**4. Relationship of muscle microstructure and meat quality**

Carcass is composed of meat, fat, adipose tissue, bone, cartilage, connective tissue and tendon. Muscle turns into flesh after cutting process because its physiological function stops. Muscle is the main component of meat constituents. All muscles have the same basic structure, consisting of muscle cells or fibers that are intertwined together in bundles and form larger groups. Collagen is the most important component related to meat texture. Collagen of old animals grow larger and they have more cross-linked connective tissues, causing the meat to become tough and less tender [12].

Muscle is composed of many bundles of muscle fibers commonly called fasciculi. Fasciculi consist of muscle fibers, whereas muscle fibers consist of many filaments called myofilaments. Connective tissue is composed of an epimysium located around the muscle, perimysium containing blood vessels, and relatively larger nerves located between fasciculi and endomysium containing amorphous component, non-fibrous tissue with fine woven binders surrounding muscle cells or muscle fibers [29].

(1) pH

pH range of 5.5–5.8.

72 Bovine Science - A Key to Sustainable Development

tenderness value.

beef.

process.

(2) Water holding capacity

of meat and its processed products [28].

to become tough and less tender [12].

The pH value of meat may indicate a deviation of the quality of the meat, since the pH value of the meat is related to the color, tenderness, taste, water holding capacity and the shelf life of the meat. The isoelectric pH points of the meat proteins are between 5.0 and 5.1 with a normal

If pH > 5.8, then there are two possibilities of normal or DFD (dark, firm, dry). The second pH test is done at 24 hours after cutting, if pH > 6.2 means the meat is DFD, whereas if the pH is about 5.5 means the meat is normal [25]. Ref. [26] reported that meat with high pHu has a low

Ref. [27] compares the physical characteristics of ongole crossbreed beef at different body weights. The results showed that body weight has a very low correlation with pH value of meat, that is, 0.192 in *Longissimus dorsi* (average pH value of 5.59) and 0.000 on *bicep femoris* (average pH value of 5.57). Ref. [18] reported that pH bali beef is no different from wagyu

The pH value of meat is generally more influenced by the factor at the time of the slaughter

Water is the most important part in meat composition. Meat contains about 75% water. Muscle protein (myofibrillar) plays an important role in water binding, which determines the quality

Water holding capacity is the ability of the meat (especially myofibrillary proteins) to bind water or water added during external influences (e.g. meat cutting, heating, grinding and pressing). Ref. [29] found that water holding capacity of buffalo meat is not affected by age, but it is affected by sex during the storage period of 0, 24, and 48 hours. Result of analysis show water holding capacity of buffalo meat is not influenced by age and sex [20]. There is no difference in water holding capacity of bali beef and wagyu beef [18]. Ref. [16] also reported that there was no difference in binding power of brahman cross beef, bali cattle, ongole cross-

Carcass is composed of meat, fat, adipose tissue, bone, cartilage, connective tissue and tendon. Muscle turns into flesh after cutting process because its physiological function stops. Muscle is the main component of meat constituents. All muscles have the same basic structure, consisting of muscle cells or fibers that are intertwined together in bundles and form larger groups. Collagen is the most important component related to meat texture. Collagen of old animals grow larger and they have more cross-linked connective tissues, causing the meat

breed cattle and simmental × ongole crossbreed cattle on *Semitendinosus* muscles.

**4. Relationship of muscle microstructure and meat quality**

Muscle fiber is composed of myofibrils containing many myofilaments. Myofibril is an organelle of cylindrical muscle fiber with a diameter of approximately 1–2 μm. A muscle fiber that has a diameter of 50 μm contains 1000–2000 myofibrils. Myofibril consists of segments called sarcomere. The length of sarcomere at rest is approximately 2.5 μm. Sarcomeres have two forms of myofilaments, namely thick filaments (myosin) with a diameter of 10–12 μm and thin filaments (actin) with a diameter of approximately 5–7 μm. The lighter portion of myofibril is called I band, while the thicker part is called A band. I band and A band are arranged in longitudinal parallel within muscle fibers, which causes the cross section of skeletal muscle fibers to appear transverse [12, 30]. Increasing number of muscle cells during prenatal growth can be indicated from the addition of the amount of muscle per fasciculus. Increased muscle size during postnatal growth can be indicated from the addition of muscle cross-sectional area.

Observations on histology of muscle not only result in obtaining images or descriptions of muscle tissues (existence of muscle fibers, connective tissues and intramuscular fat tissues), but also in discovering the size of the tissues (such as diameter of muscle fiber, diameter of fasciculus, and thickness of connective tissue). Nuraini et al. [20] state that the average diameter of muscle fibers of buffalo meat, which is 38.32 ± 1.9 μm, increases under 1 year of age (I.0 ) and reaches the highest point at the age of 3 years (I3 ) with 54.95 ± 8.6 μm (P < 0.05). This is in line with the decline of buffalo meat tenderness level, which is 6.53 ± 2.89 kg cm−2 (under 1 year of age) to 9.63 ± 1.45 kg cm−2 (3 years of age). Ref. [29] mentions that many factors affect the diameter of muscle fibers, such as the level of nutrition, the rate of postnatal body weight development, the level of muscle performance and the age of livestock.

Ref. [31] describe the histology and histomorphometry of bali beef and wagyu beef. It appears that the muscle cell diameter (75.00 ± 1.72 μm) and fat cell (195.20 ± 2.17 μm) of wagyu cattle were larger than the muscle cell diameter (45.00 ± 1.89 μm) and fat cell (90.10 ± 2.69 μm) of bali cattle. Foreign tourists in Bali prefer wagyu beef than bali beef. This is partly because wagyu beef is more tender. Histologic observation results in wagyu cattle muscle illustrates that the connective tissue of wagyu beef is very little so that the meat is more tender.

Samples of muscle histology can also be used to discover the thickness of connective tissue that can be an indicator of the level of meat tenderness. Thickness of connective tissue of female buffalo at I0 age (15.59 ± 2.00 μm) is smaller than at I<sup>2</sup> age (16.29 ± 5.96 μm) and at I3 age (18.2 ± 5.81 μm) [20]. This condition illustrates that there is an increase in connective tissue as the livestock ages. It is related to the level of collagen in animal tissues. Collagen is the principal protein component of connective tissue and has a major influence on toughness of meat [30]. Collagen of old livestock is more stable against the influence of temperature change, which results in formation of thicker and larger connective tissue. An increase in livestock age is related to increased level of pyridinoline. The level of *pyridinoline* in younger livestock is lower, making collagen labile against heat.

Some of the circumstances causing the low quality of meat in Indonesia are most of the breeders employing cattle and buffalo, low quality of feeding, older slaughter age and handling before and at the time of slaughtering process that does not pay attention to aspects of animal welfare. The meat industry in Indonesia is only able to form two market segments namely the local market for middle to lower class consumers and special markets for hotel, restaurant, catering and franchise consumers. Efforts to improve livestock management, selection and crosses with *Bos taurus* breeds are expected to improve local livestock performance in

Meat Quality of Indonesian Local Cattle and Buffalo http://dx.doi.org/10.5772/intechopen.79904 75

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

The authors declare that there is no conflict of interest regarding the publication of this paper.

1 Department of Animal Production and Technology, Faculty of Animal Science, Bogor Agricultural University, Jl. Agathis Bogor Agricultural University, Darmaga, Bogor,

3 Assessment Institute for Agricultural Technology, Ministry of Agricultural, Tidore

[1] Kusuma SB, Ngadiyono N, Sumadi S. The estimation of population dynamic and reproduction performance of Ongole crossbred cattle in Kebumen regency, central java province. Bulletin of Animal Science. 2017;**41**(3):230-242. DOI: 10.21059/buletinpeternak.

Henny Nuraini1,2\*, Edit Lesa Aditia1,2 and Bram Brahmantiyo3

2 Halal Science Center, Bogor Agricultural University, Indonesia

\*Address all correspondence to: hennynuraini@ymail.com

Kepulauan City, North Malucas, Indonesia

Indonesia.

Publishing Fee.

**Acknowledgements**

**Conflict of interest**

**Author details**

West Java, Indonesia

**References**

v41i3.13618

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 with greater intercellular distance [32].

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

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 improve the tenderness of meat.
