Role of calpains in postmortem proteolysis in chicken muscle.
Tenderness is governed by postmortem biochemical processes, particularly proteolysis. In mammals, the calpain system is generally accepted as the main system involved in postmortem proteolysis. In poultry, the 2 calpains (mu and mu/m--a form only found in bird tissue) have greater calcium sensitivity. In this study, we quantified by zymography the changes in postmortem calpain system activity. The mu/m-calpain activity remained steady, whereas the mu-calpain activity had disappeared by 6 h after postmortem, showing an activation by calcium. Changes in the electrophoretic pattern of sarcoplasmic and myofibrillar proteins are observed in the first postmortem hours concomitantly to the decrease in mu-calpain activity. The 30-kDa protein, considered as a good marker of postmortem aging in cattle, appeared from 6 h and then steadily increased. In chicken muscle, the rapid maximum tenderness reached could be explained by a greater activation of the calpain system.
Lee
H L
HL
Laboratoire de Génie Chimique et Biochimique, Unité Biochimie, Polytech'Clermont-Ferrand, Université Blaise Pascal, 63174 Aubière, France.
Santé-Lhoutellier
V
V
Vigouroux
S
S
Briand
Y
Y
Briand
M
M
D000003:Abattoirs; D000818:Animals; D001835:Body Weight; D002154:Calpain / Q000502:physiology*; D002364:Caseins / Q000378:metabolism; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D009124:Muscle Proteins / Q000302:isolation & purification / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000502:physiology*; D011180:Postmortem Changes; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D013997:Time Factors
D002364:Caseins; D009124:Muscle Proteins; D002154:Calpain; D046988:Proteasome Endopeptidase Complex