Myosin heavy chain isoform expression and meat quality characteristics of different muscles in yak (Bos grunniens).

Myosin heavy chain (MHC) isoforms and meat quality characteristics of different muscles were investigated to explore their potential relationships in yaks. Results showed that semitendinosus (ST), longissimus thoracis (LT), and infraspinatus (IS) have a greater ratio of MHC IIb (47.84%), MHC IIa (73.27%), and MHC I (24.26%), respectively, than the other two muscles. Compared with LT or ST, IS exhibited more intense color, greater water-holding capacity, and initial tenderness with higher intermuscular fat (IMF) and collagen (of lower cross-linking level), presenting overall better quality. Variations in MHC isoforms accounted for the muscle-specific meat quality. Specifically, MHC I was positively associated with redness, myoglobin, IMF, collagen, pH, and thermal stability and negatively associated with myofibril fragmentation index, fiber thickness, collagen cross-linking, and drip loss. These results provide insights into the relationships between MHC isoforms and meat quality in yaks and the MHC I isoform has an extensive influence on meat quality.

Effect of slaughter age and postmortem aging time on tenderness and water-holding capacity of yak (Bos grunniens) longissimus thoracis muscle.

The present study investigated the effect of slaughter age (2.43 ± 0.20, 4.15 ± 0.19, 6.62 ± 0.18, 10.59 ± 0.74 years) and postmortem aging time (1, 24, and 72 h) on the tenderness and water-holding capacity (WHC) of yak longissimus thoracis muscles to determine the most suitable age for slaughter to ensure product consistency. Under conventional postmortem aging conditions (4 °C), muscles of each age group exhibited the effect of cold shortening. Once the cold shortening occurred, the age effect on thickening muscle fiber and developing cross-links of collagen, considered to intensify the meat toughness, became less important. Owing to greater carcass weight and intramuscular fat, muscles of the older carcass (over 6-year-old) were less influenced by the cold shortening effect during the chilling process and showed lessened sarcomere contraction, delayed formation of drip loss channels, and increased level of myofibril fragmentation index (MFI) and myofiber structural disintegration, resulting in greater tenderness and WHC, especially 6-7 years group. Aging of 72 h structurally disintegrated the collagen cross-linking and integrity of muscle fibers and elevated the MFI, improving the meat tenderness. Therefore, the suitable slaughter age for yak is 6-7 years old and after 72 h aging, improved quality of yak meat can be obtained.

Muscle fiber composition affects the postmortem redox characteristics of yak beef.

Yak infraspinatus (IS), longissimus thoracis (LT), and semitendinosus (ST) muscles were used to explore relationships between myofiber types and postmortem redox characteristics. IS mainly consisted of myofiber type Ⅰ (49.2%), LT has a vast majority of type IIa (72.7%), while ST possessed a similar percentage of type IIa (44.7%) and IIb (51.5%). Compared with LT and ST, IS exhibited higher initial H2O2, myoglobin (T-Mb), and metmyoglobin (MetMb) contents that provoked severe protein oxidation despite higher endogenous antioxidative capacity (e.g., glutathione antioxidative system). Three muscles showed specificities in myofiber type composition and redox characteristics, which were strongly correlated. Specifically, type Ⅰ myofiber positively correlated with H2O2, T-Mb, and multiple antioxidase activity/content while negatively correlated with lipid peroxidation, MetMb, and lactic dehydrogenase activity; also, they tended to employ more SFAs in more intermuscular fat assembly. Overall, muscle-specific myofiber type/redox attributes required differentiated processing to prevent meat oxidation and produce standardized products.

Effects of NaCl-assisted regulation on the emulsifying properties of heat-induced type I collagen.

Although collagen is widely used as an emulsifier in the food industry, its emulsifying properties are strongly influenced by processing conditions. This research investigated the effects of NaCl on the emulsifying properties of type I collagen after heating. Before heating, the solubility, emulsifying activity index (EAI), emulsifying stability index (ESI), and viscosity of type I collagen initially increased after adding NaCl (0.2 M), after which decreased with increasing NaCl concentration (0.4 M and 0.6 M) due to salt-in effect and the salt-out effects of the protein. While after heating (90℃, 30 min), the collagen became more soluble, with improved EAI and ESI, viscosity, and reduced particle size in response to increasing NaCl concentrations. It was found that NaCl increased the EAI of type I collagen twice after heating, and the EAI reached its maximum at 0.6 M NaCl concentration. We concluded that the improved emulsifying properties may due to thermal denaturation of the protein, resulting in an unfolded and disordered structure with increase of hydrogen bonds with water, rupture of disulfide bonds, and exposure of hydrophobic groups, leading to the increase of adsorption at the oil/water interface. Meanwhile, the Raman spectra analysis and Atomic Force Microscope (AFM) images showed that unfolding of the collagen triple helix was gradually destroyed after NaCl addition and heating, with emulsifying properties improved. The specific outcomes of present study can be adapted towards the requirements to improve the quality of emulsified meat products in the food industry.

The effect of shower time, electrolyte treatment, and electrical stimulation on meat quality of cattle longissimus thoracis muscle in cold weather.

The effects of three treatments (two levels each), namely shower time (ST), electrolyte treatment (ET), and electrical stimulation (ES), on meat quality were investigated using 112 cattle which were randomly allocated to different combinations of each treatment level. ST2, compared with ST1, increased ultimate pH from 6.05 to 6.23 and blood adrenaline levels while deteriorating beef color. ST2 also improved the water-holding capacity (WHC), exhibiting more immobilized water and less free water. Finally, it promoted protein unfolding and the conversion of α-helix to random coil, thus producing tenderer beef. In contrast, results indicated that ET either decreased pHu in ST1 groups or relieved pre-slaughter stress in ST2 groups. ES accelerated pH1 drop with maximum efficiency in an ST1-ET combination, but it did not alter pHu. In addition, ES decreased WHC with an enlarged relaxation time for bound water while causing beef tenderization through protein unfolding. ST1-ET(-ES/NES) maximized pHu reduction and provided an alternative for dark-cutting prevention in cold weather.

Age-specific effect on endogenous oxidative and antioxidative characteristics of longissimus thoracis muscle of yak during early postmortem period.

Effects of age on postmortem redox states were investigated in yak muscles. Extended postmortem time reduced the muscle antioxidant capacity and induced oxidation in lipids, myoglobin, and proteins. Compared with older yaks, muscles of younger ones could delay this oxidation process due to lower initial myoglobin content of 30.7%, lipid peroxidation of 42.4%, H2O2 of 41.2%, and intramuscular fat of 65.6% (of 3.66 times higher PUFAs). They also possessed greater antioxidase content/activity, such as phospholipase A2 content of 30.7% and glutathione reductase activity of 50.6%. Muscles exhibited age-specific overall antioxidative characteristics during 72 h postmortem and gradually formed overall oxidative ones after 72 h postmortem with an initial similarity between 2- and 4-year (or 6- and 12-year) on canonical discriminant analyses. The formation of age-specific overall oxidative characteristics can be attributable to the antioxidative specificity of age on canonical correlation analyses. Age-specific redox characteristics required differentiated preference in meat processing and preservation.