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Soybean Protein Amyloid Fibrils as Natural Cryoprotectants: Structural Characterization and Water Interaction
Guannan Liu1, Ying Wang1, Xilin Niu1
1Sanya Institute of Nanjing Agricultural University, Whole Grain Food Engineering Research Center, College of Food Science and Technology, Nanjing Agricultural University, Nanjing, Jiangsu 210095, China.
Biomacromolecules
|January 9, 2026
Summary
Soybean protein amyloid fibrils (SAFs) effectively inhibit ice recrystallization. These SAFs demonstrate significant cryoprotective potential, improving cell recovery after freezing.
Area of Science:
- Biomaterials Science
- Protein Self-Assembly
- Cryobiology
Background:
- Self-assembled proteins can inhibit ice recrystallization, crucial for cryoprotection.
- Soybean protein isolate (SPI) can be processed into amyloid fibrils (SAFs).
Purpose of the Study:
- To fabricate soybean protein amyloid fibrils (SAFs) with enhanced ice recrystallization inhibition (IRI) activity.
- To investigate the structural basis of SAFs' IRI activity and their cryoprotective efficacy.
Main Methods:
- Combined germination and acid-heat treatment to fabricate SAFs from SPI.
- Assessed IRI activity, ice nucleation, and ice crystal morphology.
- Analyzed structural changes (aggregation, hydrophobicity, β-sheet content).
- Evaluated cryoprotective effect on Caco-2 cells post-thaw.
Main Results:
- Two-day germinated SPI treated for 20h (SAF-20) showed the strongest IRI activity.
- SAF-20 exhibited concentration-dependent IRI and ice nucleation without altering ice morphology.
- Structural analysis revealed increased aggregation, hydrophobicity, and β-sheet content in SAFs.
- SAF-20 significantly improved post-thaw recovery of cryopreserved Caco-2 cells.
Conclusions:
- Optimized SAFs derived from germinated soybean protein exhibit potent ice recrystallization inhibition.
- Structural modifications enhance protein-ice interactions, leading to cryoprotection.
- SAFs show promise as effective cryoprotective agents for cell preservation.
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