Literature DB >> 28039026

Unraveling proteome changes of Holstein beef M. semitendinosus and its relationship to meat discoloration during post-mortem storage analyzed by label-free mass spectrometry.

Qianqian Yu1, Wei Wu1, Xiaojing Tian1, Man Hou1, Ruitong Dai2, Xingmin Li1.   

Abstract

Label-free proteomics was applied to characterize the effect of post-mortem storage time (0, 4, and 9days at 4°C±1°C) on the proteome changes of M. semitendinosus (SM) in Holstein cattle, and correlations between differentially abundant proteins and meat color traits were investigated. The redness (a*) value decreased significantly (P<0.05) during post-mortem storage, meanwhile, the relative proportion of metmyoglobin increased significantly (P<0.05) from 16.99% at day 0 to 40.26% at day 9. A total of 118 proteins with significant changes (fold change>1.5, P<0.05) was identified by comparisons of day 4 vs. day 0, day 9 vs. day 0, and day 9 vs. day 4. Principal component and hierarchical cluster analyses of these proteins were performed, and results exhibited clear distinctions among samples from different storage times. Eighteen differentially abundant proteins were correlated closely with the a* value of meat. Bioinformatics analyses revealed that most of these proteins were involved in glycolysis and energy metabolism, electron-transfer processes, and the antioxidation function, which implied an underlying connection between meat discoloration and these biological processes. SIGNIFICANCE: It is always a challenge for scientists to improve the stability of meat color during post-mortem storage and retail display. However, the mechanism involved in meat discoloration has not been unraveled completely, and the application of label-free proteomics in studying meat discoloration has not been reported. Our work discovers some key proteins in SM muscle of Holstein cattle that were correlated with a* value of meat via label-free proteomics. Bioinformatics analyses revealed that some of these differentially abundant proteins were involved in glycolysis and energy metabolism, electron-transfer processes, and the antioxidation function, which implied an underlying connection between meat discoloration and these biological processes. These results provide the theoretic basis on understanding of complicated biochemical changes and underlying molecular mechanisms responsible for meat discoloration.
Copyright © 2016 Elsevier B.V. All rights reserved.

Entities:  

Keywords:  Label-free; M. semitendinosus; Meat color; Proteomics

Mesh:

Substances:

Year:  2016        PMID: 28039026     DOI: 10.1016/j.jprot.2016.12.012

Source DB:  PubMed          Journal:  J Proteomics        ISSN: 1874-3919            Impact factor:   4.044


  9 in total

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Journal:  Sci Rep       Date:  2020-08-04       Impact factor: 4.379

8.  The Quality Changes and Proteomic Analysis of Cattle Muscle Postmortem during Rigor Mortis.

Authors:  Zhenjiang Ding; Qichao Wei; Chunmei Liu; Hong Zhang; Feng Huang
Journal:  Foods       Date:  2022-01-13

9.  Proteomic Changes in Sarcoplasmic and Myofibrillar Proteins Associated with Color Stability of Ovine Muscle during Post-Mortem Storage.

Authors:  Xiaoguang Gao; Dandan Zhao; Lin Wang; Yue Cui; Shijie Wang; Meng Lv; Fangbo Zang; Ruitong Dai
Journal:  Foods       Date:  2021-12-03
  9 in total

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