Quality changes of whitespotted conger (Conger myriaster) based physicochemical changes and label-free proteomics analysis during frozen storage
文献类型： 外文期刊
作者： Chen, Hui 1 ; Ge, Yinggang 2 ; Yang, Ting 3 ; Wang, Shanshan 1 ; Liu, Nan 1 ; Sun, Yong 1 ; Zhou, Deqing 1 ; Xi, Rui 1 ; Sun, Guohui 1 ;
作者机构： 1.Chinese Acad Fishery Sci, Yellow Sea Fisheries Res Inst, 106 Nanjing Rd, Qingdao 266071, Shandong, Peoples R China
2.Xinjiang Univ, Coll Life Sci & Technol, 777 Huarui St, Urumqi 830046, Xinjiang, Peoples R China
3.Qingdao Huanghai Univ, Sch Med, Dept Basic Med, 1145 Linghai Rd, Qingdao 266427, Shandong, Peoples R China
4.106 Nanjing Rd, Qingdao 266071, Shandong, Peoples R China
关键词： Whitespotted conger; Frozen storage; Protein degradation; Quality deterioration; Proteomics analysis
期刊名称：CURRENT RESEARCH IN FOOD SCIENCE （ 影响因子：6.2； 五年影响因子：6.2 ）
ISSN：
年卷期： 2024 年 8 卷
页码：
收录情况： SCI
摘要： Whitespotted conger (Conger myriaster) muscle proteins were susceptible to oxidative denaturation during frozen storage. The objective of this study was to investigate the alterations in quality through physicochemical analysis and proteomics after whitespotted conger stored at temperatures of -18 degrees C and -60 degrees C. The microstructural observation revealed the noticeable variations such as increased interstitial space and fractured muscle fibre with extension of frozen storage time, and the muscle fibre of whitespotted conger stored at -60 degrees C were more intact than those stored at -18 degrees C. The raised TVB-N value indicated that the freshness of whitespotted conger decreased during 120-day frozen storage period. Analysis of myofibrillar protein content and SDS-PAGE demonstrated that compared to -18 degrees C, lower storage temperature (-60 degrees C) could better maintain the structure of whitespotted conger muscle by inhibiting protein degradation and oxidation. To reveal the mechanism of protein degradation, label-free quantitative proteomic analysis was performed through LC-MS/MS. The structural proteins including domain-associated proteins and actin-related proteins were up-regulated during frozen storage, but the phosphoglycerate kinase, phosphoglycerate mutase, and fructose-bisphosphate aldolase were down-regulated. Storage at -18 degrees C accelerated the up- or down-regulation of those differentially abundant proteins. According to KEGG analysis, up- or down-regulated pathways such as glycolysis/gluconeogenesis, carbon metabolism, biosynthesis of amino acids, and calcium signalling pathway mainly accounted for the protein degradation and quality reduction of whitespotted conger at low temperature. These results provided a theoretical basis for improving the quality stability of whitespotted conger during frozen storage.
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