**Acknowledgements**

is related to increased level of pyridinoline. The level of *pyridinoline* in younger livestock is

Efforts to improve the quality of local livestock, in this case cattle and buffalo, have been conducted in various methods, both physical (e.g. aging, cold/frozen storage) and chemically (e.g. using protease enzymes). Refrigerator storage causes the split muscle fibers. Increase in period of freezer storage can result in separation of muscle fibers as well as structural damage to muscle shape caused by ice crystal formation. The fourth day of storing meat inside freezer (−10 ± 1°C) shows mild damage. It is the beginning of muscle fibers cracking. On the 60th day, the structural damage of muscle fibers becomes more severe with ice crystals pressing and tearing cells. On the 75th day, the damage of muscle fibers becomes greater than the 60th day

According to [33] the diameter of muscle fibers of buffalo meat is not influenced by sex difference, but influenced by age difference during different storage periods. The data of research results conducted by Rao et al. [33]. The decrease in muscle fiber diameter occurs gradually from 0 to 48 hours of storage period inside freezer (−15 ± 1°C), so as to increase the tenderness of meat during the period of aging. Freezing also affects the structure of muscle fiber diameter due to histological changes in muscle tissue during frozen storage. Muscle fibers of female buffalo that were stored inside freezer at a temperature of −12°C for 35 days had less structural damage when compared to muscles stored for 79 days. Increased storage time of meat inside freezer can increase the damage of muscle fibers, so that connective tissue and the distance between muscle fibers become more easily decomposed due to the process stretch-

Another treatment to improve tenderness in meat is to use enzymes, such as papain or bromelain enzymes. Related to [34], the tissue structure of beef samples not treated with bromelain enzyme is seen to have intact-shaped structures of myofibril and sarcolemma. Meanwhile, the myofibrils structure of meat samples soaked with bromelin enzyme for 1 and 4 hours looks incomplete, or in other words, has endured degradation. Descriptively, the alterations that occur in the myofibril structure indicate that giving treatment of bromelin enzyme can

Summarizing the various studies of meat quality in Indonesia, it is illustrated that the quality of local meat for some criteria such as pH, water holding capacity, cooking loss, meat color, fat color, nutrient content, basically does not differ between local beef cattle and imported beef. The difference is seen in the fatty, degree of marbling and tenderness that will affect the juiceness of meat. But if it is connected with how to process the majority of Indonesian cuisine, which is wet cooking, like *rendang* and *semur,* meat quality already meet the requirements of consumer's preference. For cooking menu that uses dry cooking like barbeque it can be treated like aging with long period or using tenderizing like bromelin or papain enzyme.

lower, making collagen labile against heat.

74 Bovine Science - A Key to Sustainable Development

with greater intercellular distance [32].

improve the tenderness of meat.

**5. Conclusion**

ing. Such damage is most likely to result in myofibril alterations.

The authors thank those who participated in the various projects that led to these results, all those who provided funding support for this research and also thanks to the Open Access Publishing Fee.
