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The effect of recombinant caspase 3 on porcine myofibrillar proteins

Published online by Cambridge University Press:  23 November 2017

CM. Kemp  and
T. Parr
CM. Kemp*
Affiliation:
University of Nottingham, Nottingham, United Kingdom
T. Parr
Affiliation:
University of Nottingham, Nottingham, United Kingdom
*
Email:sbxcmk@nottingham.ac.uk
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Extract

Meat tenderisation results from the weakening of the myofibrillar structures and has been attributed to endogenous proteolytic enzymes. It has been proposed that tenderization is a mulitenzymatic system and the process of slaughter and exsanguination would engage muscle cells in a form of cell death (Ouali et al., 2006). Caspases are primarily associated with apoptosis and once activated they target and cleave a number of substrates including components of the Z-disk and costameres. Recent studies have shown that caspases are active in skeletal muscle during the postmortem conditioning period and our preliminary data indicates that there is a relationship between caspase activity and shear force (Kemp et al., 2006). The aim of this study was to investigate whether recombinant caspase 3 was capable of porcine degrading myofibrillar proteins in vitro.

Type
Theatre Presentations
Information
Proceedings of the British Society of Animal Science , Volume 2007 , April 2007 , pp. 112
Copyright
Copyright © The British Society of Animal Science 2007

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References

Goll, et al., 1974. Separation of subcellular organelles by differential and density gradient centrifugation. Proc Ann Recip Meat Conf 27: 250–267.Google Scholar
Kemp, et al., 2006. Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle. Journal of Animal Science 84: 2841–2846.Google Scholar
Ouali, et al., 2006. Revisiting the conversion of muscle into meat and the underlying mechanisms. Meat Science 74: 44–58.Google Scholar