Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions
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 indu...
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Elsevier
2025-07-01
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| Series: | Food Chemistry: X |
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590157525006820 |
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| author | Chang Liu Pan-Pan Tang Xiu-Bin Liu Najla AlMasoud Taghrid S. Alomar Rana Muhammad Aadil Jun-Hu Cheng Zhi-Wei Liu |
| author_facet | Chang Liu Pan-Pan Tang Xiu-Bin Liu Najla AlMasoud Taghrid S. Alomar Rana Muhammad Aadil Jun-Hu Cheng Zhi-Wei Liu |
| author_sort | Chang Liu |
| collection | DOAJ |
| description | 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-like fibrils progressively increased from 69.17 ± 23.84 nm (10 min) to 114.94 ± 38.04 nm (8 h) before decreasing to 92.24 ± 36.22 nm (24 h). The ability of OVA to stabilize HIPEs was significantly improved following fibrillation. Notably, the shorter fibrils of OAFs-10 min and OAFs-24 h exhibited superior stability in HIPEs compared to the longer fibril of OAFs-8 h. The reason may be ascribed to the robust interface adsorption ability of OAFs-10 min and OAFs-24 h with shorter length, generating a dense and thick interfacial layer in the oil/water emulsion (maximum 11.57 ± 1.98 %), as confirmed by confocal laser scanning microscopy (CLSM) imaging and interface protein adsorption analysis (maximum 31.61 ± 2.49 %), thereby preventing droplet coalescence. Additionally, HIPEs stabilized by OAFs-10 min exhibited a higher oil fraction (82.5 %), superior ionic (1200 mM) and thermal stability (100 °C), and greater astaxanthin retention (91.55 ± 1.97 %, 1200 mM) compared to those stabilized by other OAFs. Meanwhile, HIPEs stabilized by OAFs-24 h exhibited enhanced stability under freeze-thaw cycles and centrifugation, with centrifugal stability constant (Ke) of 16.18 ± 4.78 %. |
| format | Article |
| id | doaj-art-c5ba832e0d794c38b06d67a5b3f6cb7b |
| institution | Kabale University |
| issn | 2590-1575 |
| language | English |
| publishDate | 2025-07-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Food Chemistry: X |
| spelling | doaj-art-c5ba832e0d794c38b06d67a5b3f6cb7b2025-08-20T03:41:17ZengElsevierFood Chemistry: X2590-15752025-07-012910283510.1016/j.fochx.2025.102835Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsionsChang Liu0Pan-Pan Tang1Xiu-Bin Liu2Najla AlMasoud3Taghrid S. Alomar4Rana Muhammad Aadil5Jun-Hu Cheng6Zhi-Wei Liu7College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China; School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, ChinaCollege of Food Science and Technology, Hunan Agricultural University, Changsha 410128, ChinaCollege of Food Science and Technology, Hunan Agricultural University, Changsha 410128, ChinaDepartment of Chemistry, College of Science, Princess Nourah bint Abdulrahman University, PO, Box 84428, Riyadh 11671, Saudi ArabiaDepartment of Chemistry, College of Science, Princess Nourah bint Abdulrahman University, PO, Box 84428, Riyadh 11671, Saudi ArabiaNational Institute of Food Science and Technology, University of Agriculture, Faisalabad, 38000, Pakistan; Corresponding author.School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China; Guangdong Key Laboratory of Food Intelligent Manufacturing, Foshan University, Foshan 528225, China; Corresponding author at: School of Food Science and Engineering, South China University of Technology, Guangzhou 510641, China.College of Food Science and Technology, Hunan Agricultural University, Changsha 410128, China; Guangdong Key Laboratory of Food Intelligent Manufacturing, Foshan University, Foshan 528225, China; Changsha Innovation Institute for Food, Changsha, 410128, China; Corresponding author at: College of Food Science and Technology, Hunan Agricultural University, Changsha, 410128, China.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-like fibrils progressively increased from 69.17 ± 23.84 nm (10 min) to 114.94 ± 38.04 nm (8 h) before decreasing to 92.24 ± 36.22 nm (24 h). The ability of OVA to stabilize HIPEs was significantly improved following fibrillation. Notably, the shorter fibrils of OAFs-10 min and OAFs-24 h exhibited superior stability in HIPEs compared to the longer fibril of OAFs-8 h. The reason may be ascribed to the robust interface adsorption ability of OAFs-10 min and OAFs-24 h with shorter length, generating a dense and thick interfacial layer in the oil/water emulsion (maximum 11.57 ± 1.98 %), as confirmed by confocal laser scanning microscopy (CLSM) imaging and interface protein adsorption analysis (maximum 31.61 ± 2.49 %), thereby preventing droplet coalescence. Additionally, HIPEs stabilized by OAFs-10 min exhibited a higher oil fraction (82.5 %), superior ionic (1200 mM) and thermal stability (100 °C), and greater astaxanthin retention (91.55 ± 1.97 %, 1200 mM) compared to those stabilized by other OAFs. Meanwhile, HIPEs stabilized by OAFs-24 h exhibited enhanced stability under freeze-thaw cycles and centrifugation, with centrifugal stability constant (Ke) of 16.18 ± 4.78 %.http://www.sciencedirect.com/science/article/pii/S2590157525006820Cold plasmaOvalbuminAmyloid fibrilHigh internal phase emulsionAstaxanthin |
| spellingShingle | Chang Liu Pan-Pan Tang Xiu-Bin Liu Najla AlMasoud Taghrid S. Alomar Rana Muhammad Aadil Jun-Hu Cheng Zhi-Wei Liu Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions Food Chemistry: X Cold plasma Ovalbumin Amyloid fibril High internal phase emulsion Astaxanthin |
| title | Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions |
| title_full | Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions |
| title_fullStr | Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions |
| title_full_unstemmed | Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions |
| title_short | Cold plasma-induced ovalbumin amyloid fibrils: Morphological characteristics and stability on astaxanthin-loaded high internal phase emulsions |
| title_sort | cold plasma induced ovalbumin amyloid fibrils morphological characteristics and stability on astaxanthin loaded high internal phase emulsions |
| topic | Cold plasma Ovalbumin Amyloid fibril High internal phase emulsion Astaxanthin |
| url | http://www.sciencedirect.com/science/article/pii/S2590157525006820 |
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