FN Archimer Export Format
PT J
TI Calpain and cathepsin activities in post mortem fish and meat muscles
BT 
AF CHERET, Romuald
   DELBARRE LADRAT, Christine
   DE LAMBALLERIE ANTON, Marie
   VERREZ-BAGNIS, Veronique
AS 1:1;2:1;3:2;4:1;
FF 1:PDG-DOP-DCN-STAM;2:PDG-DOP-DCB-BM-BMM;3:;4:PDG-DOP-DCN-STAM;
C1 IFREMER, F-44311 Nantes 3, France.
   Ecole Natl Ingn Tech Ind Agricoles & Alimentaires, UMR 6144, CNRS, F-44322 Nantes, France.
C2 IFREMER, FRANCE
   ENITIAA, FRANCE
SI NANTES
SE PDG-DOP-DCN-STAM
   PDG-DOP-DCB-BM-BMM
IN WOS Ifremer jusqu'en 2018
   copubli-france
IF 3.052
TC 126
UR https://archimer.ifremer.fr/doc/2007/publication-3646.pdf
LA English
DT Article
DE ;Meat;Fish;Protease;Cathepsin;Calpain
AB Post mortem tenderization is one of the most unfavourable quality changes in fish muscle and this contrasts with muscle of mammalian meats. The tenderization can be partly attributed to the acid lysosomal cathepsins and cytosolic neutral calcium-activated calpains. In this study, these proteases from fish and bovine muscles were quantified and compared. The cathepsin B and L activities were in more important amounts in sea bass white muscle than in bovine muscle. On the other hand, cathepsin D activity was 1.4 times higher in meat that in fish muscle, while cathepsin H was negligible in both muscles. Calpain activities were similar in both types of muscle. Moreover, calpastatin (calpain endogenous inhibitor) level is 3.9 times higher in sea bass white muscle. These differential activities are considered in relation to their probable involvement in post mortem degradation of muscle. (c) 2006 Elsevier Ltd. All rights reserved.
PY 2007
SO Food Chemistry
SN 0308-8146
PU Elsevier
VL 101
IS 4
UT 000241764100020
BP 1474
EP 1479
DI 10.1016/j.foodchem.2006.04.023
ID 3646
ER

EF