• Korean Journal of Food Science and Technology
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• v.28 no.3
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• pp.566-572
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• 1996

The relationship between the myofibrillar fragmentation and zeugmatin during post-mortem aging was in vestigated by indirect immunofluorescence method using antizeugmatin Antiserum as a measure of meat tenderization. The antizeugmatin antiserum was prepared using bands separated by SDS-PAGE and reacted specifically with zeugmatin, showing no cross-reactivity with the other myofibrillar proteins. By the indirect immunofluorescence method, this antiserum stained the fresh myofibrillar However, the fluorescence intensity decreased with post-mortem time and almost disappeared within 24 hr of storage, in parallel with the myofibrillar fragmentation. It was therefore concluded that zeugmatin can be conveniently used as a measure of meat tenderization during post-mortem aging by immunoflurescence method.

• Food Science of Animal Resources
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• v.18 no.4
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• pp.292-300
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• 1998

This study was undertaken to determine the influence in the Z-disk domain of titin on the tenderization of meat by the structure change of myofibrillar Z-disks during post-mortem aging. After weakening the structure of Z-disks, the Z-disk region was splitted. As the results, myofibrils were fragmented by mechanical strength. Using indirect immunofluorescence microscopy, we show that the Z-disk domain of titin was disappeared from myofibrils in this period. There phenomenon were also shown by treating myofibrils with a solution containing 0.1mM $Ca^{2+}$. We conclude that change in Z-disk domain of titin is directly effected on the tenderization of meat during post-mortem aging and these change is due to manily calcium ions.