Abstract
Lagenaria siceraria is an underutilized legume that if exploited can serve as an alternative food protein source. The globulin storage protein of Lagenaria siceraria was fractionated into the legumin (11S) fraction. The globulin and legumin were characterized for their structural conformation and physicochemical properties. Arginine (14.56 g/100 g protein) and glutamic acid (11.56 g/100 g protein) were the most abundant amino acids in the proteins. Legumin showed a more folded structure compared to the globulin. Gel electrophoresis identify five major bands at 40, 90, 110, 170 and 240 kDa in the legumin fraction. The β-sheet secondary structure is the dominant structure in both proteins. Globulin displayed higher protein solubility profile than the legumin. Globulin and legumin extracted from Lagenaria siceraria have potential application as functional and nutritional ingredients in the food system.
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