Tenderization of fish muscle results in its deterioration. Different proteolytic systems exist within the muscular cell. In this decade we have integrated a new process capable to better explain the meat tenderization process namely apoptosis. This process is orchestrated by the family of cysteine aspartate-specific proteases named caspases, which are probably the first proteolytic system to be implicated in postmortem proteolysis and meat tenderization. Our study contribute to understanding proteolysis integrating the apoptosis process in the biochemistry of fish muscle. We have choosen three hallmarks of apoptosis: phosphatidylserine (PS) externalization observed by using a FITC-annexin V conjugate as a specific probe, cytochrme c liberation from mithochondria and actin degradation by western blot using a polyclonal anti-actin and anticytochrome c (Cyt c) antibody. Results demonstrate that proteolysis begin just after fishing and confirmed the degradation of actin probably by caspase 3 and release of cytochrome c by mitochondria immediately after death. These results must be completed in future works to elucidate the mechanisms of action of these proteolytic systems.