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Updated: Jan 13, 2026

High-Resolution Neutron Spectroscopy to Study Picosecond-Nanosecond Dynamics of Proteins and Hydration Water
Published on: April 28, 2022
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.
Abstract:
Self-assembled proteins can significantly inhibit ice recrystallization, offering potential for cryoprotection. Here, soybean protein amyloid fibrils (SAFs) were fabricated via combined germination and acid-heat-induced fibrillation. Germination enhanced the fibrillation efficiency of soybean protein isolate (SPI). SAFs with the strongest ice recrystallization inhibition (IRI) activity were prepared from SPI of two-day germinated soybeans after 20 h of acidic-heat treatment (SAF-20). SAF-20 exhibited concentration-dependent IRI activity, with stronger inhibition of ice crystal growth at higher concentrations. It showed high ice-affinity adsorption and ice nucleation activity without altering ice crystal morphology. Structural analyses revealed that self-assembly promoted protein aggregation and increased surface hydrophobicity and β-sheet content. These changes strengthened hydrogen bonding at the ice-water interface, forming ordered interfacial water layers that disrupted long-range water ordering and inhibited ice crystal growth. Furthermore, SAF-20 significantly improved post-thaw recovery of cryopreserved Caco-2 cells, demonstrating its cryoprotective efficacy.
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