Hostname: page-component-7bb8b95d7b-qxsvm Total loading time: 0 Render date: 2024-09-19T18:55:53.038Z Has data issue: false hasContentIssue false

The effect of recombinant caspase 3 on porcine myofibrillar proteins

Published online by Cambridge University Press:  23 November 2017

CM. Kemp*
Affiliation:
University of Nottingham, Nottingham, United Kingdom
T. Parr
Affiliation:
University of Nottingham, Nottingham, United Kingdom
Get access

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
Copyright
Copyright © The British Society of Animal Science 2007

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

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