Extraction and purification of proteins from Prunus armeniaca seeds

Abstract

Prunus armeniaca (apricot) is a nutrient-dense plant widely cultivated for its edible fruit and valuable seed components. In addition to supplying essential vitamins, minerals, and antioxidants, apricot seeds are a rich yet underexplored source of plant proteins with potential applications in food, cosmetics, and pharmaceutical industries. This study aimed to extract, purify, and characterize proteins from P. armeniaca seeds, evaluate their biological activity, and compare protein content between seeds collected from warm and cold climatic regions. Seed proteins were extracted using four different buffer systems, and purification was achieved by ammonium sulfate precipitation. The degree of purity was assessed using SDS-PAGE, while protein concentration was quantified spectrophotometrically. Functional properties were examined through antibacterial assays and methylene blue adsorption tests. Higher protein concentration was observed in the seeds of high-temperature regions compared to lower-temperature seeds. For high-temperature seed, the highest protein concentration (13.1 mg/µl) was achieved in Tris-HCl buffer, while distilled water gave the highest concentration (9.098 mg/ µl) in lower temperature seed. Optimal protein recovery was obtained at 65 % and 70 % ammonium sulfate saturation. However, the purified proteins showed no significant antibacterial activity and failed to remove methylene blue, suggesting limited antimicrobial and adsorptive potential. Comparative assessment revealed higher protein content in seeds from warmer regions, indicating temperature-related variation in protein synthesis. This work highlights P. armeniaca seeds as an important yet underutilized source of plant proteins. Environmental factors strongly influence protein yield, and further structural and functional studies are warranted to explore potential biotechnological and therapeutic applications.