4.7 Article

Differential Proteomics Analysis of Penaeus vannamei Muscles with Quality Characteristics by TMT Quantitative Proteomics during Low-Temperature Storage

期刊

JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
卷 69, 期 10, 页码 3247-3254

出版社

AMER CHEMICAL SOC
DOI: 10.1021/acs.jafc.0c08110

关键词

TMT; proteomics; Penaeus vannamei muscles; low-temperature storage

资金

  1. National Key R&D Program of China [2018YFD0901001-04]
  2. National Natural Science Foundation of China [31801465]

向作者/读者索取更多资源

In this study, tandem mass tag technology was used to investigate the relationship between proteome changes and quality characteristics of Penaeus vannamei (PNVN) muscles during low-temperature storage. A total of 506 differentially expressed proteins were identified, with nine proteins significantly correlated with quality characteristics and most proteins involved in binding, metabolic enzymes, and protein turnover. These findings provide insights into the proteome changes and mechanisms of quality decline in PNVN muscles during low-temperature storage.
A tandem mass tag technology, based on the quantitative proteomics strategy, was applied to investigate the relationships between proteome changes of Penaeus vannamei (PNVN) muscles and quality characteristics during low-temperature storage. 506 proteins were found as differentially expressed proteins (DEPs) after 10 days of storage under treatments of refrigerated storage (5 degrees C), ice temperature storage (0 degrees C), and particle freezing storage (-3 degrees C) compared with a fresh group (0 day). In addition, Uniprot Knowledgebase (UniprotKB), Gene Ontology enrichment, and Kyoto Encyclopedia of Genes and Genomes were reported. Correlation analysis indicated that nine DEPs were significantly related to quality characteristics-pH, color, and texture. Bioinformatics analysis showed that most of DEPs were involved in binding proteins, metabolic enzyme, and protein turnover. Besides, several DEPs could be good candidate biomarkers of muscle decline. These results could help to further comprehend the proteome changes and mechanisms of the quality decline of PNVN muscles during low-temperature storage.

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