On the Relation Between the Character of Polyphosphates and the Precipitation Reaction of Protein Solution

On the Effect of Polyphosphate for Proteins (Part 1)

Abstract

We have investigatated the precipitation reaction of albumin, casein, gelatin and sericin solution in the presence of sodium polyphospate. The relation between the character of polyphosphates and the precipitation of protein aqueous solution were studied. When ultra-, or hexametaphosphate were added to albumin or gelatin at pH 3 to 7, the degree of turbidity and gel weight remarkably increased, and the peaks of turbidity appeared at acidic side. In case of casein or sericin solution the degree of turidity and gel weight were less than the case without polyphosphate at lower pH. Pyro-acid pyro-, and tripolyphosphate did not influence on the precipitation reaction for all proteins at various conditions. It was suggested that the precipitation reaction of protein aqueous solution were influenced by chelation value, part of high polymer and ring structure of polyphosphates. The correlation was observed between the average chain length in the meta or ultra region of polyphosphates and the degree of turbidity of each protein aqueous solution. However, the smaller chain length of polyphosphates had no relation to them.