Abstract
Rapeseed meal was extracted in water, in 5% NaCI, or in 5% CaCl2 at pH values ranging from 2.5 to 11.0. The extracted proteins were subjected to dissociating conditions and examined for molecular weight distribution by SDS gel electrophoresis and for isoelectric point patterns by gel electrofocusing.The pH solubility profiles demonstrated the relatively high solubility of rapeseed protein over the acidic pH range and consequently, the difficulty of protein isolate production by traditional oilseed technology. Electrofocusing resolved over 30 protein species which SDS electrophoresis showed to be mainly distributed among only 3 molecular weight groupings.
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