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Thermodynamic incompatibility of proteins

by: V. I. Polyakov, Grinberg, V. B. Tolstoguzov
Food Hydrocolloids, Vol. 11, No. 2. (April 1997), pp. 171-180, doi:10.1016/s0268-005x(97)80024-0  Key: citeulike:11903090

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Abstract

Unlike mixtures of synthetic polymers, mixtures of polysaccharides and protein—polysaccharide mixtures, the thermodynamic incompatibility of proteins in solution is notable for the following general features. This phenomenon is typical of mixtures of proteins belonging to different classes according to the Osborne classification. A relatively high phase separation threshold is the other characteristic feature of mixed protein solutions. Factors such as pH, ionic strength and temperature only slightly affect protein incompatibility. This is probably due to the compactness and rigidity of protein molecules. Accordingly, incompatibility is strongly dependent upon the conformational state of the proteins and is enhanced by protein denaturation.


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