Innovative cold plasma modification of Caulerpa prolifera proteins: A strategy to improve techno-functional and antioxidant properties


Yücetepe A., OKUDAN E. Ş., Esatbeyoglu T.

LWT, cilt.238, 2025 (SCI-Expanded, Scopus) identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 238
  • Basım Tarihi: 2025
  • Doi Numarası: 10.1016/j.lwt.2025.118840
  • Dergi Adı: LWT
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, BIOSIS, Chemical Abstracts Core, Compendex, Directory of Open Access Journals
  • Anahtar Kelimeler: Macroalgae, Non-thermal technique, Protein, Protein functionality, Protein secondary structure
  • Akdeniz Üniversitesi Adresli: Evet

Özet

In this study, the effects of cold plasma (CP) on structural, techno-functional, and antioxidant properties of Caulerpa prolifera proteins were investigated for the first time. C. prolifera proteins were modified by CP to improve their techno-functional and antioxidant properties. CP conditions (power: 5, 47.5, 90 W; treatment time: 1, 15.5, 30 min; pressure: 30, 60, 90 Pa) were optimized to determine the effect of CP on water absorption capacity (WAC),oil absorption capacity (OAC), emulsion activity (EA), emulsion stability (ES), foaming capacity (FC), foaming stability (FS), free sulfhydryl group (SH) content, protein solubility (PS), and antioxidant activity (AOA) of the proteins extracts and functional groups, microstructure, color, and nutritional properties of the modified proteins were investigated. Optimum conditions were 87.50 W power, 6.63 min treatment time, and 90 Pa pressure. At optimum conditions, WAC, OAC, EC, ES, FC, FS, Free-SH content, AOADPPH, AOACUPRAC, and PS were 232.04 ± 10.25 g/hg, 350.66 ± 15.78 g/hg, 49.50 ± 5.05 g/hg, 49.95 ± 0.51 g/hg, 101.26 ± 7.89 g/hg, 70.10 ± 2.85 g/hg, 18.28 ± 1.50 mmol/kg, 3.78 ± 0.40 g Trolox equivalent (TE)/kg, 8.31 ± 0.01 g TE/kg, and 22.30 ± 4.02 g/hg, respectively. The findings showed that CP provided an increase in WAC, AOA, and PS of proteins and the results were confirmed by investigating changes in secondary structure of proteins.