Polysaccharides incompatibility

In addition to their role in primary stabilization related to viscosity increase, some hydrocolloids (particularly carrageenan) are traditionally used as secondary stabilizers. Many of the primary stabilizing hydrocolloids, including locust bean gum and carboxy methyl cellulose induce precipitation of the milk proteins in the mix. This phenomenon in ice cream mix is known as wheying-off, and may be due to direct protein-polysaccharide binding and/or protein-polysaccharide incompatibility in the water phase40. The latter phenomenon may be due to decreased solvent quality due to the competition between protein and polysaccharide for solubilisation. 

The agglutination of incompatible red blood cells, which indicates that the body s immune system has recognized the presence of foreign cells in the body and has formed antibodies against them, results from the presence of polysaccharide markers on the surface of the cells. Types A, B, and O red blood cells... 

The main hurdle for the use of starch as a reinforcing phase is its hydrophillicity leading to incompatibility with polymer matrix and poor dispersion causing phase separation. Two strategies have been adopted to improve the performance of polysaccharides. 

Dickinson, E., Semenova, M.G. (1992). Emulsifying behaviour of protein in the presence of polysaccharide under conditions of thermodynamic incompatibility. Journal of the Chemical Society, Faraday Transactions, 88, 849-854. 

Grinberg, V.Y., Tolstoguzov, V.B. (1997). Thermodynamic incompatibility of proteins and polysaccharides in solutions. Food Hydrocolloids, 11, 145-158. 

Nowadays it is well established that the interactions between different macromolecular ingredients (i.e., protein + protein, polysaccharide + polysaccharide, and protein + polysaccharide) are of great importance in determining the texture and shelf-life of multicomponent food colloids. These interactions affect the structure-forming properties of biopolymers in the bulk and at interfaces thermodynamic activity, self-assembly, sin-face loading, thermodynamic compatibility/incompatibility, phase separation, complexation and rheological behaviour. Therefore, one may infer that a knowledge of the key physico-chemical features of such biopolymer-biopolymer interactions, and their impact on stability properties of food colloids, is essential in order to be able to understand and predict the functional properties of mixed biopolymers in product formulations. 

Table 7.1 shows that rather similar results were also found by Makri et al. (2005) for samples of coarse emulsions containing thermodynamically incompatible mixtures of legume seed protein + xanthan gum. The protein surface load was found to be enhanced in the presence of xanthan gum, especially at elevated ionic strengths. That is, there was observed to be an increase in the adsorption of legume seed proteins at the surface of the emulsion droplets which could be attributed to an increase in the thermodynamic activity of the proteins in the system in the presence of the incompatible polysaccharide (see Table 7.1). Associated with the greater extent of protein adsorption, the authors reported an enhancement in the emulsion stability.

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... 

It is to be anticipated that thermodynamic incompatibility between a protein and a polysaccharide in an adsorbed film around the oil droplets or air bubbles in an emulsion or foam would have an influence on the... 

Of importance to the microstructure and viscoelastic properties of starch gels is the identified thermodynamic incompatibility of starch polysaccharides.417 Amylose... 

Conformational changes are easily followed by optical rotation (Hui and Neukom, 1964). Circular dichroism spectroscopy (CD) of polysaccharides (Morris, 1994) exploits optical anisotropy. In a CD instrumental design, the clockwise and counterclockwise rotation of two polarized beams of equal intensity, traversing a 180° path through a chiroptical medium, display a molar ellipticity maximum and minimum. CD is the differential measurement as a function of X. By CD spectroscopy, mixed interchain association rather than nonspecific incompatibility or exclusion was identified as the molecular basis of alginate-polyguluronate interaction (Thom et al., 1982). 

On mixing solutions of a protein and a polysaccharide, four kinds of mixed solutions can be obtained. Figure 3.1 shows that two single-phase systems (1 and 3) and two-types of biphase systems (2 and 4) can be produced. The two-phase liquid systems 2 and 4 differ in the distribution of biopolymers between the co-existing phases. The biopolymers are concentrated either in the concentrated phase of system 2 because of interbiopolymer complexing, or within separated phases of system 4 because of incompatibility of the biopolymers. The term biopolymer compatibility implies miscibility of different biopolymers on a molecular level. The terms incompatibility or limited thermodynamic compatibility cover both limited miscibility or limited cosolubility of biopolymers (i.e., system 2) and demixing or phase separation... 

Biopolymer incompatibility is a general phenomenon typical of aU polymers. Biopolymer incompatibility occurs even when their monomers would be miscible in all proportions. For instance, sucrose, glucose and other sugars are normally cosoluble in the common solvent, water, while different polysaccharides usually are not miscible. The transition from a mixed solution of monomers to polymers corresponds to the transition from good to limited miscibility. Normally, a slight difference in composition and/or structure is sufficient for incompatibility of macromolecules in common solvent (Tolstoguzov 1991, 2002). Compatibility or miscibility of unlike biopolymers in aqueous solutions has only been exhibited by a few biopolymer pairs (Tolstoguzov 1991). 

For instance, denaturation and partial hydrolysis of proteins oppositely influence their incompatibility with other biopolymers (Tolstoguzov 1991). Most biopolymers are polyelectrolytes. Factors such as pH and salt concentration affect their interactions with one another, with the solvent and their compatibility. For instance, when the pH is shifted to their isoelectric point (lEP), the thermodynamic incompatibility of proteins is usually enhanced by self-association of the protein molecules. Generally, protein-neutral polysaccharide mixtures separate into two phases when the salt concentration exceeds 0.15 M. 

Proteins and carboxyl-containing polysaccharides have a limited compatibility when either the pH exceeds the protein s lEP (at any ionic strength) or the pH is equal to or less than the protein s lEP and the ionic strength exceeds 0.2 M. With sulphated polysaccharides, globular proteins are usually incompatible at ionic strengths above... 

Biopolymer incompatibility seems to provide phase-separated liquid and gel-like aqueous systems. In highly volume-occupied food systems aggregation, crystallisation and gelation of biopolymers and their adsorption at oil/water interfaces favour an increase in the free volume, which is accessible for other macromolecules. Denatura-tion of proteins during food processing decreases their solubility and co-solubility of proteins with one another and with polysaccharides and induces phase separation of the system. 

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