FN Archimer Export Format PT J TI Proteolytic potential in white muscle of sea bass (Dicentrarchus labrax L.) during post mortem storage on ice: time-dependent changes in the activity of the components of the calpain system BT AF DELBARRE LADRAT, Christine VERREZ-BAGNIS, Veronique NOEL, Joelle FLEURENCE, Joel AS 1:;2:;3:;4:; FF 1:PDG-DRV-VP-BMM;2:PDG-DRV-VP-BPQ;3:PDG-DRV-VP-BMM;4:PDG-DRV-VP-BPQ; C1 IFREMER, DRV VP BPQ, F-44311 Nantes 3, France. C2 IFREMER, FRANCE SI NANTES SE PDG-DRV-VP-BMM PDG-DRV-VP-BPQ IN WOS Ifremer jusqu'en 2018 IF 1.535 TC 24 UR https://archimer.ifremer.fr/doc/2004/publication-1683.pdf LA English DT Article DE ;Proteolysis;Post mortem;Fish muscle;Calpain;Calpastatin;Neutral calcium dependent protease AB The variations in the amounts of milli-calpain and its specific inhibitor in the white muscle of sea bass (Dicentrarchus labrax) during storage at 4 degreesC for up to 7 days were determined after separation by hydrophobic chromatography on a Phenyl Sepharose vel. There was a significant decline in post-slaughter m-calpain activity with an important inter-individual variability in the rate of decrease of the total activity. In contrast with the calpastatin of mammalian post mortem muscles, calpastatin remained constant within fish muscles after death. The initial levels of protease and inhibitor activities, and their behaviour through post mortem storage. are discussed and implications for the mechanism of tenderisation of fish muscle are suggested. (C) 2003 Elsevier Ltd. All rights reserved. PY 2004 PD FEB SO Food Chemistry SN 0308-8146 PU Elsevier VL 84 IS 3 UT 000186868200017 BP 441 EP 446 DI 10.1016/S0308-8146(03)00266-8 ID 1683 ER EF