Effects of four amino acids (Arg, Gly, Lys, and Pro) on the structural integrity and emulsification properties in myofibrillar protein of <scp> <i>Litopenaeus vannamei</i> </scp> during freeze–thaw cycles
Arg, Gly, Lys, and Pro can interact with ions through hydrogen bonds to bind to specific sites of shrimp MP, inhibiting its structural damage and oxidative aggregation during F-T cycles, thereby enhancing the stability of the emulsion and providing theoretical support for the development of natural cryoprotectants. © 2025 Society of Chemical Industry.
Authors
- Xiaoshi Wei (ORCID: https://orcid.org/0000-0002-1089-4517)
- Xinyi Meng (ORCID: https://orcid.org/0000-0002-9460-8003)
- Xiaofang Zeng
- Qiaoyu Liu (ORCID: https://orcid.org/0000-0002-1719-6252)
- Lin Cai (ORCID: https://orcid.org/0009-0008-4491-5380)
- Hao Dong (ORCID: https://orcid.org/0000-0001-7611-3341)
- Weidong Bai (ORCID: https://orcid.org/0000-0002-7209-1699)
- Sili Xiao (ORCID: https://orcid.org/0000-0002-3337-6042)
Institutions
- Ministry of Education of the People's Republic of China (CN)
- Guangzhou Electronic Technology (China) (CN)
- Zhongkai University of Agriculture and Engineering (CN)
Publication Details
- Journal
- Journal of the Science of Food and Agriculture
- Published
- 2025-10-29
- DOI
- https://doi.org/10.1002/jsfa.70278
- Primary Topic
- Crustacean biology and ecology
- Type
- article
- Field-Weighted Citation Impact
- 0.00