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Differences in meat quality and the calpain enzyme system in pigs supplied by 4 different commercial production units

Published online by Cambridge University Press:  20 November 2017

P.L. Sensky ,
T. Parr ,
G.P. Scothern ,
R.G. Bardsley ,
P.J. Buttery ,
J.D. Wood  and
C. C. Warkup
P.L. Sensky
Affiliation:
Division of Nutritional Biochemistry, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LE12 5RD, UK
T. Parr
Affiliation:
Division of Nutritional Biochemistry, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LE12 5RD, UK
G.P. Scothern
Affiliation:
Division of Nutritional Biochemistry, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LE12 5RD, UK
R.G. Bardsley
Affiliation:
Division of Nutritional Biochemistry, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LE12 5RD, UK
P.J. Buttery
Affiliation:
Division of Nutritional Biochemistry, School of Biological Sciences, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LE12 5RD, UK
J.D. Wood
Affiliation:
Division of Food Animal Science, School of Veterinary Science, University of Bristol, Langford, BS18 7DY, UK
C. C. Warkup
Affiliation:
Meat & Livestock Commission, PO Box 44, Winterhill House, Snowdon Drive, Milton Keynes, MK6 1AX, UK
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Extract

The calpain enzyme system plays an important role in the proteolytic events leading to the conversion of muscle to meat in livestock species. Evidence in beef has shown that the levels of calpastatin, the inhibitory component of the system, measured 24 h after slaughter can be used to predict the degree of tenderisation achieved at the end of the normal conditioning period (Koohmaraie et al., 1995). In pigs there is now evidence that calpastatin levels measured within the first hour of slaughter correlate with tenderness measured after conditioning (Sensky et al., 1998). In this study we report differences in the calpain system in pigs supplied by four different commercial production units who supplied pigs with predominantly tough (A and B below) or tender meat (C and D below) in a previous study (Sensky et al., 1998).

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Proceedings of the British Society of Animal Science , Volume 1999 , 1999 , pp. 193
Copyright
Copyright © The British Society of Animal Science 1999

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References

Koohmaraie, M., Killefer, J., Bishop, M. D., Shackelford, S. D., Wheeler, T. L. and Arbona, J. R. 1995. Calpastatin-based methods for predicting meat tenderness. In Expression of tissue proteinases and regulation of protein degradation as related to meat quality (eds. Ouali, A., Demeyer, D..I. and Smulders, F. J. M.), pp 395–411, ECCEAMST, Utrecht, The Netherlands.Google Scholar
Sensky, P. L., Parr, T., Bardsley, R. G. and Buttery, P. J. 1996. Relationship between plasma epinephrine concentration and the activity of the calpain enzyme system in porcine longissimus muscle. Journal of Animal Science 74: 380–387.Google Scholar
Sensky, P. L., Parr, T., Scothern, G. P., Perry, A., Bardsley, R. G., Buttery, P. J., Wood, J. D. and Warkup, C. C. 1998. Differences in the calpain enzyme system in tough and tender samples of porcine longissimus dorsi. Proceedings of the British Society of Animal Science (1998), 16.Google Scholar