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Effects of phosphoglycerate kinase 1 and pyruvate kinase M2 on metabolism and physiochemical changes in postmortem muscle
•Glycolysis was promoted in PGK1 and PKM2 activator groups compared to PGK1 and PKM2 inhibitor groups.•Adding PGK1 and PKM2 activators promoted desmin degradation, μ-calpain activity and caspase-3 abundance.•Troponin-T degradation with the higher level in PGK1 activator group than that in PGK1 inhib...
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Published in: | Food Chemistry: X 2024-03, Vol.21, p.101125, Article 101125 |
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Main Authors: | , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | •Glycolysis was promoted in PGK1 and PKM2 activator groups compared to PGK1 and PKM2 inhibitor groups.•Adding PGK1 and PKM2 activators promoted desmin degradation, μ-calpain activity and caspase-3 abundance.•Troponin-T degradation with the higher level in PGK1 activator group than that in PGK1 inhibitor group.•The degradation of troponin-T was promoted both in PKM2 activator and inhibitor groups.
The objective of this work was to investigate the influence of phosphoglycerate kinase-1 (PGK1) and pyruvate kinase-M2 (PKM2) activity on glycolysis, myofibrillar proteins, calpain system, and apoptosis pathways of postmortem muscle. The activity of PGK1 and PKM2 was regulated by their inhibitors and activators to construct the postmortem glycolysis vitro model and then incubated at 4 °C for 24 h. The results showed that compared to PGK1 and PKM2 inhibitors groups, the addition of PGK1 and PKM2 activators could accelerate glycogen consumption, ATP and lactate production, while declining pH value. Moreover, the addition of PGK1 and PKM2 activators could increase desmin degradation, μ-calpain activity, and caspase-3 abundance. Interestingly, troponin-T degradation was significantly increased both in PKM2 inhibitor and activator groups. It was suggested that PGK1 and PKM2 might be used as robust indicators to regulate meat quality by affecting the glycolysis, myofibrillar proteins, μ-calpain and apoptosis pathways in postmortem muscle. |
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ISSN: | 2590-1575 2590-1575 |
DOI: | 10.1016/j.fochx.2024.101125 |