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Differences in the calpain enzyme system in tough and tender samples of porcine longissimus dorsi

Published online by Cambridge University Press:  05 November 2021

P.L. Sensky ,
T. Parr ,
G.P. Scothern ,
A. Perry ,
R.G. Bardsley ,
P.J. Buttery ,
J.D. Wood  and
C. C. Warkup
P.L. Sensky
Affiliation:
Nutritional Biochemistry, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LEI 2 5RD, UK
T. Parr
Affiliation:
Nutritional Biochemistry, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LEI 2 5RD, UK
G.P. Scothern
Affiliation:
Nutritional Biochemistry, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LEI 2 5RD, UK
A. Perry
Affiliation:
Div of Food Animal Science, School of Veterinary Science, University of Bristol, Langford, Bristol, BS18 7DY, UK
R.G. Bardsley
Affiliation:
Nutritional Biochemistry, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LEI 2 5RD, UK
P.J. Buttery
Affiliation:
Nutritional Biochemistry, University of Nottingham, Sutton Bonington Campus, Loughborough, Leicestershire, LEI 2 5RD, UK
J.D. Wood
Affiliation:
Div of Food Animal Science, School of Veterinary Science, University of Bristol, Langford, Bristol, 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). Recent experimental work in pig muscle has shown that calpastatin can be increased by protocols which mimic stress and that these increases relate to changes in tenderness (Sensky et al., 1996; Sensky et al., 1997). In this study differences in the calpain system in randomly selected pigs slaughtered at a commercial slaughterhouse were investigated, with respect to the degree to which the meat tenderised.

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Proceedings of the British Society of Animal Science , Volume 1998 , 1998 , pp. 16
Copyright
Copyright © The British Society of Animal Science 1998

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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: 380–387.10.2527/1996.742380xCrossRefGoogle ScholarPubMed
Sensky, P. L., Parr, T., Bardsley, R. G. and Buttery, P. J. 1997. The effect of varying the degrees of (β-receptor stimulation on the activity of the calpain - calpastatin system at slaughter in porcine longissimus dorsi. Proceedings of the British Society of Animal Science 1: 104.Google Scholar