Relevance of calpain and calpastatin activity for texture in super-chilled and ice-stored Atlantic salmon (Salmo salar L.) fillets.

Autor: Gaarder MØ; Norwegian University of Life Sciences (UMB), Department of Animal- and Aquacultural Sciences (IHA), Post Box 5003, 1432 Aas, Norway. Electronic address: mari.gaarder@umb.no., Bahuaud D; Norwegian University of Life Sciences (UMB), Department of Animal- and Aquacultural Sciences (IHA), Post Box 5003, 1432 Aas, Norway., Veiseth-Kent E; Nofima Mat AS, Osloveien 1, 1430 Aas, Norway., Mørkøre T; Nofima Marin AS, Osloveien 1, 1430 Aas, Norway., Thomassen MS; Norwegian University of Life Sciences (UMB), Department of Animal- and Aquacultural Sciences (IHA), Post Box 5003, 1432 Aas, Norway.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2012 May 01; Vol. 132 (1), pp. 9-17. Date of Electronic Publication: 2011 Oct 19.
DOI: 10.1016/j.foodchem.2011.09.139
Abstrakt: The aim of the present experiment was to measure the protease activities in ice-stored and super-chilled Atlantic salmon (Salmo salar) fillets, and the effect on texture. Pre-rigour fillets of Atlantic salmon were either super-chilled to a core temperature of -1.5°C or directly chilled on ice prior to 144h of ice storage. A significantly higher calpain activity was detected in the super-chilled fillets at 6h post-treatment compared to the ice-stored fillets and followed by a significant decrease below its initial level, while the calpastatin activity was significantly lower for the super-chilled fillets at all time points. The cathepsin B+L and B activities increased significantly with time post-treatment; however, no significant differences were observed at any time points between the two treatments. For the ice stored fillets, the cathepsin L activity decreased significantly from 6 to 24h post-treatment and thereafter increased significantly to 144h post-treatment. There was also a significantly lower cathepsin L activity in the super-chilled fillets at 0h post-treatment. No significant difference in breaking force was detected; however, a significant difference in maximum compression (Fmax) was detected at 24h post-treatment with lower Fmax in the super-chilled fillets. This experiment showed that super-chilling had a significant effect on the protease activities and the ATP degradation in salmon fillets. The observed difference in Fmax may be a result of these observed differences, and may indicate a softening of the super-chilled salmon muscle at 24h post-treatment.
(Copyright © 2011 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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