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Caseinates emulsifying properties

But we must appreciate how the phosphate group acts much like the anion from a weak acid (see Chapter 6), so its exact composition will depend on the pH of solution. The pH of cow s or human milk is about 7 (see Table 6.4). If the pH decreases much below about 6 (e.g. by adding an acid in the form of orange juice), the phosphates become protonated. The emulsifying properties of casein cease as soon as its structure changes, causing the milk to separate. [Pg.513]

Since the emulsifying properties depend on the balance between hydro-phobicity and hydrophilicity at the protein surface, a very high yield of phosphorylation may disrupt this balance. The higher improvement of emulsifying properties of K-casein was due to its original high hydro-phobicity, which diminished after phosphorylation. [Pg.8]

Chobert, J.-M., Sitohy, M.Z., and Whitaker, J.R. 1988a. Solubility and emulsifying properties of caseins modified enzymatically by Staphylococcus aureus V8 protease. J. Agric. Food Chem. 36, 220-224. [Pg.62]

Dickinson, E. 1989 Surface and emulsifying properties of caseins. J. Dairy Res. 56, 471-477. Goff, H.D., Liboff, M., Jordan, W.K., Kinsella, J.E. 1987. The effects of polysorbate 80 on the fat emulsion in ice cream mix evidence from transmission electron microscopy studies. Food Microstruct. 6, 193—198. [Pg.362]

Britten, M., Giroux, H.J., and Rodrigue N. (1991). Emulsifying properties of whey protein and casein composite blends. IDF Special Issue 9303,368 374. [Pg.301]

Citrate salts have long been used in the processed cheese industry as "emulsifying salts," and there is still interest in the mechanism of their action. Shirashoji et al. (2006) examined the effects of trisodium citrate on the properties of processed cheese. Increasing concentration of sodium citrate decreased the size droplets of the cheese. This effect is typical when emulsifying properties of a system are improved. This is expected as the complexation of calcium by citrate causes dissociation of the casein micelle, making the casein more available for emulsifying fat droplets. This possibly contributed to the reinforcement of the structure of the processed cheese. [Pg.15]

The dissociation of a quaternary structure or denaturation of proteins is required prior to emulsification. Therefore, casein micelles are adsorbed at an interface in a semi-intact form (Oortwijn et al., 1977). The thermal denaturation of globular proteins prior to emulsification was reported to improve the emulsifying properties. The high level of the thermally denatured whey protein fraction in mixed proteins (of denatured and undenatured proteins) increased the emulsion viscosity and coalescence stability compared with the low-level denatured fraction (Britten et al., 1994). [Pg.270]

Casein Dextran Galactomannan Emulsifying properties Biosci. Biotech. Bio-chem. 56 567-571 (1992)... [Pg.121]

Precipitation with ethanol. The casein in milk coagulates at pH 6.6 on addition of ethanol to about 40% stability decreases sharply as the pH is reduced, and only 10-15% ethanol is required at pH 6. Ethanol-precipitated casein may be dispersed in a micellar form and has very good emulsifying properties. The commercial production of ethanol-precipitated casein is probably economically viable but the process is not being used commercially. [Pg.215]

Water is necessarily a medium of choice for glycation of proteins, although aqueous syrups were successfully employed for syntheses of small D-fructosamines as well. ° Food proteins, most often casein or lactoglobulin, have been purportedly modified by reducing saccharides, in order to improve their solubility, thermal stability, emulsifying properties, or to reduce the allergenicity. The reaction is carried out in the solid phase and with controlled humidity.Optimal conditions for formation of the protein Amadori product from lyophilized protein-carbohydrate mixtures are 55-60 °C, water activity = 0.44-0.65, carbohydrate-protein molar ratio >2. [Pg.303]

P-NMR and C-NMR may be used to study the emulsifier properties at the 0/W interfaee. The analysis of TI relaxation times of selected and P nuclei of P-casein in oil/water emulsions indicates (74) that the conformation and dynamics of the N-terminal part of P-casein are not strongly altered at the oil/water inter face. A large part of the protein was found in a ran dom-coil conformation with restricted motion and a relatively long interal correlation time. [Pg.293]

For example, succinylated wheat gluten is quite soluble at pH 5 (cf. Fig. 1.40). This effect is related to disaggregation of high molecular weight gluten fractions (cf. Fig. 1.41). In the case of succinylated casein it is obvious that the modification shifts the isoelectric point of the protein (and thereby the solubility minimum) to a lower pH (cf. Fig. 1.42). Succinylation of leaf proteins improves the solubility as well as the flavor and emulsifying properties. [Pg.81]

Liu M, Damodaran S. Effect of transglutaminase-catalyzed polymerization of beta-casein on its emulsifying properties. 7 A ric Food Chem. 47 (4) 1514-1519,1999. [Pg.516]

Chem. Descrip. Distilled monoglyceride, polyglycerol ester of fatty acids, caseinate Uses Sponge cake emulsifier Properties Powd. [Pg.397]


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