Octenyl succinic anhydride-modified amyloid protein fibrils demonstrate enhanced ice recrystallization inhibition activity and dispersibility.

Octenyl succinic anhydride (OSA) modification of amyloid proteins fibrils (APFs) was employed to improve dispersibility and ice recrystallization inhibition activity. OSA mainly reacted with the amino groups of APFs without significantly changing morphology. OSA-modified APFs (OAPFs) had lower pI, carried more negative charges, and were more hydrophobic. OSA-modification showed a pH-dependent effect on the dispersibility of fibrils. At pH 7.0, OSA-modification improved dispersibility and inhibited heat-induced gelation of fibrils at weakened electrostatic repulsion. OAPFs were more prone to aggregation with lower dispersity at acidic pH values and demonstrated stronger IRI activity than unmodified fibrils at pH 7.0. Our findings indicate OSA-modification favors the industrial application of APFs as an ice recrystallization inhibitor with enhanced dispersibility.

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Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.