Rapeseed meal and protein isolates were analyzed for total nitrogen, total phosphorus, low molecular weight phosphorus, phytic acid, RNA, DNA, and phospholipids. The influence of electrolytes on the nitrogen and phosphorus solubility of rapeseed protein isolates was studied at different pH values. The solubility profiles were displaced differently by different salts. The displacements could be explained by ion binding to the proteins and to the other polymers present in the isolates. The higher binding strength anions had for proteins the more effective they were in decreasing the nitrogen solubility of the protein isolate at pH 0.7 and in increasing the nitrogen solubility at pH 5.4, the pH corresponding to the nitrogen solubility minimum in the absence of added salt.
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Lars Gillberg (1978) studied this question.
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