Abstract
This trial aimed to assess the qualitative traits of five muscles of 14 Nellore bulls with 450 kg ± 30.7 kg BW, feedlot fed for 60 days. After slaughter and carcass chilling, samples of the Biceps femoris (BF), Longissimus (LD), Gluteus medius (GM), Semitendinosus (ST) and Trapezius thoracis (TT) muscles were collected, vacuum-packed and aged at 0 to 2 oC for 1, 7 and 14 days and subsequently stored at -20oC for chemical and quality analysis. The pH, shear force, water holding capacity, cooking losses, meat color and ether extract were evaluated in all aging times. Data were analyzed in a split-plot design using the PROC MIXED procedure of SAS. Aging affected quality traits and chemical properties of the meat, improving aspects, such as tenderness (p < 0.01) and lightness (p < 0.01). The Trapezius thoracis muscle has a higher color stability compared with the Longissimus muscle. Aging is not recommended for the ST muscle because the tenderness is not improved. The GM and BF muscles are tender on the first day, and the aging process is indicated for these cuts for adding value to the beef.
Highlights
Tenderness has been considered a major contributor to eating experience in beef (Guerrero, Valero, Campo & Sañudo, 2013; Miller, Carr, Ramsey, Crockett & Hoover, 2001)
No interactions were detected between aging times and muscles (Table 2) for pH, L* and ether extract (EE); the results were discussed separately
The aging reduced the pH values in relation to the beef evaluated at the time 1, where in the pH dropped on day 7 (5.2) and increased again on day 14 (5.7), but with a lower value in relation to day 1 (5.7)
Summary
Tenderness has been considered a major contributor to eating experience in beef (Guerrero, Valero, Campo & Sañudo, 2013; Miller, Carr, Ramsey, Crockett & Hoover, 2001). Animal Sciences contraction state, degradation of the myofibril, intramuscular fat and diameter of muscle fibers. This affects the meat tenderness directly and indirectly. Some muscles have a greater physical activity than others, and, as a consequence, they have a large proportion of red fibers among the white fibers (Kirchofer, Calkins & Gwartne, 2002). Myoglobin stores and transports oxygen in the muscles, such that the concentration of myoglobin increases as the oxygen requirement of the muscle is increased, and the levels of these pigments are higher in the most active muscles (Mancini & Hunt, 2005)
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