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The effect of breed on calpastatin isoforms and longissimus shear force in pigmeat

Published online by Cambridge University Press:  20 November 2017

P.L. Sensky ,
T. Parr ,
R.G. Bardsley ,
P.J. Buttery  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
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
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. Increasing evidence suggests that calpastatin, the inhibitory component of the system, correlates negatively with tenderness in beef and pigs (Koohmaraie et al., 1995; Sensky et al., 1998). In this study, the immunoreactivity of calpastatin in three pig breeds with different meat quality traits have been measured.

Thirty-six female pigs, comprising equal numbers of Duroc (D), Large White (LW) and Duroc x Large White (50:50 DxLW) breeds were reared under identical conditions at a commercial pig unit and slaughtered at a commercial slaughterhouse on the same day by electrical stunning and severance of the carotid arteries. Carcass weight, backfat thickness, pH45 and pHu were all monitored.

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Programme
Information
Proceedings of the British Society of Animal Science , Volume 1999 , 1999 , pp. 194
Copyright
Copyright © The British Society of Animal Science 1999

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References

Arnold, M. K., Parr, T, Sensky, P. L., Bardsley, R. G. and Buttery, P. J. 1995. Differential calpastatin expression in cardiac and skeletal-muscle. Biochemical Society Transactions 23: S454.Google Scholar
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., 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