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Abstract
The purpose of this study was to increase the knowledge on the relationship between proteolysis of myofibrillar proteins and the water-holding of meat. Myofibrils isolated from porcine longissimus thoracis et lumborum muscle were used as a model system. Myofibrils were incubated with either calpain-2, the proteasome or a lysosomal extract at 25°C for 2h. All three proteolytic systems improved the relative water-holding and generally there was a larger effect with increasing amount of enzymes in the incubation. The improved water-holding occurred in parallel to degradation of myofibrillar proteins. Desmin was degraded by calpain-2 as well as by lysosomal enzymes and α-actinin was released by the proteasome. We here propose a model in which degradation of proteins in and around the Z-disk allows overall swelling of the filament lattice and more specifically in the I-band area. In conclusion, proteolytic degradation of myofibrillar proteins by calpain-2, the proteasome or lysosomal enzymes improves the water-holding of myofibrils.
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