| Status | 已发表Published |
| Title | Ultrasonic treatment treated sea bass myofibrillar proteins in low-salt solution: Emphasizing the changes on conformation structure, oxidation sites, and emulsifying properties |
| Creator | |
| Date Issued | 2024-03-01 |
| Source Publication | Food Chemistry
 |
| ISSN | 0308-8146 |
| Volume | 435 |
| Abstract | The physiochemical properties, structure characteristics, oxidation, and emulsifying properties of myofibrillar proteins (MPs) in low salt solution after treated by the ultrasound were investigated. The solubility, mean diameters, sulfhydryl content, and carbonyl contents of MPs after ultrasonic treatment increased, while the turbidity decreased. The surface hydrophobicity of MPs with 200 W–600 W treatment increased, but decreased at 800 W treatment. The circular dichroism analysis revealed that α-helix content increased, while β-sheet and random coil content decreased after ultrasonic treatment. Fluorescence spectroscopy indicated the fluorescence intensities of MPs were increased after ultrasonic treatment. SDS-PAGE results showed more protein polymers due to myosin heavy chain (MHC) aggregation via disulfide bonds. Based on LC-MS/MS result, the myosin heavy chain was susceptible to oxidation, with monooxidation being the main oxidative modification. Finally, the emulsions stabilized by ultrasonically treated MPs, especially those treated at 800 W, exhibited decreased particle size, improved uniformity, and enhanced stability. |
| Keyword | Emulsifying properties Low-salt solution Myofibrillar protein Oxidation Ultrasonic treatment |
| DOI | 10.1016/j.foodchem.2023.137564 |
| URL | View source |
| Indexed By | SCIE |
| Language | 英语English |
| WOS Research Area | Chemistry ; Food Science & Technology ; Nutrition & Dietetics |
| WOS Subject | Chemistry, Applied ; Food Science & Technology ; Nutrition & Dietetics |
| WOS ID | WOS:001097696900001 |
| Scopus ID | 2-s2.0-85173557298 |
| Citation statistics | |
| Document Type | Journal article |
| Identifier | http://repository.uic.edu.cn/handle/39GCC9TT/11395 |
| Collection | Beijing Normal-Hong Kong Baptist University |
| Corresponding Author | Li, Bing |
| Affiliation | 1.College of Food Science and Engineering,Guangdong Province Key Laboratory for Green Processing of Natural Products and Product Safety,Engineering Research Center of Starch and Plant Protein Deep Processing,South China University of Technology 2.School of Chemical Engineering and Energy Technology,Dongguan University of Technology,Dongguan,523808,China 3.College of Biological Science and Technology,Fuzhou University,Fuzhou,350108,China 4.International School of Public Health and One Health,Hainan Medical University,Haikou,571199,China 5.Beijing Normal University-Hong Kong Baptist University United International College,Zhuhai,China |
| Recommended Citation GB/T 7714 | Lan, Meijuan,Li, Tongshuai,Li, Linet al. Ultrasonic treatment treated sea bass myofibrillar proteins in low-salt solution: Emphasizing the changes on conformation structure, oxidation sites, and emulsifying properties[J]. Food Chemistry, 2024, 435. |
| APA | Lan, Meijuan., Li, Tongshuai., Li, Lin., Wang, Shaoyun., Chen, Juncheng., .. & Li, Bing. (2024). Ultrasonic treatment treated sea bass myofibrillar proteins in low-salt solution: Emphasizing the changes on conformation structure, oxidation sites, and emulsifying properties. Food Chemistry, 435. |
| MLA | Lan, Meijuan,et al."Ultrasonic treatment treated sea bass myofibrillar proteins in low-salt solution: Emphasizing the changes on conformation structure, oxidation sites, and emulsifying properties". Food Chemistry 435(2024). |
| Files in This Item: | There are no files associated with this item. | |||||
Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.
BNBU 
Library
Edit Comment