globalchange  > 气候变化与战略
DOI: 10.1002/jsfa.10045
Effects of temperature on protein phosphorylation in postmortem muscle
Author: Ren C.; Hou C.; Li Z.; Li X.; Bai Y.; Zhang D.
Source Publication: Journal of the Science of Food and Agriculture
ISSN: 225142
Publishing Year: 2020
Volume: 100, Issue:2
Language: 英语
Keyword: ATP content ; glycolysis ; muscle ; phosphorylation level ; temperature
Scopus Keyword: muscle protein ; animal ; chemistry ; devices ; food storage ; glycolysis ; meat ; phosphorylation ; postmortem change ; procedures ; sheep ; skeletal muscle ; temperature ; Animals ; Food Storage ; Glycolysis ; Meat ; Muscle Proteins ; Muscle, Skeletal ; Phosphorylation ; Postmortem Changes ; Sheep ; Temperature
English Abstract: BACKGROUND: Phosphorylation is one of the most important post-translational modifications. Currently, many postmortem protein phosphorylation studies in muscle have been related to meat quality such as tenderness and color stability. However, the effects of various storage temperatures (25, 15, 4 and −1.5 °C) on the phosphorylation level of protein are poorly understood. Changes in the protein phosphorylation levels in postmortem ovine muscle at various storage temperatures were determined in this study. RESULTS: The obtained data showed that pH decline rate was significantly inhibited at −1.5 °C from 12 h to 7 days postmortem (P < 0.05). The ATP consumption rate was higher at 25 °C than that at other three temperatures (P < 0.05). Analysis of the temperature, pH and ATP content revealed that the ATP content was related to the phosphorylation levels of individual protein bands. Phosphorylated myofibrillar and sarcoplasmic proteins, such as myosin binding protein C, troponin T3, myosin light chain 1, glucose-6-phosphate isomerase and pyruvate kinase, were mainly involved in glycolysis and muscle contraction. CONCLUSION: The global and specific protein phosphorylation levels can be influenced by the postmortem storage temperature of muscle. Phosphorylation of proteins was correlated with glycolysis and muscle contraction. Certain phosphorylated proteins, such as heat shock proteins, require further study to clarify their effects on meat traits. © 2019 Society of Chemical Industry. © 2019 Society of Chemical Industry
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被引频次[WOS]:3   [查看WOS记录]     [查看WOS中相关记录]
Document Type: 期刊论文
Appears in Collections:气候变化与战略

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Affiliation: Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-Product Processing, Ministry of Agriculture and Rural Affairs, Beijing, China

Recommended Citation:
Ren C.,Hou C.,Li Z.,et al. Effects of temperature on protein phosphorylation in postmortem muscle[J]. Journal of the Science of Food and Agriculture,2020-01-01,100(2)
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