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

被引：2

作者：

Fu, Yuying ^{[1
]}

Li, Yuan ^{[1
]}

Everett, David W. ^{[1
,2
,3
]}

Weng, Shuni ^{[1
]}

Zhai, Yun ^{[1
]}

Wang, Mengtin ^{[1
]}

Li, Teng ^{[1
]}

机构：

[1] Zhejiang Gongshang Univ, Sch Food Sci & Biotechnol, Hangzhou 310018, Peoples R China

[2] AgResearch, Palmerston North, New Zealand

[3] Riddet Inst, Palmerston North, New Zealand

来源：

INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES | 2023年 / 252卷

基金：

中国国家自然科学基金;

关键词：

Amyloid protein fibrils; Octenyl succinic anhydride; Ice recrystallization inhibition; GROWTH-INHIBITION; BINDING; AGGREGATION; FABRICATION; PEPTIDES;

D O I：

10.1016/j.ijbiomac.2023.126439

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 OSAmodification favors the industrial application of APFs as an ice recrystallization inhibitor with enhanced dispersibility.

引用

页数：10

共 56 条

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