RESUMEN
The purpose of this study was to compare postmortem calpain changes in porcine muscle between Lanyu native (n = 10) and Kaohsiung crossbred (50% Meishan and 50% Duroc, n = 10) black pigs. Longissimus dorsi (LM) muscles (4th to 10th ribs) from both sides of carcasses were hot-sectioned in 30 min postmortem, vacuum-packaged, and stored at 5°C. LM samples from the left side of carcasses were sampled at 0 (30 min postmortem), 3, 6, 12, 24, 48, and 72 h of storage. The 24 and 72 h samples of shear force measurement were taken from the LM at the 8th and 10th ribs of the right side of carcasses, respectively. Our results showed that the decreases in calpain-1 activity, desmin content, and shear force were slower (P < 0.05) in Lanyu native black pig than in Kaohsiung crossbred black pig samples. Therefore, postmortem proteolysis and tenderization were more limited in LM from Lanyu native pigs than from Kaohsiung crossbred pigs.
Asunto(s)
Calpaína , Enfermedades de los Porcinos , Animales , Porcinos , Calpaína/metabolismo , Carne/análisis , Cambios Post Mortem , Músculo Esquelético/metabolismo , Proteolisis , Enfermedades de los Porcinos/metabolismoRESUMEN
White Roman goose (12-wk-old male, N = 30) carcasses were obtained from a local government-inspected slaughter plant at approximately â¼10-min postmortem. Each carcass was individually sealed in a zip-lock bag and chilled immediately in a water bath at 15°C for 1 h. Both sides of Pectoralis major muscles were excised from each carcass and incubated in 30 mM CaCl2 or 30 mM EDTA at 15°C for 5 h. After incubation, calcium-incubated and EDTA-incubated breast muscles were vacuum-packaged individually and stored at 5°C for 72 h. Control samples (without CaCl2 or EDTA incubation) were directly vacuum-packaged and chilled in a water bath at 15°C for 5 h and stored at 5°C for 72 h. Muscle specimens were taken from the left side of breast muscles at 1 h of chilling (â¼1-h postmortem) and at 5 h of incubation at 15°C (â¼6-h postmortem), as well as 24, 48, and 72 h of aging at 5°C for measuring the activities of calpain-1 and calpain-11 as well as the contents of 80 kDa calpain-1 subunit and desmin. The samples of shear force value and myofibril fragmentation index (MFI) were taken from the right side of breast muscle at 24 h and 72 h of 5°C storage. Our results showed that the decrease of the activities of calpain-1 and calpain-11 and the contents of 80 kDa calpain-1 subunit and desmin was more rapid (P < 0.05) in calcium-incubated samples than in control and EDTA-incubated samples. The shear force was lower, but the MFI was higher in calcium-incubated samples than in control and EDTA-incubated samples (P < 0.05). Therefore, our results suggest that the calpain-mediated proteolysis and tenderization in postmortem goose muscle could be greatly enhanced by combine effects of stepwise chilling with calcium incubation at 15°C and thereafter aging at 5°C. With applying this procedure, commercial slaughter plants may have an alternative way to improve the tenderness of goose meat.
Asunto(s)
Calpaína , Gansos , Animales , Proteolisis , Calpaína/metabolismo , Gansos/metabolismo , Calcio/metabolismo , Músculo Esquelético/fisiología , Ácido Edético/farmacología , Ácido Edético/metabolismo , Cloruro de Calcio/metabolismo , Desmina/metabolismo , Cambios Post Mortem , Pollos/metabolismo , Calcio de la Dieta/metabolismo , Carne/análisis , Agua/metabolismoRESUMEN
Meat tenderness is considered as the most important criterion for meat quality by consumers and can be improved by the actions of endogenous proteases, mainly calpains, during postmortem storage at 0-5°C. The purpose of this study, therefore, was to examine the postmortem calpain activation and proteolysis in breast (BM) and leg and thigh (LM) muscles of White Roman goose. BM and LM were taken from goose carcasses (n = 15) at 0 (10-15 min postmortem), 1, 3, and 7 days of storage at 5°C. The decrease in postmortem pH, calpain-1 and -11 activities, and contents of the calpain-1 80 kDa subunit and desmin was more rapid (p < .05) in BM than in LM. Our results show that postmortem proteolysis was more extensive in BM than in LM of White Roman goose, not only because the difference in fiber type composition between two muscles, but because the rate and extent of calpain activation were greater in BM as well. These results may provide useful information to optimize meat processing for different muscles in goose industry.
Asunto(s)
Calpaína/metabolismo , Calidad de los Alimentos , Gansos , Carne , Músculo Esquelético/metabolismo , Proteolisis , Animales , Calpaína/análisis , Frío , Manipulación de Alimentos , Almacenamiento de Alimentos/métodos , Concentración de Iones de Hidrógeno , Carne/análisis , Cambios Post Mortem , Factores de TiempoRESUMEN
The purpose of this study was to compare postmortem proteolysis and tenderization between Chinese and Wuzong goose breast muscles. Four months old Chinese (CG, n = 15) and Wuzong (WZ, n = 15) goose carcasses were vacuum-packaged 10 to 15 min postmortem and stored at 5°C. Breast (Pectoralis major) samples from each carcass were sampled at 0 (â¼10 min postmortem), 1, 3, and 7 D of storage. Our results showed that the decrease in pH and calpain-1 activity was not different in CG and WG samples. However, the decrease in calpain-11 activity, desmin content, and shear force were more rapid (P < 0.05) in WZ than in CG samples. Our results indicate that postmortem proteolysis and tenderization of goose breast muscle were more extensive in WZ than in CG goose muscle.
Asunto(s)
Calpaína/química , Carne/normas , Músculo Esquelético/química , Cambios Post Mortem , Animales , Anseriformes , Calpaína/metabolismoRESUMEN
Meat tenderization can be affected by a variety of factors including animal age. However, results obtained from goose, chicken, turkey, and ostrich studies have shown that the effects of age on meat tenderization were insignificant, which may be due to a very limited age difference in birds used in those studies. Therefore, the purpose of this study was to investigate the effects of animal age on postmortem proteolysis and tenderization of breast muscle from developing and mature White Roman geese. Goose carcasses from mature (50 mo old, n = 10) and young (3 mo old, n = 10) geese were vacuum-packaged and stored at 5°C within 10 min postmortem. Breast (pectoralis major) samples were taken at 0 (â¼10 min postmortem), 1, 3, and 7 D of storage. Our results showed that the decrease in pH, calpain-1 and -11 activities, desmin content and shear force, as well as the increase in myofibrillar fragmentation index were more rapid (P < 0.05) in young than in mature goose breast. These results suggest that postmortem proteolysis and tenderization of goose muscle are extensively affected by age.
Asunto(s)
Calpaína/metabolismo , Gansos/fisiología , Músculo Esquelético/fisiología , Factores de Edad , Animales , Masculino , Carne/análisis , Cambios Post Mortem , ProteolisisRESUMEN
The postmortem calpain-11 role in ostrich muscle was investigated. Pairs of ostrich muscle (Iliotibialis cranialis) were excised from 32 ostrich carcasses in 3-h postmortem and randomly assigned into four treatments. The muscle was cut into 2.5-cm thick meat cores. The cores were incubated in 30â¯mM CaCl2, 30â¯mM EDTA, 90â¯mM NaCl, or control. The cores from the left-side carcasses were sampled after 0, 1, 2, and 3â¯days of incubation at 5⯰C, while the right-side meat cores were taken at 1-day and 3-day incubation for shear force measurements. The results showed that the decrease in unautolyzed and total activities of calpain-11, desmin content and shear force was more rapid in CaCl2-incubated samples than in control, NaCl- and EDTA-incubated samples. Thus, present results suggest that in the absence of calpain-1, calpain-11 with an extensive activation by adding exogenous Ca2+ could enhance the postmortem proteolysis and tenderization of ostrich muscle.
Asunto(s)
Proteínas Aviares/metabolismo , Calpaína/metabolismo , Almacenamiento de Alimentos , Carne/análisis , Músculo Esquelético/química , Animales , Proteínas Aviares/antagonistas & inhibidores , Quelantes del Calcio/farmacología , Cloruro de Calcio/química , Calpaína/antagonistas & inhibidores , Desmina/metabolismo , Ácido Edético/farmacología , Activación Enzimática/efectos de los fármacos , Inhibidores Enzimáticos/farmacología , Aditivos Alimentarios/química , Aditivos Alimentarios/farmacología , Isoenzimas/antagonistas & inhibidores , Isoenzimas/metabolismo , Músculo Esquelético/efectos de los fármacos , Músculo Esquelético/metabolismo , Cambios Post Mortem , Proteolisis/efectos de los fármacos , Refrigeración , Resistencia al Corte , Struthioniformes , TaiwánRESUMEN
The objective of this study was to study the postmortem calpain change in ostrich muscle. Iliotibialis cranialis and Obturatorius medialis muscles were removed from the both sides of carcasses (n=8). The muscles from the left side were sampled after 0, 1, 2, 3, and 7days of storage at 5°C, while the right-side muscles were taken at 1-, 3-, and 7-day postmortem for shear force measurements. The results showed that the calpain-1 activity was not detected in ostrich muscle during the entire 7-day postmortem storage period, while the calpain-11 was. The unautolyzed calpain-11 activity decreased and the autolyzed calpain-11 activity increased with time postmortem. Desmin content and shear force did not change during postmortem storage although a minor degradation of desmin was observed. Therefore, our results suggest that limited postmortem proteolysis (as suggested by the limited degradation of desmin) and tenderization might be due to the lack of calpain-1 and/or insufficient calpain-11 activity present in ostrich muscle.
Asunto(s)
Calpaína/química , Cambios Post Mortem , Struthioniformes/fisiología , Animales , Calpaína/clasificación , Calpaína/fisiología , Desmina/química , Desmina/metabolismo , Músculo Esquelético/metabolismoRESUMEN
Postmortem changes in proteins that have been implicated in affecting muscle integrity were examined in goose (GG) and duck (DG) gizzard smooth muscle stored at 5°C. GG and DG smooth muscles were sampled at 0, 1, 3 and 7 day of storage. The pH was approximately 7 in both GG and DG samples during postmortem storage. Casein zymograms showed that 0-day µ-calpain activity was higher (p<0.05) in GG than in DG samples. As postmortem time progressed, µ-calpain was activated and autolyzed more extensively in GG than in DG samples. However, µ/m-calpain remained relatively stable in both samples. Western blots indicated that postmortem desmin degradation was more rapid in GG than in DG samples. In contrast, α-actinin remained nearly unchanged in both samples. Therefore, our results suggest that µ-calpain has an important role in the postmortem proteolysis of gizzard smooth muscle.
Asunto(s)
Proteínas Aviares/metabolismo , Calpaína/metabolismo , Patos/metabolismo , Gansos/metabolismo , Molleja de las Aves/metabolismo , Músculo Liso/enzimología , Actinina/metabolismo , Animales , Desmina/metabolismo , Concentración de Iones de Hidrógeno , Músculo Liso/química , Cambios Post Mortem , ProteolisisRESUMEN
BACKGROUND: It is generally agreed that calpains are involved in postmortem proteolysis of skeletal muscle and improve meat tenderness. However, little information regarding the postmortem role of calpains in duck skeletal muscle is known. Therefore, the purpose of this study was to examine the role of calpains in Pekin duck postmortem breast muscles (BM) and leg and thigh muscles (LM) muscles at 5 °C. RESULTS: The postmortem pH was lower (P < 0.05) in BM than in LM. Western blots indicated that postmortem desmin degradation and the 30/32 kDa troponin-T degradation product accumulation were more rapid in BM than in LM. Casein zymograms showed that at-death µ-calpain activity was higher in BM than in LM. As time post mortem increased, µ-calpain was activated and autolyzed more rapidly and extensively in BM than in LM, but µ/m-calpain was activated at a relative slower rate compared with µ-calpain. Correlation results showed that µ-calpain activity, rather than µ/m-calpain activity, in BM samples was highly correlated with the abundance of desmin and the 30/32 kDa troponin-T degradation components across the postmortem period. However, no such correlations were found with LM µ- and µ/m-calpains. CONCLUSION: Therefore, our results suggest that BM µ-calpain with a faster and more extensive activation and autolysis would play a relatively dominant role in dictating degradation of desmin and troponin-T in postmortem duck muscle.
Asunto(s)
Calpaína/metabolismo , Desmina/metabolismo , Carne/análisis , Músculo Esquelético/metabolismo , Cambios Post Mortem , Troponina T/metabolismo , Animales , Mama , Patos , Concentración de Iones de Hidrógeno , Extremidad Inferior , ProteolisisRESUMEN
BACKGROUND: Several studies have reported that the postmortem changes are more rapid in breast muscles (BM) than in leg and thigh muscles (LM) of chickens. However, the reasons for the differences in postmortem proteolysis of BM and LM are still uncertain. The purpose of this study was therefore to compare the postmortem degradation of desmin and calpains in BM and LM from Taiwan black-feathered country chickens at 5 °C. RESULTS: The pH was lower (P < 0.05) in BM than in LM. Western blot indicated that postmortem desmin degradation was more rapid in BM than in LM. Casein zymograms showed that at-death µ-calpain activity was higher in BM than in LM. As postmortem time proceeded, µ-calpain was activated and autolyzed more extensively in BM than in LM. However, the µ/m-calpain activity remained stable during postmortem storage in both BM and LM. CONCLUSION: Our results suggest that the more rapid postmortem proteolysis found in BM than in LM at 5 °C similar with the previous study could be mainly explained by both greater amounts and faster activation and autolysis of µ-calpain in BM.