Thermodynamic incompatibility of proteins and polysaccharides in solutions

doi:10.1016/S0268-005X(97)80022-7

Food Hydrocolloids

Volume 11, Issue 2, April 1997, Pages 145-158

https://doi.org/10.1016/S0268-005X(97)80022-7 Get rights and content

Abstract

The thermodynamic incompatibility of proteins and polysaccharides is of a general nature. This phenomenon is observed under conditions which inhibit complexing between proteins and polysaccharides and promote association between macromolecules of the same type, i.e. provide self-association of biopolymers. Conditions for incompatibility are dependent on the structure and composition of a given biopolymer pair. Incompatibility decreases in the order: carboxyl-containing polysaccharides > neutral polysaccharides > sulphate-containing polysaccharides. Normally, linear polysaccharides are more incompatible with proteins than branched polysaccharides. The difference in hydrophilicity between proteins and polysaccharides, the so-called Δχ-effect, is of great importance for phase equilibria in protein—polysaccharide—water systems and significantly affects this phenomenon. This is reflected in the marked tie slope asymmetry of the phase diagrams of mixed pro tein—polysaccharide solutions.

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On the Thermodynamic Compatibility of Gelatin and Poly-D-glucans in Aqueous Media

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Thermodynamic incompatibility of proteins and polysaccharides in solutions

Abstract

Vestnik Akad. Nauk SSSR

Polymer Bull.

Nahrung

Nahrung

Carbohydr. Polym.

Carbohydr. Polym.

Food Hydrocoll.

Food Hydrocoll.

Stärke

Zentralbl. Bakteriol. Parasitenkd. Infektionskr. 2 Abt.

Untersuch. Strukt.

Zeitschr. Chem. Ind. Kolloide (Kolloid Z.)

Kolloid Z.

Kolloid Z.

Bull. Soc. Chim. Belg.

Biochim. Biophys. Acta

Biochem. J.

Nahrung

Nahrung

J. Agric. Food Chem.

On the Thermodynamic Compatibility of Gelatin and Poly-D-glucans in Aqueous Media