Polysaccharide, protein-, complexes

The other major component of an articular joint is synovial fluid, named by Paracelsus after synovia (egg-white). It is essentially a dialysate of blood plasma with added hyaluronic acid. Synovial fluid contains complex proteins, polysaccharides, and other compounds. Its chief constituent is water (approximately 85%). Synovial fluid functions as a joint lubricant, nutrient for cartilage, and carrier for waste products. 

Proteins, the main constituents of the animals body, are polypeptides, biopolymers consisting of many amino acid molecules (the monomers) combined together (see Chapter 11) collagen, for example, the main component of animal skin, is a complex protein consisting of many molecules of amino acids combined together into polypeptide chains (see Fig. 71). Polysaccharides, the essential constituents of plants, also consist of many monosaccharide molecules combined together. Cellulose, the most abundant biological material on earth, which makes up most of the structural... 

Chemical analyses of capsular material from a number of bacteria show wide differences in composition. For this reason it is impossible to make statements which apply to all bacteria. In some organisms the capsular material appears to be a glycoprotein in others, a protein-polysaccharide complex in still others, a polysaccharide framework with the spaces filled in by a larger amount of glutamyl polypeptide. 

Attachment There is a high specificity in the interaction between virus and host. The most common basis for host specificity involves the attachment process. The virus particle itself has one or more proteins on the outside which interact with specific cell surface components called receptors. The receptors on the cell surface are normal surface components of the host, such as proteins, polysaccharides, or lipoprotein-polysaccharide complexes, to which the virus particle attaches. In the absence of the receptor site, the virus cannot adsorb, and hence cannot infect. If the receptor site is altered, the host may become resistant to virus infection. However, mutants of the virus can also arise which are able to adsorb to resistant hosts. 

Finally, the versatility of the technique and its use as a chemical imaging technique allow retrieval of the structural composition of a sample, in order to understand its complete recipe [Mazel et al. 2008]. The composition of a sample from the Dogon statuette 71.1935.105.169 has been studied. Proteins, polysaccharides, lipids and minerals have been found. The distribution of these different chemicals shows that the patina sample can be divided into four different layers (Figure 15.14). Layers 1 and 3 are mainly composed of proteins whereas layer 2 consists of lipids and polysaccharides. Minerals can be found at the interface of layers 1 and 2, and 2 and 3. Finally, layer 4 is the more complex because it contains all the types of compounds. One can suppose that it is in fact composed of different layers that do not appear clearly on the cross-section. 

Macromolecules such as proteins, polysaccharides, nucleic acids differ only in their physicochemical properties within the individual groups and their isolation on the basis of these differences is therefore difficult and time consuming. Considerable decreases may occur during their isolation procedure due to denaturation, cleavage, enz3rmatic hydrolysis, etc. The ability to bind other molecules reversibly is one of the most important properties of these molecules. The formation of specific and reversible complexes of biological macromolecules can serve as basis of their separation, purification and analysis by the affinity chromatography [6]. 

The finding that, when the protein-polysaccharide complex (mainly chondroitin 4-sulfate) from pig rib-cartilage was treated with 0.2 M potassium hydroxide for 20 hours at 4°, only about 80% of the carbohydrate moieties were removed by /3-elimination, was interpreted as... 

It is well known that a great variety of biomolecules exist where metals and metalloids are bound to proteins and peptides, coordinated by nucleic acids or complexed by polysaccharides and small organic ligands such as organic acids.55 Most proteins contain amino acids with covalently bonded heteroelements such as sulphur, selenium, phosphorus or iodine.51 Several reviews have been published on the development of mass spectrometric techniques for bioanalysis in metal-lomics , which integrate work on metalloproteins, metalloenzymes and other metal containing biomolecules.1 51 53 54 56-59 The authors consider trace metals, metalloids, P and S (so-called... 

B) complexes of polysaccharides or disordered proteins with amphiphilic compounds inclusion... 

B) protein-polysaccharide complex with amphiphilic compounds... 

Turgeon, S.L., Schmitt, C., Sanchez, C. (2007). Protein-polysaccharide complexes and coacervates. Current Opinion in Colloid and Interface Science, 12, 166-178. 

Schmitt, C., Sanchez, C., Sobry-Banon, S., Hardy, J. (1998). Structure and technofunctional properties of protein-polysaccharide complexes. Critical Reviews in Food Science and Nutrition, 38, 689-753. 

Dickinson, E., Galazka, V.B. (1992). Emulsion stabilization by protein-polysaccharide complexes. In Phillips, G.O., Wedlock, D.J., Williams, P.A. (Eds). Gums and Stabilisers for the Food Industry 6, Oxford IRL Press, pp. 351-362. 

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. 

At the mixing ratio where coacervation is maximized, the protein-polysaccharide complexes are electrically neutral. 

The expected greater size of protein-polysaccharide complexes can reduce the diffusion rate of the adsorbing species towards the interface. This effect is especially important for small monomeric proteins. In addition, Ganzevles and co-workers (2006) have suggested that the diffusion of protein in the complexes may not solely be responsible for the slow surface tension decay. Rather, the gradual dissociation (and subsequent adsorption) of protein from complexes, when they are in close proximity to the interface, could also contribute to the behaviour. 

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.

Surface shear rheology at the oil-water interface is a sensitive probe of protein-polysaccharide interactions. In particular, there is considerable experimental evidence for a general increase in surface shear viscosity of protein adsorbed layers as a result of interfacial complexation with polysaccharides (Dickinson et al., 1998 Dickinson and Euston, 1991 Dickinson and Galazka, 1992 Semenova et al., 1999a Jourdain et al., 2009). One such example is the case of asi-casein + pectin at pH = 5.5 and ionic strength = 0.01 M (Ay = - 334 x 10 cm /mol) the interfacial viscosity after 24 hours was found to be five times larger in the presence of pectin (i.e., values of 820 80 and 160 20 mN m 1 with and without pectin, respectively) (Semenova et al., 1999a). 

Therefore, two contributory factors may provide an explanation for more effective electrostatic / steric stabilization of the so-called mixed emulsions in comparison with the sequentially assembled biopolymer interfaces of the bilayer emulsions firstly, a greater hydrophilicity of the adsorbed protein-polysaccharide complexes, caused by the larger net negative charge, and, secondly, a more bulky architecture of the normal complexes as compared to the interface complexes. 

In general, surface activity behaviour in food colloids is dominated by the proteins and the low-molecular-weight surfactants. The competition between proteins and surfactants determines the composition and properties of adsorbed layers at oil-water and air-water interfaces. In the case of mixtures of proteins with non-surface-active polysaccharides, the resulting surface-activity is usually attributed to the adsorption of protein-polysaccharide complexes. By understanding relationships between the protein-protein, protein-surfactant and protein-polysaccharide interactions and the properties of the resulting adsorbed layers, we can aim to... 

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