The character of phase transformations and composition of the phases obtained during interaction of proteins precipitating in the vicinity of the isoelectric point with dextransulfate was investigated with the aid of nephelometric measurements and chemical analysis. Clearly expressed hysteresis of the acid‐base nephelometric titration which is not observed in the presence of 7‐M of urea was revealed. Composition of the phases obtained is determined by the system prehistory. The soluble protein‐dextransulfate complexes are highly stable to precipitation and destruction under action of the low molecular salts.
It is common knowledge that most of vegetable proteins are precipitated in the vicinity of the isoelectric point. This circumstance hampers their being processed into food. The present work shows that interaction of some proteins with sulfonated dextran improves the solubility of those proteins in a wide range of pH values.
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