Propriétés Physico-Chimiques et Composition en Acides Aminés des Fractions de Protéines de Soya, de Féverole, de Colza et de Feuilles de Luzeme

Abstract

Fractions were prepared and purified from proteins of four different vegetable sources by a method based on differences of solubility in ammonium sulfate solutions. Sedimentation coefficient SW25, distribution of amino-acid residues, absorption coefficient at 280 and 260 nm and solubility in ammonium sulfate solutions of various concentrations have been determined with the isolated fractions. Results indicated that solubility decreased logarithmically with increases in concentration of ammonium sulfate. It is shown for the five fractions studied that solubility is related to the ratio of the number of polar/neutral residues.