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Post-mortem softening of fish tissue often results in low yield and decreased product quality. In this study, proteolytic profiles of trout stored 5 days oil ice were obtained by SDS-PAGE. The link between protein hand intensities and firmness of trout fillets was examined through a correlation Study. In parallel, trout extracts were incubated with cathepsin B, cathepsin L and cathepsin D, alone or in combination, in order to evaluate the effect of each cathepsin on the texture-related proteins. Proteins from both myofibrillar (alpha-actinin, actin, MLC1, MLC2. and N-terminal 70 kDa MHC fragment) and sarcoplastic (glycogen phosphorylase, creatine kinase, and TPI) fractions correlated closely with firmness. Cathepsins D, B and L affected, respectively, 10, 9 and 4 out of the 17 protein bands correlating with firmness, and most changes induced by cathepsin D were unfavourable to firmness. This implies that cathepsin D is likely to be involved in textural change of trout, due to breakdown of the muscle structure.
Original languageEnglish
JournalFood Chemistry
Issue number4
Pages (from-to)889-896
StatePublished - 2009
CitationsWeb of Science® Times Cited: 66


  • Softening, Trout, Fish, Oncorhynchus mykiss, Cathepsins, SDS-PAGE, Texture
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ID: 4020368