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	Provedor de dados ArchiMer (4) Autor Delbarre Ladrat, Christine (3) Verrez-bagnis, Veronique (3) Cheret, Romuald (2) Fleurence, Joel (2) Noel, Joelle (2) Taylor, Romuald (1) Mais... Palavra-chave Fish muscle (4) Proteolysis (3) Neutral calcium dependent protease (2) Bovine muscle (1) Calpain (1) Calpastatin (1) Cathepsins (1) Enzymes (1) Hautes pressions (1) High pressure (1) Indicator (1) Muscle de poisson (1) Muscular proteins (1) Post mortem (1) Postmortem (1) Postmortem aging (1) Proteases (1) Protéases (1) Protéines musculaires (1) Quality (1) Mais... Tipo do documento Text (4) Ano 2006 (1) 2005 (1) 2004 (2) País France (4) Idioma Inglês (3) Francês (1)		Ordenar por:  Relevância Autor Título Ano Registros recuperados: 4 Primeira ... 1 ... Última Effet des hautes pressions sur les indicateurs de maturation de la viande et d'altération du muscle de poisson ArchiMer Cheret, Romuald. This study deals with the influence of the high pressure process on the ageing of meat and the degradation of the fish muscle. The aim is to characterize the effect of the high pressure treatment on the protease activities responsible for degradation for the sea bass muscle (Dicentrarchus labrax L.) and bovine muscle (Biceps femoris), but also on the texture, the colour and the microstructure. The samples were pressurized between 0 and 500 MPa during 5 minutes, and were stored at 4°C. The different proteasic systems involved in the post-mortem degradation of the muscle (mainly cathepsins and calpains) were quantified after the high pressure treatment and during the post-mortem storage. The results shown that the sensitivity of the proteases depended on... Tipo: Text Palavras-chave: Enzymes; Muscular proteins; Bovine muscle; Fish muscle; Proteases; High pressure; Protéines musculaires; Enzymes; Viande bovine; Muscle de poisson; Protéases; Hautes pressions. Ano: 2005 URL: http://archimer.ifremer.fr/doc/2005/these-553.pdf 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 ArchiMer Delbarre Ladrat, Christine; Verrez-bagnis, Veronique; Noel, Joelle; Fleurence, Joel. 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)... Tipo: Text Palavras-chave: Proteolysis; Post mortem; Fish muscle; Calpain; Calpastatin; Neutral calcium dependent protease. Ano: 2004 URL: http://archimer.ifremer.fr/doc/2004/publication-1683.pdf 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 Trends in postmortem aging in fish: Understanding of proteolysis and disorganization of the myofibrillar structure ArchiMer Delbarre Ladrat, Christine; Cheret, Romuald; Taylor, Romuald; Verrez-bagnis, Veronique. Introduction : Quality attributes of fish flesh, including food safety, organoleptic features, nutritional quality and aptitude to industrial transformation, influence consumption and acceptability of fish as food. Fish sensorial changes and texture properties are closely linked to freshness. Along with ante mortem muscle biochemistry, postmortem biochemical processes are directly linked to final quality attributes. The understanding of postmortem mechanisms is a prerequisite for an accurate control of the quality of commercialized fish by the identification of objective markers or indicators. Postmortem tenderization is one of the most important quality attributes of fish muscle. Loss of freshness is due to a complex combination of biochemical, chemical... Tipo: Text Palavras-chave: Indicator; Quality; Proteolysis; Postmortem; Fish muscle. Ano: 2006 URL: http://archimer.ifremer.fr/doc/2006/publication-1810.pdf Registros recuperados: 4 Primeira ... 1 ... Última

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