Functional Properties of Protein Fractions Obtained from Pumpkin (Cucurbita Maxima) Seed

Protein fractions were extracted from pumpkin (Cucurbita maxima) seeds with deionized water, salt solution, and alkali solution, and characterized under alkaline (pH 8) and ionic strength conditions for protein solubility, interfacial pressure, and functional properties. The supernatants obtained from the protein fractions after hydration and centrifugation were designed deionized water supernatant, salt solution supernatant, and alkali solution supernatant. All protein fractions showed poor foamability and very low stability. The designed deionized water supernatant presented the highest emulsifying properties. In terms of stability, designed deionized water supernatant emulsions flocculate during storage but with low rates of coalescence compared to the two other fractions.