背最长肌
蛋白质组
温柔
化学
生物化学
食品科学
生物
作者
Guangyu Wu,Chuan Yang,Heather L. Bruce,Bimol C. Roy,Xia Li,Chunhui Zhang
标识
DOI:10.1021/acs.jafc.2c04207
摘要
This study was designed to investigate the differences in the proteomes of bovine Longissimus dorsi (LD) muscle during an alternating electric field (AEF)-assisted freezing–thawing–aging sequence based on a data-independent acquisition strategy. When compared to that of the only postmortem aging (OA) group, the meat quality of the freezing–thawing–aging sequence (FA) and AEF-assisted freezing–thawing–aging sequence (EA) groups showed a declining trend. However, the group assisted by AEF was significantly enhanced in color, water-holding capacity, and tenderness. Three hundred fifty-two proteins in LD muscle were differentially abundant proteins (DAPs) among FA, EA, and OA treatments. Furthermore, among the 40 DAPs in the FA versus EA comparison, 5 DAPs with variable importance in projection scores higher than 1 were identified as biochemical markers of beef quality. Bioinformatic analysis revealed that most of these proteins were involved in structural constituents of ribosome and catalytic activity. These results provide a basis for further understanding the quality of beef following a freezing–thawing–aging sequence assisted by AEF.
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