Trends in postmortem aging in fish: understanding of proteolysis and disorganization of the myofibrillar structure.
Postmortem tenderization is caused by enzymatic degradation of key structural proteins in myofibrils as well as in extracellular matrix, and of proteins involved in intermyofibrillar linkages and linkages between myofibrils and the sarcolemma. The function of these proteins is to maintain the structural integrity of myofibrils. Current data indicate that calpains and cathepsins may be responsible for degradation of these proteins. Other phenomena occurring in cells postmortem (pH drop, sarcoplasmic Ca2+ increase, osmotic pressure rise, oxidative processes) may act in synergy with proteases. Our understanding of the underlying mechanisms of muscle degradation should be improved for an accurate evaluation of the postmortem muscle changes and consequently of the fish quality.
Delbarre-Ladrat
Christine
C
IFREMER, DRV-VP, Rue de l'Ile d'Yeu, BP21105, Nantes Cedex 3, 44311, France.
Chéret
Romuald
R
Taylor
Richard
R
Verrez-Bagnis
Véronique
V
D000818:Animals; D002118:Calcium / Q000032:analysis; D003080:Cold Temperature; D005399:Fishes; D005519:Food Preservation; D006863:Hydrogen-Ion Concentration; D008460:Meat; D009124:Muscle Proteins / Q000378:metabolism*; D009132:Muscles / Q000737:chemistry / Q000378:metabolism / Q000648:ultrastructure; D009210:Myofibrils / Q000648:ultrastructure*; D010447:Peptide Hydrolases / Q000378:metabolism*; D011180:Postmortem Changes; D011786:Quality Control; D012519:Sarcoplasmic Reticulum / Q000737:chemistry
D009124:Muscle Proteins; D010447:Peptide Hydrolases; D002118:Calcium