Octenyl succinic anhydride-modified amyloid protein fibrils demonstrate enhanced ice recrystallization inhibition activity and dispersibility.
Int J Biol Macromol
; 252: 126439, 2023 Dec 01.
Article
em En
| MEDLINE
| ID: mdl-37611688
ABSTRACT
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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01-internacional
Base de dados:
MEDLINE
Assunto principal:
Amido
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Gelo
Idioma:
En
Revista:
Int J Biol Macromol
Ano de publicação:
2023
Tipo de documento:
Article
País de afiliação:
China