casein micelles, globular proteins, and lipoprotein particles... [Pg.202]

Colloidal calcium phosphate (CCP) acts as a cement between the hundreds or even thousands of submicelles that form the casein micelle. Binding may be covalent or electrostatic. The casein micelles are not static there are three dynamic equilibria between the micelle and its surroundings ... [Pg.206]

The following factors must be considered when assessing the stability of the casein micelle The role of Ca++ is very significant in milk. More than 90% of the calcium content of skim milk is associated in some way or another with the casein micelle. The removal of Ca++ leads to reversible dissociation of P-casein without micellular disintegration. The addition of Ca++ leads to aggregation. The same reaction occurs between the individual caseins in the micelle, but not as much because there is no secondary structure in casein proteins. [Pg.206]

Van der Waals forces There has been some success in relating these forces to micellar stability. However, the steric stabilization has been found to be also of some importance. Especially, the hairy layer interferes with the interparticle approach. There are several factors that will affect the stability of the casein micelle system ... [Pg.207]

Caseins are able to aggregate if the surface of the micelle is reactive. Although the casein micelle is fairly stable, there are four major ways in which aggregation can be induced ... [Pg.207]

The viscosity of milk and milk products is reported to be important in the rate of creaming. The viscosity of milk increases with decrease in temperature because the increased voluminosity of casein micelles temperatures above 65°C increases viscosity due to the denaturation of whey proteins pH an increase or decrease in the pH of milk also causes an increase in casein micelle voluminosity. Fat globules that have undergone cold agglutination may be dispersed due to agitation, causing a decrease in viscosity. [Pg.209]

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