RESUMEN
The aim of this study was to determine the impact of accelerated aging (AA) on shelf stability, product loss, sensory and biochemical characteristics of 2 lower quality beef cuts. Triceps brachii (TB) and semimembranosus (SM) were collected and fabricated from 10 USDA Choice beef carcasses and assigned to 1 of 6 treatments: 3 d cooler aged (control), 21 d cooler aged, AA 49 °C for 2 h, AA 49 °C for 3 h, AA 54 °C for 2 h, and AA 54 °C for 3 h. The results showed that AA can decrease APC counts on steak surface and in purge and redness, but increase lightness and product loss of the steaks (P < 0.01). Lower shear force was also found for AA steaks compared to those from the control (P < 0.01), with the AA 54 °C treatments being comparable to 21 d cooler aging. However, the trained sensory panel determined AA steaks were less juicy and flavorful than those from the control and 21 d cooler aged samples (P < 0.05). There was no off-flavor detected in AA steaks though lipid oxidation was higher in AA samples than those in the control steaks (P < 0.01). The AA treatments stimulated cathepsin activity (P < 0.05), which may have enhanced the solubilization of stromal proteins and led to a different troponin-T degradation pattern compared to those from the 21 d aged samples (P < 0.01). Although AA is an economical and time-efficient method to increase tenderness of lower-quality beef cuts, further research is needed to determine strategies to mitigate the decrease in juiciness from AA treatments.
Asunto(s)
Color , Almacenamiento de Alimentos , Músculo Esquelético , Carne Roja , Gusto , Animales , Carne Roja/análisis , Bovinos , Músculo Esquelético/química , Almacenamiento de Alimentos/métodos , Humanos , Resistencia al Corte , Manipulación de Alimentos/métodos , Catepsinas/metabolismo , MasculinoRESUMEN
Matrix metalloproteinases (MMPs) are responsible for the turnover of intramuscular connective tissue in live animals. We hypothesize that MMPs may play a role in postmortem aging of beef muscles for the degradation of connective tissues. Four different experiments were performed to: 1) characterize MMP activity during postmortem aging of beef; 2) determine if the native beef MMP can contribute to connective tissue degradation in a simulated standard industry postmortem aging condition; 3) explore approaches to improve the native beef MMP activity and 4) characterize MMP activity in beef from cattle supplemented with supranutritional level of Zn. In experiment 1, MMP was active throughout the entire aging periods (3, 21, 42 and 63 d) for beef muscles Longissimus lumborum, Gluteus medius and Gastrocnemius, and the unknown MMP responsible for the collagen degradation was identified as MMP-9 by Western Blot. In experiment 2 and 3, MMP-9 activity was noticeable in the gels after 42 d of storage in the cooler. Moreover, the addition of ZnCl2 in the model system significantly increased MMP-9 activity when compared to the control (P < 0.01). In experiment 4, Longissimus thoracis from animals supplemented with a supranutritional Zn level had increased Zn availability and MMP-9 activity than those from animals fed with a control diet (P < 0.05). Further research is needed better understand MMP-9 mechanism during postmortem aging of meat. With a better understanding of MMP-9 in the aging process, the beef industry can provide better connective tissue management strategies for lower-quality beef cuts.
Asunto(s)
Colágeno , Metaloproteinasa 9 de la Matriz , Bovinos , Animales , Músculos , Envejecimiento , Suplementos DietéticosRESUMEN
The aim of this study was to characterize structural and property modifications of intramuscular connective tissue (IMCT) during extended aging. Longissimus lumborum (LL), Gluteus medius (GM), and Gastrocnemius (GT) muscles were collected from 10 USDA choice carcasses, fabricated and assigned to one of four aging periods: 3, 21, 42, or 63 days (n = 120). As expected, tenderness improved, and IMCT texture weakened after 21 days of postmortem aging (dpm; P < 0.05). In addition, transition temperature of collagen decreased (P < 0.01) after 42 dpm. It is interesting to note the collagen structure was also altered where relative % of γ chain decreased after 42 dpm (P < 0.05), and the α1 chain % increased at 63 days (P < 0.01). Finally, The LL and GT had a decrease in the 75 kDa aggrecan fragments from 3 to 21 to 42 dpm (P < 0.05). This study provided evidence that IMCT weakens during postmortem aging due to the modifications of IMCT components such as collagen and proteoglycan.