| The process of myofibrillar protein degradation, in muscle and in post mortem meat tenderization, is still poorly understood. Much research has been carried out investigating the roles of endogenous muscle proteinases, the cathepsins and the calpains. However, it does not appear that proteolytic degradation of myofibrillar proteins alone is the key to understanding protein turnover in muscle and the postmortem meat tenderization process.;Actin binding proteins, with the ability to bind and sever F-actin filaments have become the focus of many investigators in the recent past. In particular, the protein gelsolin, has been well characterized and studied. Research has shown that gelsolin is present in blood and muscle of many animals including pigs, chicken and cattle. This research aims to confirm its presence in bovine skeletal muscle and to investigate gelsolin's role in disrupting the integrity of the myofibril, during postmortem aging of meat. This project also examined co-operativity between the action of gelsolin and endogenous enzymes, which could have implications for protein turnover in living muscle.;This study also addressed the proteolytic susceptibility of gelsolin. The N-terminal fragment of gelsolin retains its severing ability, after cleavage from the C-terminal end of the protein. Therefore, production of this peptide by an endogenous muscle proteinase may impact upon gelsolin's role in postmortem myofibrillar turnover. |
