Background: Recent advances in analytical approaches presented new potentials for plant-based drug manufacture within the realms of peptides and proteins. 
 
Methods: Enzymatic hydrolysis of plant-derived parent proteins yields bioactive peptides, which have been investigated for potential applications across diverse experimental contexts. Differences in pH and ionic strength induced significant effects on the solubility of extracted pumpkin seed proteins, as a direct relationship was observed between the solubility of pumpkin proteins and alkaline pH. 
 
Result: Applying the kind of solvent for seed defatting significantly influences protein solubility. Specifically, applying the chloroform-methanol (CM) mixture approach for lipid extraction, as opposed to pentane (P), clearly weakened protein solubility. The objective of the current study is to explore how varied environmental parameters, namely pH and ionic strength, can influence the functional properties of pumpkin seed protein isolate (PSPI), including solubility, interfacial properties and emulsifying activity, compared to pumpkin seed protein hydrolysate (PSPH). 
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Preparing Protein Hydrolysates from Pumpkin Seeds and Studying Their Chemical and Antioxidant Properties