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<p>This study examines the influence of cold plasma (CP) treatment on the structural and functional properties of hyacinth bean (<i>Lablab purpureus</i>) protein (HBP) in an aqueous dispersion. CP was applied at 10, 15, and 20&#xa0;kV for 20 to 100&#xa0;min, and the resulting alterations in protein conformation, oxidation, dispersion behavior, and functional performance were systematically assessed. Moderate CP treatment yielded the most pronounced structural enhancement by increasing sulfhydryl availability, while higher-intensity treatment caused a marked rise in carbonyl formation. Secondary structure analysis indicated a shift away from α-helix–dominated conformations toward higher proportions of β-turns and random coils, while fluorescence measurements exhibited a redshift. These structural changes corresponded with a reduction in particle size and an increase in zeta potential magnitude under optimal conditions, thereby enhancing dispersibility and colloidal stability. Functionally, moderate CP treatment produced clear enhancements, with solubility increasing by approximately 21%, water absorption capacity rising from 2.49 ± 0.02 to 3.49 ± 0.02&#xa0;g/g (about 40% increase), and oil absorption capacity increasing from 3.43 ± 0.04 to 5.48 ± 0.03&#xa0;g/g (about 60% increase) under optimal conditions. Emulsifying activity and emulsion stability reached their peak at 15&#xa0;kV for 80&#xa0;min, accompanied by reinforced viscoelastic behavior in emulsions. Conversely, excessive CP treatment (20&#xa0;kV for 100&#xa0;min) induced aggregation, solubility decline, and diminished functional performance. Collectively, these results demonstrate that controlled CP treatment is an effective strategy to tailor the structural flexibility and techno-functional properties of HBP for applications in plant-based and emulsion-based food systems.</p>

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Characterization of structural, functional, and rheological modifications in the hyacinth bean (Lablab purpureus) protein induced by multipin cold plasma treatment

  • 期刊论文

  • 发表日期：

    2026年1月2日

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  • Pratik Madhukar Gorde,
  • Poonam Singha,
  • Sushil Kumar Singh

摘要

This study examines the influence of cold plasma (CP) treatment on the structural and functional properties of hyacinth bean (Lablab purpureus) protein (HBP) in an aqueous dispersion. CP was applied at 10, 15, and 20 kV for 20 to 100 min, and the resulting alterations in protein conformation, oxidation, dispersion behavior, and functional performance were systematically assessed. Moderate CP treatment yielded the most pronounced structural enhancement by increasing sulfhydryl availability, while higher-intensity treatment caused a marked rise in carbonyl formation. Secondary structure analysis indicated a shift away from α-helix–dominated conformations toward higher proportions of β-turns and random coils, while fluorescence measurements exhibited a redshift. These structural changes corresponded with a reduction in particle size and an increase in zeta potential magnitude under optimal conditions, thereby enhancing dispersibility and colloidal stability. Functionally, moderate CP treatment produced clear enhancements, with solubility increasing by approximately 21%, water absorption capacity rising from 2.49 ± 0.02 to 3.49 ± 0.02 g/g (about 40% increase), and oil absorption capacity increasing from 3.43 ± 0.04 to 5.48 ± 0.03 g/g (about 60% increase) under optimal conditions. Emulsifying activity and emulsion stability reached their peak at 15 kV for 80 min, accompanied by reinforced viscoelastic behavior in emulsions. Conversely, excessive CP treatment (20 kV for 100 min) induced aggregation, solubility decline, and diminished functional performance. Collectively, these results demonstrate that controlled CP treatment is an effective strategy to tailor the structural flexibility and techno-functional properties of HBP for applications in plant-based and emulsion-based food systems.