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Relationship between pigmeat toughness and the calpain proteolytic system

Published online by Cambridge University Press:  05 November 2021

P.L. Sensky ,
T. Parr ,
S.N. Brown ,
R.G. Bardsley ,
P.J. Buttery  and
J.D. Wood
P.L. Sensky
Affiliation:
Department of Applied Biochemistry & Food Science, University of Nottingham, School of Agriculture, Sutton, Bonington, Loughborough, Leicestershire, LE12 5RD, United Kingdom
T. Parr
Affiliation:
Department of Applied Biochemistry & Food Science, University of Nottingham, School of Agriculture, Sutton, Bonington, Loughborough, Leicestershire, LE12 5RD, United Kingdom
S.N. Brown
Affiliation:
Division of Food Animal Science, School of Veterinary Science, University of Bristol, Longford Bristol, BS18 7DY, United Kingdom
R.G. Bardsley
Affiliation:
Department of Applied Biochemistry & Food Science, University of Nottingham, School of Agriculture, Sutton, Bonington, Loughborough, Leicestershire, LE12 5RD, United Kingdom
P.J. Buttery
Affiliation:
Department of Applied Biochemistry & Food Science, University of Nottingham, School of Agriculture, Sutton, Bonington, Loughborough, Leicestershire, LE12 5RD, United Kingdom
J.D. Wood
Affiliation:
Division of Food Animal Science, School of Veterinary Science, University of Bristol, Longford Bristol, BS18 7DY, United Kingdom
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Extract

Variability in the rate of postmortem meat tenderisation occurs in the carcasses of pigs, even those of similar genotype raised under common conditions (Koohmaraie et al, 1995). Recent work has shown that administration of synthetic (β-agonists enhances muscle growth, reduces tenderisation and increases the activity of calpastatin, the natural inhibitor of the proteolytic enzymes μ-calpain and m-calpain, after slaughter (Kretchmar et al., 1990, Parr et al., 1992). Therefore, it is possible that part of the above variability may be related to levels of natural β-agonists, i.e. adrenaline. In this study the relationship between pigmeat toughness and the calpain proteolytic system has been investigated, using adrenaline infusion in an attempt to perturb the calpain system and create a wide range of meat qualities.

Type
Pig Nutrition
Information
Proceedings of the British Society of Animal Science , Volume 1996 , March 1996 , pp. 156
Copyright
Copyright © The British Society of Animal Science 1996

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References

Koohmaraie, M., Killefer, J., Bishop, M.D., Shackleford, 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 (ed. Ouali, A., Demeyer, D.I. and Smulders, F.J.M.), pp. 395–411. ECCEAMST, Utrecht.Google Scholar
Kretchmar, D.H., Hathaway, M.R., Epley, R.J. and Dayton, W.R. 1990. Alterations in postmortem degradation of myofibrillar proteins in muscle of lambs fed a β-adrenergic agonist. Journal of Animal Science 68: 1760–1772.10.2527/1990.6861760xCrossRefGoogle ScholarPubMed
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