The experiment was conducted to determine the effect of temperature and time during heat treament on the activity of µ- and m-calpain and cathepsin B + L. In addition the degradation of the structural protein desmin was studied. Porcine longissimus muscle was sampled at 24 hours postmortem and incubated at temperatures of 25, 40, 55 and 70°C for the next 24 hours. At 25°C µ-calpain lost most of its extractable activity within the first 3 hours, whereas m-calpain was more stable. At 40 °C m-calpain activity disappeared within 3 hours. At 55°C µ-and m-calpain was rapidly inactivated, whereas cathepsin B + L was remained active throughout the heat treatment up to 24 hours. At 70°C calpains were inactivated within 10 minutes, cathepsin B + L within 90 minutes and desmin was not degraded. Desmin was degraded more rapidly at 40°C than at 25°C, whereas less degradation occurred at 55 °C. In conclusion, the data suggests that meat proteolysis is accelerated during the initial stages of cooking. Calpains were active for 1 to 3 hours at 40°C. Cathepsin B and L remained active at 55°C, but only around 1 hour at 70°C.
|Titel på gästpublikation||Proceedings 58th International Congress on Meat Science and Technology|
|Status||Publicerad - 2012|
|MoE-publikationstyp||A4 Artikel i en konferenspublikation|
|Evenemang||International Congress of Meat Science and Technology - Montreal, Kanada|
Varaktighet: 12 aug 2012 → 17 aug 2012
- 416 Livsmedelsvetenskap
Citera det här
Ertbjerg, P., Christiansen, L., Pedersen, A., & Kristensen, L. (2012). The effect of temperature and time on activity of calpains and lysosomal enzymes and degradation of desmin in porcine longissimus muscle. I Proceedings 58th International Congress on Meat Science and Technology (s. Paper 358). Montreal: IcoMST.