Effect of static magnetic field-assisted freezing at different temperatures on the structural and functional properties of pacific white shrimp (Litopenaeus vannamei) myofibrillar protein
{"title":"Effect of static magnetic field-assisted freezing at different temperatures on the structural and functional properties of pacific white shrimp (Litopenaeus vannamei) myofibrillar protein","authors":"Qihang Wei, Qinxiu Sun, Qian Hou, Ouyang Zheng, Naiyong Xiao, Shucheng Liu","doi":"10.1016/j.foodchem.2025.142836","DOIUrl":null,"url":null,"abstract":"The effects of static magnetic field-assisted freezing (MF) on the structural and functional characteristics of <em>Litopenaeus vannamei</em> myofibrillar protein (MP) at various temperatures (−35 ~ −20 °C) were examined to assess its influence on MP and its energy-saving potential. The results indicated that −35 °C MF (MF-35) exhibited greater solubility and lower turbidity than −35 °C immersion freezing (IF-35), suggesting that MF-35 inhibited MP aggregation. MF-35 prevented the reduction in fluorescence intensity and <em>α</em>-helix content, protecting the MP tertiary and secondary structures. The emulsifying stability and gel strength of MF-35 surpassed those of the other frozen samples, indicating that MF-35 was the most efficient at mitigating the degradation of MP emulsifying and gel properties generated by freezing. No significant differences in solubility, surface hydrophobicity, emulsifying activity, and gel strength were detected between IF-35 and MF-25 (<em>P</em> > 0.05). In conclusion, MF impeded the denaturation of MP and exhibited energy-saving potential.","PeriodicalId":318,"journal":{"name":"Food Chemistry","volume":"280 1","pages":""},"PeriodicalIF":9.8000,"publicationDate":"2025-01-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1016/j.foodchem.2025.142836","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
引用次数: 0
Abstract
The effects of static magnetic field-assisted freezing (MF) on the structural and functional characteristics of Litopenaeus vannamei myofibrillar protein (MP) at various temperatures (−35 ~ −20 °C) were examined to assess its influence on MP and its energy-saving potential. The results indicated that −35 °C MF (MF-35) exhibited greater solubility and lower turbidity than −35 °C immersion freezing (IF-35), suggesting that MF-35 inhibited MP aggregation. MF-35 prevented the reduction in fluorescence intensity and α-helix content, protecting the MP tertiary and secondary structures. The emulsifying stability and gel strength of MF-35 surpassed those of the other frozen samples, indicating that MF-35 was the most efficient at mitigating the degradation of MP emulsifying and gel properties generated by freezing. No significant differences in solubility, surface hydrophobicity, emulsifying activity, and gel strength were detected between IF-35 and MF-25 (P > 0.05). In conclusion, MF impeded the denaturation of MP and exhibited energy-saving potential.
期刊介绍:
Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.