Artículos de revistas
Protease activity and the ultrastructure of broiler chicken PSE (pale, soft, exudative) meat
Fecha
2010Registro en:
FOOD CHEMISTRY, v.119, n.3, p.1201-1204, 2010
0308-8146
10.1016/j.foodchem.2009.08.034
Autor
WILHELM, Allan E.
MAGANHINI, Magali B.
HERNANDEZ-BLAZQUEZ, Francisco J.
IDA, Elza I.
SHIMOKOMAKI, Massami
Institución
Resumen
The biological cause of broiler PSE meat seems to be an excessive release of Ca(2+), promoted by a genetic mutation of ryanodine receptors located in the sarcoplasmic reticulum of skeletal muscle cells. Excessive Ca(2+), associated with protein denaturation in meat, enhances protease activity and influences the functional properties of PSE meat. Twenty-four-hour post-mortem Pectoralis major m. samples exhibited lower values for pH, water-holding capacity, and shear force than did control samples, in contrast to colour (L*) and cooking loss values. Protease activity, measured as myofibril fragmentation index, presented higher values in PSE meat than in control samples. Ultrastructural examination revealed shrinking and depolymerisation of myofilaments and Z-lines disorganisation within the sarcomere in PSE meat. Intense calpain activity was also observed, indicating that the process may initiate at the filaments, because of protein denaturation, and spread through Z-lines, resulting in the collapse of the sarcomere structure. (C) 2009 Elsevier Ltd. All rights reserved.