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Changes in proteasome activity during postmortem aging of bovine muscle
Marie Lamare1, Richard G Taylor, Luc Farout
1Université Blaise Pascal, Laboratoire de Biochimie Appliquée, associé INRA, 63174 Aubiere, France.
Meat Science
|November 9, 2011
Summary
Proteasome activities in bovine muscle remained stable postmortem, suggesting a role in meat tenderization. These enzymes are crucial for improving meat quality during storage.
Area of Science:
- Biochemistry
- Food Science
- Animal Science
Background:
- Proteasomes are crucial cellular machines involved in protein degradation.
- Understanding postmortem proteasome activity is key to improving meat quality and tenderness.
- Bovine rectus abdominis muscle is a significant component of beef products.
Purpose of the Study:
- To investigate the changes in various proteasome activities in bovine muscle during early postmortem storage.
- To assess the stability of proteasome activities under physiological conditions and decreasing pH.
- To determine the potential role of proteasomes in postmortem meat tenderization.
Main Methods:
- Enzyme assays were conducted on crude extracts of bovine rectus abdominis muscle.
- Measurements included chymotrypsin-like, trypsin-like, peptidylglutamylpeptide hydrolyzing, and caseinolytic activities.
- Assays were performed at cellular pH and during the first seven days of postmortem storage at 4°C.
Main Results:
- Proteasome activities exhibited considerable stability during the first 7 days of postmortem storage.
- After 7 days, activities ranged from 40% to 76% of their initial at-death values.
- The different proteasome activities showed varying stability profiles at cellular pH.
Conclusions:
- Proteasome activities are remarkably stable postmortem in bovine muscle, even with significant pH decline.
- This stability suggests that proteasomes actively contribute to meat tenderization.
- Proteasomes likely work synergistically with other proteolytic systems to enhance meat quality.
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