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In vitro proteolysis of myofibrillar and sarcoplasmic proteins of white muscle of sea bass (Dicentrarchus labrax L.): effects of cathepsins B, D and L ArchiMer
Delbarre Ladrat, Christine; Verrez-bagnis, Veronique; Noel, Joelle; Fleurence, Joel.
The purpose of this study was to obtain additional information regarding proteolysis mechanisms and disorganization of fish myofibrils resulting in a loss of flesh quality. The ability of cathepsins to degrade in vitro myofibrillar and sarcoplasmic proteins from fish muscle was investigated in order to explain their role in post mortem softening. This led to the identification of substrates of the enzymes. Cathepsins degraded myosin heavy chain and a-actinin. Tropomyosin and actin were only susceptible to the action of cathepsin L. Troponin T (assumed 32 kDa component) was resistant only to the action of cathepsin D. Desmin was degraded by cathepsins B and L. Slight changes of some other myofibrillar or cytosolic proteins were also observed (creatine...
Tipo: Text Palavras-chave: Post mortem degradation; Fish muscle proteins; Cathepsins; In vitro proteolysis.
Ano: 2003 URL: http://archimer.ifremer.fr/doc/2003/publication-1684.pdf
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Proteins and proteolytic activity changes during refrigerated storage in sea bass (Dicentrarchus labrax L.) muscle after high-pressure treatment ArchiMer
Cheret, Romuald; Hernandez Andres, Aránzazu; Delbarre Ladrat, Christine; De Lamballerie, Marie; Verrez-bagnis, Veronique.
Contrary to other preservation methods like thermal treatments, high pressure can destroy microorganisms without affecting the nutritional quality, color, or food texture. The firm texture of fish flesh is an important quality parameter. During the refrigerated storage, the tissue becomes softer and the muscle is deteriorated by different proteases. The aim of this study was to study the modification of the fish muscle proteins after high-pressure treatment during the refrigerated storage and to evaluate the effect of high-pressure treatment level on the post-mortem protein changes and enzyme activities. The calpain activity decreased with the high-pressure treatment and evolved differently during the refrigerated storage, depending on the level of...
Tipo: Text Palavras-chave: Cathepsins; Calpains; Sarcoplasmic proteins; Myofibrillar proteins; Post mortem denaturation; High pressure; Fish.
Ano: 2006 URL: http://archimer.ifremer.fr/doc/2006/publication-1708.pdf
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Relative contribution of calpain and cathepsins to protein degradation in muscle of sea bass (Dicentrarchus labrax L.) ArchiMer
Delbarre Ladrat, Christine; Verrez-bagnis, Veronique; Noel, Joelle; Fleurence, Joel.
The effects of a milli(m)-calpain isolated from the white muscle of sea bass (Dicentrarchus labrax L) and commercial cathepsins B, D and L, used in combination on the myofibrillar and sarcoplasmic proteins were examined. Protein digestion was first performed by the endogenous m-calpain, (luring 2 h before the addition of a mixture of cathepsins B, D and L and a further incubation up to 22 h. Calpain degraded a 27 kDa sarcoplasmic component as well as myosin heavy chain, a-actinin, desmin and a 32 kDa component from the myofibrillar fraction. A 97 kDa component and the assumed creatine kinase-aldolase doublet were degraded during the incubation of sarcoplasmic proteins with the cathepsin mixture while, among the myofibrillar proteins, myosin, actin,...
Tipo: Text Palavras-chave: Postmortem aging; Fish muscle; Proteolysis; Cathepsins; Neutral calcium dependent protease.
Ano: 2004 URL: http://archimer.ifremer.fr/doc/2004/publication-1682.pdf
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