Extraction, fractionation and characterization of bitter melon seed proteins

Area of Science:

• Food Science
• Biochemistry
• Plant-based Proteins

Background:

• Bitter melon (Momordica charantia) seeds are a potential source of underutilized plant proteins.
• Understanding the physicochemical properties of bitter melon seed proteins is crucial for their application in food systems.

Purpose of the Study:

• To sequentially extract and characterize protein fractions from defatted bitter melon seeds.
• To evaluate the biochemical and thermal properties of these protein fractions.

Main Methods:

• Sequential extraction of protein fractions (albumin, globulin, glutelin, prolamin) using specific solvents.
• Analysis of protein yield, surface hydrophobicity, molecular size, and denaturation temperature.
• Amino acid profiling of the extracted protein fractions.

Main Results:

• Albumin was the predominant fraction (49.3%), followed by globulin (29.3%). Prolamin was undetectable, with 18.3% non-extractable protein.
• Significant differences in surface hydrophobicity and denaturation temperatures were observed among albumin, globulin, and glutelin.
• All essential amino acids met nutritional requirements for preschool children, except for threonine.

Conclusions:

• Bitter melon seed protein fractions possess distinct physicochemical properties and high thermal stability.
• These protein fractions demonstrate potential as functional food ingredients for developing novel food products.