Meat quality
Meat quality attributes for goat LD muscle as influenced by protein level are presented in Table 2. The results revealed that pH1h was higher in 18% protein group than in 15, 9 and 12% groups, respectively (P<0.05). However, the ultimate pH (pH24h) in LD did not significantly differ among the treatments (P>0.05). In addition, it was observed that the redness (
a*) of muscle from the 15 and 18% protein groups was higher than for the 12% dietary protein group (P<0.05). However, the lightness (
L*) and yellowness (
b*) of meat did not significantly differ (P>0.05). The dietary protein level at 12% gave a higher thawing loss than the other treatments (P<0.05). However, meat water loss during chilling (drip loss) and cooking loss was not significantly different (P>0.05).
Warner-Bratzler shear force (WBSF) and texture profile analysis (TPA)
Effects of protein level in TMR on WBSF and TPA of native goat meat are shown in Table 3. The WBSF results showed that the high protein group (18%) had the greatest shear force, larger than in the 9 and 12% dietary protein groups (P<0.05), but not significantly different from the 15% dietary protein group. In TPA hardness, cohesiveness, adhesiveness, springiness and chewiness of meat did not significantly differ by treatment (P>0.05). However, a high protein level in the feed tended to increase the hardness of meat (P<0.1), which was consistent with the WBSF.
Collagen contents and chemical compositions of meat
Collagen contents and chemical compositions of LD of Thai native goats are shown in Table 4. The results indicated that the insoluble collagen and the total collagen content in goat meat had statistically significant differences (P<0.05). The 12% protein diet gave the highest insoluble collagen content and total collagen content. However, the soluble collagen did not significantly differ by treatment (P>0.05). In chemical compositions, the fat content of goat meat was highest in the 9% group, followed by the 12, 15 and 18% dietary protein groups (P<0.05). However, the moisture and the protein contents had no significant differences (P>0.05).
Generally, the meat pH is a measurement of the post mortem glycolysis and it depends on many important factors, for example on pre-slaughter stress, fasting, carcass temperature, as well as on factors intrinsic to the animal itself, such as species, age,
etc. (McGeehin et al., 2001). The pH of meat decreases slowly from the initial about 7.0 and reaches 5.6-5.7 in 6-8 hours post mortem, then drops to the final pH between 5.3-5.7 within 24 hours post mortem.
Pratiwi et al., (2007) indicated that muscle pH in general declined during the immediate post mortem period and the acceptable range for pH at 24 h for goat meat is within 5.6-5.8. In this study, the muscle pH at 24 h was within the acceptable range for goat meat in all cases. Rate and extent of pH decline are known to affect the development of meat quality attributes, such as color and tenderness
(Simela et al., 2004). In this study, muscle pH corresponded to reported values for muscles of various goat breeds
(Dhanda et al., 2003; Kadim et al., 2003). Simela et al., (2004) reported a tendency towards the dark firm and dry (DFD) condition for chevon with an ultimate pH higher than 6. In bovine, muscles with a pH higher than 5.8 are usually classified as DFD (
Tarrant and Sherington, 1980). Moreover, the pH is an important measure of meat quality and
Warriss (2010) explains that the ultimate pH (pH24h) is related to the drip loss of meat. In the present study, the pH24h showed no differences between treatments, so that the %drip loss of meat might not differ as well. Besides water holding capacity of meat, pH is also strongly related to the color of the meat. In other words, a higher pH tends to match a darker meat color (
Fletcher, 1995).
In this study, the WBSF results are consistent with
Tang et al., (2010), which reported that animal diet with a low protein level reduced WBSF in pork. However, the mechanism for increasing the tenderness of meat in the low-protein diet is unknown, but it may be by the accumulation of intramuscular fat in animal muscles during a low-protein diet.
Wang et al., (2015) investigated the effects of two dietary protein levels (15% and 17%) and three dietary energy levels (11.72, 12.55 and 13.39 MJ/Kg DM) on meat quality of the Hainan black goat and found that the tenderness of the
Longissimus dorsi and
Semimembranosus decreased when the protein level of the feed was higher, while tenderness tended to increase when the energy level of feed was higher.
Collagen is a component of the muscle connective tissue and increases meat toughness. In other words, collagen is considered to be “background toughness” of meat and especially soluble collagen is associated with toughness of the meat (
Moon, 2006). However, the collagen content of meat may differ by muscle type. In this experiment, it was observed that the dietary protein level did not affect soluble collagen that plays an important role in the toughness of the meat, which is inconsistent with
Moon (2006) who found that the tender muscle had a lower total collagen content and lower shear force in beef. Therefore, the softness of meat in this study is likely due to differences in fat contents of the muscles. On considering the protein level in the diet, the group fed with low protein had a high fat content in meat and this made the meat more tender. Aside from the collagen content, intramuscular fat can play an important role in the meat tenderness
(Nishimura et al., 1999).