Poult. Sci.
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Poult Sci 2008. 87:2126-2132. doi:10.3382/ps.2007-00296
© 2008 Poultry Science Association
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PROCESSING, PRODUCTS, AND FOOD SAFETY

Role of Calpains in Postmortem Proteolysis in Chicken Muscle

H. L. Lee*,1, V. Santé-Lhoutellier{dagger},1, S. Vigouroux*, Y. Briand*,2 and M. Briand*,2

* Laboratoire de Génie Chimique et Biochimique, Unité Biochimie, Polytech’Clermont-Ferrand, Université Blaise Pascal, 63174 Aubière, France; and{dagger} INRA UR370, Qualité des Produits Animaux, 63122 Saint-Genès-Champanelle, France

2 Corresponding author: Yves.briand{at}univ-bpclermont.fr

Tenderness is governed by postmortem biochemical processes, particularly proteolysis. In mammals, the calpain system is generally accepted as the main system involved in postmortem proteolysis. In poultry, the 2 calpains (µ and µ/m – a form only found in bird tissue) have greater calcium sensitivity. In this study, we quantified by zymography the changes in postmortem calpain system activity. The µ/m-calpain activity remained steady, whereas the µ-calpain activity had disappeared by 6 h after postmortem, showing an activation by calcium. Changes in the electrophoretic pattern of sarcoplasmic and myofibrillar proteins are observed in the first postmortem hours concomitantly to the decrease in µ-calpain activity. The 30-kDa protein, considered as a good marker of postmortem aging in cattle, appeared from 6 h and then steadily increased. In chicken muscle, the rapid maximum tenderness reached could be explained by a greater activation of the calpain system.

Key Words: meat tenderness • chicken • postmortem proteolysis • calpain • muscle

1 The first two authors have equally contributed to this work.






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