Journal article
Contribution of cathepsins B, L and D to muscle protein profiles correlated with texture in rainbow trout (Oncorhynchus mykiss)
National Institute of Aquatic Resources, Technical University of Denmark1
Section for Aquatic Process and Product Technology, National Institute of Aquatic Resources, Technical University of Denmark2
Section for Aquatic Protein Biochemistry, National Institute of Aquatic Resources, Technical University of Denmark3
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.
Language: | English |
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Year: | 2009 |
Pages: | 889-896 |
ISSN: | 18737072 and 03088146 |
Types: | Journal article |
DOI: | 10.1016/j.foodchem.2008.08.012 |
ORCIDs: | Hyldig, Grethe and Jessen, Flemming |