Abstract
A mechanism of postmortem tenderization by adenosine 5'-monophosphate (AMP) on spent hen meat was investigated. Breast meat samples were made into a rectangular size of 7.5 × 5 × 2 cm and grouped into 5 different treatments, followed by immersion for 24 h at 4 ± 2°C in AMP marinade solutions of 0, 15, 30, 45, and 60 mmol/L that dissolved in 0.9% (w/v) saline solution. To investigate the enzymatic changes and tenderness-related traits, samples were stored until day 5 at a temperature of 2 ± 2°C. Result showed that each increase of 15 mmol/L AMP within marinade solution remarkably improved the myofibril fragmentation index and texture properties. The upregulation of tenderness-related enzymes was found for caspase-3 at 1 to 20.4 fold and 1 to 1.2 fold higher for the cathepsin-B, while a slight effect on calpains enzyme was observed. When compared with day 0 as a reference sample, the activity of the caspase-3 enzyme was more stable, as was cathepsin-B on the ultimate storage day, while the calpains enzyme showed a declining activity even after treatment. The flavor enhancement of 2.16- to 5.10-fold seemed to be a consequence of the AMP conversion into IMP that was responsible for the intensification of the umami-like flavor. No adverse effect was observed for instrumental surface color during the postmortem period. Therefore, this study suggested that the synergistic results after AMP treatment strongly contributed to postmortem tenderization mainly through cathepsin-B and caspase-3 enzyme upregulation, which led to more myofibrillar fragmentation and structural alteration of myofibrillar protein.