Activity of porcine muscle glycogen debranching enzyme in relation to pH and temperature

Abstract

The activity of glycogen debranching enzyme (GDE) was studied in relation to pH value and temperature in porcine masseter and longissimus dorsi muscles. A glycogen limit dextrin was used as the substrate for GDE, and the enzyme was derived from raw meat extracts. In both muscles, the pH only weakly affected on activity of GDE at the pH values found in carcasses post-slaughter. However, the activity of GDE decreased strongly (P < 0.001) when the temperature decreased from values of 39 °C and 42 °C found just after slaughter to values of 4 °C and 15 °C found during cooling. In both muscles the activity of GDE began to fall at temperatures below 39 °C and was almost zero when the temperature decreased to below 15 °C. Thus, the activity of GDE may control the rate of glycogenolysis and glycolysis, but does not block rapid glycolysis and pH decrease when the temperature is high. This may be important in PSE meat, where the pH decreases rapidly at high temperatures, but rapid cooling could limit the activity of GDE and thus glycogenolysis. As expected, GDE was more active in the light longissimus dorsi muscle than in the dark masseter muscle