Evaluating the effects of protein-glutaminase treatment on the structural and functional properties of pumpkin (Cucurbita moschata) seed protein.

Pumpkin seed meal, an underutilized by-product of the oil extraction industry, is rich in high-quality proteins but limited in food applications due to poor functional properties like low solubility. To enhance PSP solubility, this study extracted pumpkin seed protein (PSP) via alkaline solvent and acid precipitation, followed by protein-glutaminase deamidation. Deamidation improved protein-water interactions by converting amide groups to carboxyl groups. Optimal enzyme conditions (enzyme-to-protein ratio 1:100, 12-h reaction) increased PSP solubility from 19.35 % to 44.73 %. Extending deamidation to 24 h slightly boosted hydrolysis but marginally affected the deamidation extent. SDS-PAGE revealed partial degradation of 8-17 kDa proteins and the disappearance of aggregates under non-reducing conditions after 24-h treatment. Secondary structure analysis showed a 5 % reduction in α-helix and an 8 % increase in β-sheet content, with minor β-turn changes. These findings confirm that protein-glutaminase deamidation effectively improves PSP functionality.

• Publication year

  2025

• Venue

  International Journal of Biological Macromolecules

• Publication date

  2025-04-08

• Fields of study

  Agricultural and Food Sciences, Medicine

• Identifiers
  DOI 10.1016/j.ijbiomac.2025.142989PMID 40210054
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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