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<p>Protein isolates obtained by aqueous extraction followed by isoelectric precipitation (pH 4.5) of <i>Lupinus albus var. multolupa</i> (WPI) and <i>Lupinus luteus L.</i> (YPI) were characterised for their physico-chemical, structural and techno-functional properties. The protein recovered was greater in YPI (82.10%) than in WPI (66.51%). WPI had higher emulsifying activity and stability, foaming capacity and oil absorption capacity compared to YPI. YPI presented higher water absorption capacity (8.98 mL/g protein) and higher foaming stability (52.59%). The film formed at the YPI powder/water interface showed a significant higher resistance compared to WPI. Differential scanning calorimetry (DSC) curves showed the presence of a single broad endothermic peak at 82.9&#xa0;°C and 91.1&#xa0;°C, corresponding respectively, to the denaturation temperature of WPI and YPI. YPI exhibited a lower emission tryptophan fluorescence intensity at 376&#xa0;nm compared to WPI, while WPI showed higher surface hydrophobicity than YPI. The two isolates showed higher amounts of β-sheets and β-turns. It could be concluded that the structure composition of the WPI and YPI impacted significantly their functional properties.</p>

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A comparative characterisation of functional and structural properties of white and yellow lupin protein isolates

  • 期刊论文

  • 发表日期：

    2026年2月17日

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  • Paterne Nahimana,
  • Inès Bouaicha,
  • Christine Chèné,
  • Hanaa Abdelmoumen,
  • Moncef Hammami,
  • Christophe Blecker,
  • Romdhane Karoui

摘要

Protein isolates obtained by aqueous extraction followed by isoelectric precipitation (pH 4.5) of Lupinus albus var. multolupa (WPI) and Lupinus luteus L. (YPI) were characterised for their physico-chemical, structural and techno-functional properties. The protein recovered was greater in YPI (82.10%) than in WPI (66.51%). WPI had higher emulsifying activity and stability, foaming capacity and oil absorption capacity compared to YPI. YPI presented higher water absorption capacity (8.98 mL/g protein) and higher foaming stability (52.59%). The film formed at the YPI powder/water interface showed a significant higher resistance compared to WPI. Differential scanning calorimetry (DSC) curves showed the presence of a single broad endothermic peak at 82.9 °C and 91.1 °C, corresponding respectively, to the denaturation temperature of WPI and YPI. YPI exhibited a lower emission tryptophan fluorescence intensity at 376 nm compared to WPI, while WPI showed higher surface hydrophobicity than YPI. The two isolates showed higher amounts of β-sheets and β-turns. It could be concluded that the structure composition of the WPI and YPI impacted significantly their functional properties.