FN Archimer Export Format
PT J
TI Effect of high pressure on the calpain-calpastatin system in fish muscle
BT 
AF CHERET, Romuald
   DELBARRE LADRAT, Christine
   VERREZ-BAGNIS, Veronique
   DE LAMBALLERIE, Marie
AS 1:2;2:2;3:2;4:1;
FF 1:PDG-DOP-DCN-STAM;2:PDG-DOP-DCB-BM-BMM;3:PDG-DOP-DCN-STAM;4:;
C1 CNRS, Ecole Natl Ingn Tech, Ind Agr & Alimentaries, UMR 6144,GEnie Procedes Enironm & Agr, F-44322 Nantes 3, France.
   IFREMER, F-44311 Nantes, France.
C2 ENITIAA, FRANCE
   IFREMER, FRANCE
SI NANTES
SE PDG-DOP-DCN-STAM
   PDG-DOP-DCB-BM-BMM
IN WOS Ifremer jusqu'en 2018
   copubli-france
   copubli-univ-france
IF 1.255
TC 10
UR https://archimer.ifremer.fr/doc/2007/publication-2786.pdf
LA English
DT Article
DE ;Postmortem denaturation;High pressure;Fish;Calpain system
AB Calpains (calcium-activated neutral proteases) of sea bass (Dicentrarchus labrax L.) muscle may participate in the degradation of muscle tissue during postmortem storage. These enzymes are regulated by calpastatin, their endogenous specific inhibitor. The objective of this study was to evaluate the changes encountered by the calpain system during the postmortem storage of fish muscle after high-pressure treatment. From 100 MPa, high-pressure treatment of purified calpains results in a loss of their activity as well as in the dissociation of the heterodimeric form. In muscle, the high-pressure processing decreases the initial activity of calpain. This loss in activity may be due to an inactivation by a change of structure. Initial calpastatin activity is not modified by the high-pressure treatment, but it decreases during the storage from the beginning for a treatment at 300 MPa after which calpastatin is stable during 2 d. Therefore, this study also suggests that high-pressure treatment could be a useful way to improve fish flesh quality.  
PY 2007
PD AUG
SO Journal of Food Science
SN 0022-1147
PU Blackwell science
VL 72
IS 6
UT 000248725200005
DI 10.1111/j.1750-3841.2007.00410.x
ID 2786
ER

EF