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A simple method of dehulling and demucilaging of linseed was developed. Solubility of the proteins the linseed meal in water, 0.5 and 1.0 M NaC1, and 2% sodium hexametaphosphate solutions was in the pH range 2-12. The solubility was minimum around pH 3-6 and maximum around 8.0. The solubility minimum shifted to pH 0.5-4.5 in 1 M NaCl and to 0.6-5.3 in 2% sodium . The total proteins were characterized by techniques of gel filtration, ion-exchange , electrophoresis, and ultracentrifugation. The presence of at least three components observed. The meal extracts showed proteolytic and trypsin inhibitor activities but no hemagglutinating . Amylase and amylase inhibitor activities were not detected.
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Madhusudhan et al. (1983) studied this question.
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