Emulsion stability, effect proteins

Figure 3.4 Effect of polysaccharide on protein-stabilized emulsions. The diameter ratio, j43nuxtlire / J43protem is plotted against the molar ratio R (moles polysaccharide / moles protein). Here J43nuxtlire is average droplet diameter in fresh emulsion prepared with protein + polysaccharide, and d43pTOtQm is average diameter in emulsion stabilized by protein alone. Key , , legumin + dextmn (48 kDa) or legumin + dextran (500 kDa), respectively (0.5 w/v % protein, 10 vol% oil, pH = 8.0, /= 0.1 M) (Dickinson and Semenova, 1992) O, , asi-casein + pectinate and p-casein + pectinate at pH = 7.0, / = 0.01 M (2.0 w/v % protein, 40 vol% oil), respectively , p-casein + pectinate at pH = 5.5, / = 0.01 M (2.0 w/v % protein, 40 vol% oil) (Semenova et al, 1999). Reproduced from Semenova (2007) with permission.

Lethuaut L, Metro F, Genot C (2002) Effect of droplet size on lipid oxidation rates of oil-in-water emulsions stabilized by protein. Journal of the American Oil Chemists Society 79 425-430. 

Effect of Interdroplet Forces on Centrifugal Stability of Protein-Stabilized Concentrated Oil-in-Water Emulsions... 

Industrialization and need for increase in agricultural activity, 1-2 Inosine monophosphate, taste enhancer, 17,19 Interdroplet forces, effect on centrifugal stability for protein-stabilized oil-in-water emulsions,... 

The presence of a thermodynamically incompatible polysaccharide in the aqueous phase can enhance the effective protein emulsifying capacity. The greater surface activity of the protein in the mixed biopolymer system facilitates the creation of smaller emulsion droplets, i.e., an increase in total surface area of the freshly prepared emulsion stabilized by the mixture of thermodynamically incompatible biopolymers (see Figure 3.4) (Dickinson and Semenova, 1992 Semenova el al., 1999a Tsapkina et al., 1992 Makri et al., 2005). It should be noted, however, that some hydrocolloids do cause a reduction in the protein emulsifying capacity by reducing the protein adsorption efficiency as a result of viscosity effects. 

In a recent study by Sun et al. (2007) of 20 vol% oil-in-water emulsions stabilized by 2 wt% whey protein isolate (WPI), the influence of addition of incompatible xanthan gum (XG) was investigated at different concentrations. It was demonstrated that polysaccharide addition had no significant effect on the average droplet size (d32). But emulsion microstructure and creaming behaviour indicated that the degree of flocculation was a sensitive function of XG concentration with no XG present, there was no flocculation, for 0.02-0.15 wt% XG, there was a limited... 

Table 7.2 Effect of the presence of an anionic polysaccharide on the measured zeta potential (Q of emulsion droplets stabilized by proteins under experimental conditions corresponding to protein-polysaccharide complexation. In all cases the complexes were formed in the bulk aqueous medium before emulsification.

Lin et al. (68) investigated the effects of supplementing wieners with sunflower flour and diffusion-extracted protein concentrates. The sunflower products showed good emulsion stability, less shrinkage, and less cooking loss than all-meat controls. 

Emulsification is a stabilizing effect of proteins a lowering of the interfacial tension between immiscible components that allow the formation of a protective layer around oil droplets. The inherent properties of proteins or their molecular conformation, denaturation, aggregation, pH solubility, and susceptibility to divalent cations affect their performance in model and commercial emulsion systems. Emulsion capacity profiles of proteins closely resemble protein solubility curves and thus the factors that influence solubility properties (protein composition and structure, methods and conditions of extraction, processing, and storage) or treatments used to modify protein character also influence emulsifying properties. 

The dye l-Anilino 8-Naphthalene Sulfonic acid (ANS) has high specificity for protein. It fluoresces only when bound to protein [30]. In smears and handsections (i.e. unembedded materials) we have never observed it to effect emulsion stability in the manner more traditional protein dyes such as Coomassie Brilliant Blue or Fast Green often do. This relative pH independence probably is due to the mode of action of this dye. It becomes fluorescent in hydrophobic pockets on protein molecules [30] in contrast to the ionic bonding necessary for Fast Green FCF and Coommassie Blue [22]. We have not observed a strong cross-reaction with lipids, either, although a fluorescence of different spectral characteristics sometimes is seen. 

Stability in plasma is an important requirement for IV emulsions as flocculated droplets may result in lung embolism. It was found that tocol-based emulsions stabilized by sodium deoxycholate/lecithins flocculated strongly when mixed with mouse, rat, and sheep plasma and serum, whereas soya oil-based emulsions with the same emulsifiers did not [123], It was hypothesized that this effect was caused by the adsorption of plasma proteins onto the tocol droplets (opsonization). Indeed, the steric stabilization of emulsions by incorporation of emulsifiers like poloxamer 188 or PEGylated phospholipids such as PEG5000PE proved to be effective in the stabilization of tocol-based emulsions in plasma. Conversely, in vitro studies were... 

Effect of heat processing method on emulsion stability of an acid-precipitated protein fraction from soymilk... 

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