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<p>There is growing global interest in alternative protein sources to replace meat in the human diet. As such, the current study investigated the techno-functional potential of microalgal protein isolated from <i>Chlorella vulgaris</i> (CHP) for food applications. Light microscopy confirmed green, unicellular coccoid cells with cup-shaped chloroplasts. CHP contained 56.87% protein and 199.31&#xa0;mg/g total amino acids. SEM revealed smooth, sheet-like crystalline morphology for CHP, in contrast to the octahedral and irregular surfaces observed in soya (SP) and pea protein (PP). Circular dichroism indicated reduced α-helix and β-turn structures and increased β-sheet and random coil contents in CHP relative to SP and PP. XRD patterns of all proteins exhibited an A-type crystalline structure. CHP also demonstrated superior thermal stability, with a denaturation temperature of 60.77&#xa0;°C and the highest enthalpy of denaturation (194.63&#xa0;J/g), exceeding the values for SP and PP. SDS-PAGE showed that CHP proteins ranged from 25–60&#xa0;kDa, compared with broader distributions in SP (2–100&#xa0;kDa) and PP (24–95&#xa0;kDa). Functionally, CHP exhibited the greatest surface hydrophobicity, highest foaming capacity (91.5%) and stability, strongest emulsion capacity (75.08%) and stability, and comparable water and oil absorption capacities. Overall, CHP demonstrates promising structural and functional attributes, supporting its potential as an effective alternative protein for meat analogue development.</p>

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Production and techno-characterization of Chlorella vulgaris microalgae as an alternative meat protein: Comparison with soya and pea proteins

  • 期刊论文

  • 发表日期：

    2026年3月5日

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  • Rehana Akhter,
  • F. A. Masoodi,
  • Touseef Ahmed Wani

摘要

There is growing global interest in alternative protein sources to replace meat in the human diet. As such, the current study investigated the techno-functional potential of microalgal protein isolated from Chlorella vulgaris (CHP) for food applications. Light microscopy confirmed green, unicellular coccoid cells with cup-shaped chloroplasts. CHP contained 56.87% protein and 199.31 mg/g total amino acids. SEM revealed smooth, sheet-like crystalline morphology for CHP, in contrast to the octahedral and irregular surfaces observed in soya (SP) and pea protein (PP). Circular dichroism indicated reduced α-helix and β-turn structures and increased β-sheet and random coil contents in CHP relative to SP and PP. XRD patterns of all proteins exhibited an A-type crystalline structure. CHP also demonstrated superior thermal stability, with a denaturation temperature of 60.77 °C and the highest enthalpy of denaturation (194.63 J/g), exceeding the values for SP and PP. SDS-PAGE showed that CHP proteins ranged from 25–60 kDa, compared with broader distributions in SP (2–100 kDa) and PP (24–95 kDa). Functionally, CHP exhibited the greatest surface hydrophobicity, highest foaming capacity (91.5%) and stability, strongest emulsion capacity (75.08%) and stability, and comparable water and oil absorption capacities. Overall, CHP demonstrates promising structural and functional attributes, supporting its potential as an effective alternative protein for meat analogue development.