Changes in proteasome activity during postmortem aging of bovine muscle

Changes in the chymotrypsin-like, trypsin-like, peptidylglutamylpeptide hydrolyzing and caseinolytic activities of proteasomes in bovine rectus abdominis muscle were measured during the first seven days of postmortem storage. Enzyme assays were performed in crude extracts under near-physiological conditions, since the activities are likely to be altered by purification. The different proteasome activities at cellular pH were stable at different times postmortem, and were 40, 76, 50 and 61% of their at-death value after 7 days of storage at 4 °C. This considerable postmortem stability of proteasome activities, despite the marked decrease in pH, allows them to play a role in meat tenderization in synergy with other proteolytic systems.