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Pumpkin (Cucurbita maxima) seed proteins: sequential extraction processing and fraction characterization
Leila Rezig1, Farhat Chibani, Moncef Chouaibi
1Food Conservation and Valorization Laboratory, High Institute of Food Industries , 58 Avenue Alain Savary, El Khadra City, Tunis 1003, Tunisia.
Journal of Agricultural and Food Chemistry
|July 23, 2013
Summary
Tunisian pumpkin seed proteins exhibit pH-dependent solubility, influenced by defatting solvents. These protein extracts, rich in essential amino acids, offer unique properties for food applications.
Area of Science:
- Food Science
- Protein Chemistry
- Nutritional Science
Background:
- Pumpkin seed proteins (Cucurbita maxima) are a potential food ingredient.
- Understanding their extraction and properties is crucial for utilization.
Purpose of the Study:
- To investigate the solubility and extraction of Tunisian pumpkin seed proteins.
- To determine the amino acid profile and denaturation temperatures of protein fractions.
Main Methods:
- Proteins were sequentially extracted using the Osborne procedure.
- Solubility was analyzed based on pH, ionic strength, and defatting solvent (pentane vs. chloroform/methanol).
- Amino acid composition and denaturation temperatures (via differential scanning calorimetry) were determined.
Main Results:
- Protein solubility was highest in alkaline pH regions and varied with defatting solvent.
- Alkali extract was the major protein fraction, especially when using pentane for defatting.
- Most essential amino acids met FAO/WHO/UNU requirements, except threonine and lysine.
- Denaturation temperatures were high (96.6 °C for salt extract, 93.4 °C for alkali extract).
Conclusions:
- Tunisian pumpkin seed proteins can be effectively extracted and fractionated.
- Defatting solvent significantly impacts protein yield and solubility.
- The protein extracts possess favorable amino acid profiles and high thermal stability.
- These characteristics suggest potential for use as novel food ingredients.
