The effect of temperature and time on activity of calpains and lysosomal enzymes and degradation of desmin in porcine longissimus muscle

Per Ertbjerg, Liv Christiansen, Anders Pedersen, Lars Kristensen

Forskningsoutput: Kapitel i bok/rapport/konferenshandlingKonferensbidragVetenskapligPeer review


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 gästpublikationProceedings 58th International Congress on Meat Science and Technology
Antal sidor4
SidorPaper 358
ISBN (elektroniskt)978-0-9810463-6-5
StatusPublicerad - 2012
MoE-publikationstypA4 Artikel i en konferenspublikation
EvenemangInternational Congress of Meat Science and Technology - Montreal, Kanada
Varaktighet: 12 aug 201217 aug 2012
Konferensnummer: 58


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