Proteomics Studies on Myoglobin Content and Its Transformation into Derivatives in Muscle of Qinchuan Cattle during Postmortem Storage

被引：0
|
作者：
Zhang X. [1 ]
Yang B. [2 ]
Li Y. [1 ]
Luo R. [1 ]
Ruan Z. [1 ]
Sa M. [1 ]
Zhao J. [1 ]
机构：
[1] School of Agriculture, Ningxia University, Yinchuan
[2] School of Life Sciences, Ningxia University, Yinchuan
来源：
Shipin Kexue/Food Science | 2021年 / 42卷 / 07期
关键词：
4D-label-free proteomics; Meat color; Meat of Qinchuan cattle; Myoglobin; Myoglobin derivatives;
D O I：
10.7506/spkx1002-6630-20200315-239
中图分类号：
学科分类号：
摘要：
In this paper, 4D-label-free proteomics (4D-LFQ) was used to explore changes in the content of myoglobin and its transformation into derivatives in the Longissimus dorsi muscle in Qinchuan cattle during the first eight days of postmortem storage.The results showed that during storage from day 0 to day 4, the expression of the myoglobin had an upward trend, but then decreased.Totally 14 differentially expressed proteins related to myoglobin and its derivatives were identified, including metabolic enzyme, oxidoreductase, peroxidase and chaperone protein, which could together regulate the change in myoglobin content and the transformation between myoglobin and its three derivatives.Specifically, myoglobin expression showed an overall downward trend, and the relative content of oxymyoglobin continuously declined, while the relative contents of deoxymyoglobin and metmyoglobin gradually rose, resulting in browning in meat color.The results of this study will be useful for understanding the complex biochemical mechanism underlying color changes in the meat of Qinchuan cattle during storage. © 2021, China Food Publishing Company. All right reserved.
引用
收藏
页码：226 / 231
页数：5
相关论文
共 25 条
  • [1] WU Shuang, LUO Xin, YANG Xiaoyin, Et al., Understanding the development of color and color stability of dark cutting beef based on mitochondrial proteomics, Meat Science, 163, (2020)
  • [2] HERAWATI M, WARDAYA, MULYAWAN W, Et al., Expression of hypoxia-inducible factor-1α and myoglobin in rat heart as adaptive response to intermittent hypobaric hypoxia exposure, HAYATI Journal of Biosciences, 24, 3, pp. 131-135, (2017)
  • [3] YIN Shuang, FAUSTMAN C, TATIYABORWORNTHAM N, Et al., Species-specific myoglobin oxidation, Journal of Agricultural and Food Chemistry, 59, 22, pp. 12198-12203, (2011)
  • [4] pp. 12-14, (2019)
  • [5] RANDEZ-GILL F, SANCHEZ-ADRIA I E, ESTRUCH F, Et al., The formation of hybrid complexes between isoenzymes of glyceraldehyde-3-phosphate dehydrogenase regulates its aggregation state, the glycolytic activity and sphingolipid status in Saccharomyces cerevisiae, Microbial Biotechnology, 13, 2, pp. 562-571, (2020)
  • [6] pp. 29-31, (2013)
  • [7] pp. 10-12, (2017)
  • [8] pp. 27-28, (2016)
  • [9] pp. 54-59, (2019)
  • [10] pp. 6-8, (2018)
123