Electrostatic interactions protein-polysaccharide

Dickinson, E. (1998). Stability and rheological implications of electrostatic milk protein-polysaccharide interactions. Trends in Food Science and Technology, 9, 347-354. 

It is well known the tendency of polysaccharides to associate in aqueous solution. These molecular associations can deeply affect their function in a particular application due to their influence on molecular weight, shape and size, which determines how molecules interact with other molecules and water. There are several factors such as hydrogen bonding, hydrophobic association, an association mediated by ions, electrostatic interactions, which depend on the concentration and the presence of protein components that affect the ability to form supramolecular complexes. 

The electrostatic interaction between oppositely charged protein and polysaccharide can be utilized for encapsulation and delivery of hydro-phobic nutraceuticals. As a result of this interaction, we may have either complex coacervation (and precipitation) or soluble complex formation, depending on various factors, such as the type of polysaccharide used (anionic/cationic), the solution pH, the ionic strength, and the ratio of polysaccharide to protein (see sections 2.1, 2.2 and 2.5 in chapter seven for more details) (Schmitt et al, 1998 de Kruif et al., 2004 Livney, 2008 McClements et al, 2008, 2009). The phenomenon of complex... 

It seems that there is probably greater availability of positively charged residues on the adsorbed protein for electrostatic interaction with sulfate groups of the anionic polysaccharide. This could lead to a greater extent of neutralization of dextran sulfate as a result of complex formation, and consequently to a lower thermodynamic affinity of the complexes for the aqueous medium and a lower value of the ( -potential for emulsion droplets in bilayer emulsions. 

Ganzevles, R.A., van Vliet, T., Cohen Stuart, M.A., de Jongh, H.H.J. (2007). Manipulation of adsorption behaviour at liquid interfaces by changing protein-polysaccharide electrostatic interactions. In Dickinson, E., Leser, M.E. (Eds). Food Colloids Self-Assembly and Material Science, Cambridge, UK Royal Society of Chemistry, pp. 195-208. 

Ye, A. (2008). Complexation between milk proteins and polysaccharides via electrostatic interaction principles and applications - a review. International Journal of Food Science and Technology, 43, 406 115. 

In the pH range close to the protein s lEP an interesting phenomenon of non-uniform redistribution of protein molecules among polysaccharide chains occurs (Tolstoguzov et al. 1985). The reason is that in the vicinity of the protein lEP the hydrophobic protein-protein and electrostatic protein-polysaccharide interactions can be energetically comparable with each other. Protein-protein association on the anionic polysaccharide matrix (or self-association of proteins), which is mainly due to hydrophobic interactions, is usually enhanced when the pH approaches the protein lEP. Accordingly, under conditions of a relatively weak protein-polysaccharide interaction, each free site situated near the site on the polysaccharide chain already occupied by a protein molecule becomes thermodynamically preferable for further binding of protein molecules. This leads to cooperative protein adsorption on an anionic polysaccharide. Some parts of polysaccharide chains tend to be completely covered by protein molecules (as in a virus) while other parts are completely free of protein. 

At the second critical pH (pH,, ), which is usually below the protein isoelectric point, strong electrostatic interaction between positively charged protein molecules and anionic polysaccharide chains will cause soluble protein/polysaccharide complexes to aggregate into insoluble protein/polysaccharide complexes. For negatively charged weak acid-based (e.g., carboxylic acid) polysaccharides like pectin, with the decrease of pH below the pKa of the polysaccharide, protein (e.g., bovine serum albumin (BSA))/polysaccharide (e.g., pectin) insoluble complexes may dissociate into soluble complexes, or even non-interacted protein molecules and polysaccharide chains, due to the low charges of polysaccharide chains as well as the repulsion between the positively charged proteins (Dickinson 1998). 

Type V includes chiral stationary phases based on immobilized proteins as well as polysaccharide phases such as cellulose and amylose carbamate. They are used in conjunction with aqueous buffered mobile phases. The interaction between the stationary phase and the analytes is based on hydrophobic interaction as well as electrostatic interaction in the case of proteins. The retention of the analytes can be controlled by the addition of organic modifiers such methanol, ethanol, and 2-propanol. 

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