||Cheret Romuald1, Delbarre Ladrat Christine1, de Lamballerie Anton Marie2, Verrez-Bagnis Veronique1
||1 : IFREMER, F-44311 Nantes 3, France.
2 : Ecole Natl Ingn Tech Ind Agricoles & Alimentaires, UMR 6144, CNRS, F-44322 Nantes, France.
||Food Chemistry (0308-8146) (Elsevier), 2007 , Vol. 101 , N. 4 , P. 1474-1479
|WOS© Times Cited
||Meat, Fish, Protease, Cathepsin, Calpain
||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.