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J Sci Food Agric ; 92(13): 2727-40, 2012 Oct.
Article in English | MEDLINE | ID: mdl-22522408

ABSTRACT

BACKGROUND: The objective of this work was to study the post-mortem evolution of potential biomarkers (µ-calpain activity and proteolytic profile) of meat tenderisation in bovine longissimus dorsi (LD) muscle from several biotypes coming from two beef breeds ('Asturiana de los Valles' and 'Asturiana de la Montaña') and showing different levels of muscular hypertrophy (mh/mh, mh/+, + /+). RESULTS: LD samples were taken at 2, 12, 24 and 48 h and 3, 7, 14 and 21 days post-mortem. The presence of muscular hypertrophy produced a faster rate of pH decline, faster exhaustion of µ-calpain activity and earlier occurrence of proteolytic changes. Changes in the electrophoretic pattern of some peptides from sarcoplasmic (glyceraldehyde-3-phosphate dehydrogenase) and myofibrillar (troponin T and troponin I) muscle extracts within the first 24 h significantly correlated with meat toughness and allowed accurate discrimination of meat products into two groups: (1) fast tenderising meat, coming from mh-biotypes, and (2) late tenderising meat, from normal (+/+) biotypes. CONCLUSION: Early monitoring (within 24 h after slaughter) of selected biomarkers in LD muscle allowed accurate prediction of ultimate meat toughness and could be used in the meat industry as a tool for early classification of beef into fast and late tenderising meat.


Subject(s)
Calpain/metabolism , Meat/analysis , Muscle, Skeletal/metabolism , Postmortem Changes , Animals , Biomarkers , Cattle , Glyceraldehyde-3-Phosphate Dehydrogenases/metabolism , Hydrogen-Ion Concentration , Hypertrophy , Meat/classification , Muscle, Skeletal/enzymology , Myofibrils/metabolism , Peptides/metabolism , Proteolysis , Sarcoplasmic Reticulum/metabolism , Species Specificity , Troponin T/metabolism
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