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Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions

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成果类型:
期刊论文
作者:
Liu, Chang;Tang, Pan-Pan;Liu, Xiu-Bin;AlMasoud, Najla;Alomar, Taghrid S;...
通讯作者:
Rana Muhammad Aadil
作者机构:
[Tang, Pan-Pan; Liu, Xiu-Bin] College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China
School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China
[AlMasoud, Najla; Alomar, Taghrid S] Department of Chemistry, College of Science, Princess Nourah bint Abdulrahman University, PO, Box 84428, Riyadh 11671, Saudi Arabia
Guangdong Key Laboratory of Food Intelligent Manufacturing, Foshan University, Foshan 528225, China
Changsha Innovation Institute for Food, Changsha, 410128, China
通讯机构:
[Rana Muhammad Aadil] N
National Institute of Food Science and Technology, University of Agriculture, Faisalabad, 38000, Pakistan
语种:
英文
关键词:
Amyloid fibril;Astaxanthin;Cold plasma;High internal phase emulsion;Ovalbumin
期刊:
Food Chemistry: X
ISSN:
2590-1575
年:
2025
卷:
29
页码:
102835
机构署名:
本校为第一机构
院系归属:
食品科学技术学院
摘要:
The morphological characteristics of cold plasma (CP)-induced ovalbumin (OVA) amyloid fibrils (OAFs) and their ability to stabilize astaxanthin-loaded high internal phase emulsions (HIPEs) were investigated. The results indicated that CP treatment significantly accelerated OVA fibrillization by inducing its globular structure unfolding and polypeptide cleavage, leading to the rapid formation of short, worm-like fibrils within 10 min of fibrillation. Compared to untreated OVA, which had a diameter of 18.65 ± 6.47 nm, the length of OVA worm-...

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