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Comparative analysis of high-intensity non-thermal physical treatments on the structural and functional properties of Spirulina platensis protein

  • Junwen Wang
  • , Qinhao Guan
  • , Zhiting Liu
  • , Jiangfei Li
  • , Li Baiyi Zhou
  • , Qiaoyun Qi
  • , Yue Zhang
  • , Elena Ibañez
  • , Alejandro Cifuentes
  • , Weihong Lu*
  • *Corresponding author for this work
  • School of Medicine and Health, Harbin Institute of Technology
  • Harbin Institute of Technology
  • CSIC

Research output: Contribution to journalArticlepeer-review

Abstract

Spirulina platensis protein (SPP) has attracted attention as a sustainable alternative to conventional proteins. However, its structural and functional performance under different processing conditions remains underexplored. This study investigated the effects of three non-thermal physical treatments—high hydrostatic pressure (HHP, 100–600 MPa), high-intensity ultrasound (HIU, 70–100 % amplitude), and high-speed shear homogenization (HSS, 1.0–2.5 W)—on the structure and functionality of SPP. SDS-PAGE revealed treatment-specific alterations in protein subunits, accompanied by distinct changes in sulfhydryl/disulfide, surface hydrophobicity, intrinsic fluorescence, and secondary structure. HIU induced the strongest structural disruption, characterized by reduced α-helix content, exposure of hydrophobic residues, and a pronounced decrease in particle size and ζ-potential, whereas HHP promoted unfolding at moderate pressures but aggregation at higher levels. HSS primarily reduced particle size with moderate effects on unfolding. Collectively, these results indicate that high-Intensity non-Thermal physical treatments effectively modulate the functional properties of SPP, demonstrating its potential as a protein ingredient for food applications.

Original languageEnglish
Article number107623
JournalUltrasonics Sonochemistry
Volume122
DOIs
StatePublished - Nov 2025

Keywords

  • Emulsifying properties
  • Foaming properties
  • High-intensity ultrasound
  • Non-thermal physical modifications
  • Spirulina platensis protein
  • Structure

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