Solubilization, electorphoretic characterization and in vitro digestibility of almond (Prunus amygdalus) proteins

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Sathe, S.K., 1992. Solubilization, electorphoretic characterization and in vitro digestibility of almond (Prunus amygdalus) proteins. J Food Biochem. 16:249-64.

The major U.S. marketing varieties of almonds contained moisture, protein, fat, and ash in the range 4.35-5.86%, 16.42-22.17%, 53.59-56.05%, and 2.69-2.93%, respectively. Two fatty acids, oleic (range 52.44-67.07%) and linoleic (range 22.05-38.67%) accounted for up to 90% of the total fat. The majority of almond proteins (≥ 95%) are water soluble with a minimum solubility at pH ≤ 4.0. Sodium chloride (1.0 M) decreased the almond protein solubility in aqueous medium. Electrophoretic analyses indicated that one water soluble protein dominates the almond protein composition. This oligomeric major protein is made up of two kinds of polypeptides (molecular weight range 20,000-22,000 and 38,000-41,000) linked via disulfide bonds. Among the proteases tested, pepsin was the most efficient in hydrolyzing the almond proteins.